Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O08675
|
PAR3_MOUSE
|
MKILILVAAGLLFLPVTVCQSGINVSDNSAKPTLTIKSFNGGPQNTFEEFPLSDIEGWTGATTTIKAECPEDSISTLHVNNATIGYLRSSLSTQVIPAIYILLFVVGVPANIVTLWKLSLRTKSISLVIFHTNLAIADLLFCVTLPFKIAYHLNGNNWVFGEVTCRITTVVFYGNMYCAILILTCMGINRYLATAHPFTYQKLPKRSFSMLMCGMVWVMVFLYMLPFVILKQEYHLVHSEITTCHDVVDACESPSSFRFYYFVSLAFFGFLIPFVIIIFCYTTLIHKLKSKDRIWLGYIKAVLLILVIFTICFAPTNIILVIHHANYYYHNTDSLYFMYLIALCLGSLNSCLDPFLYFVMSKVVDQLNP
| null | null |
blood coagulation [GO:0007596]; G protein-coupled receptor signaling pathway [GO:0007186]; ligand-gated ion channel signaling pathway [GO:1990806]; positive regulation of insulin secretion [GO:0032024]; positive regulation of Rho protein signal transduction [GO:0035025]
|
apical plasma membrane [GO:0016324]; protein-containing complex [GO:0032991]
|
G protein-coupled receptor activity [GO:0004930]; proteinase-activated receptor activity [GO:0001648]; receptor ligand activity [GO:0048018]; thrombin-activated receptor activity [GO:0015057]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
|
PTM: A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.
|
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation.
|
Mus musculus (Mouse)
|
O08677
|
KNG1_MOUSE
|
MKLITTLLLCSGLLLTLTQGEEAQEIDCNDEAVFQAVDFSLKQFNPGVKSGNQYMLHRVIEGTKTDGSPTFYSFKYLIKEGNCSAQSGLAWQDCDFKDAEEAATGECTATVGKRENEFFIVTQTCKIAPSKAPILKAYFPCIGCVHAISTDSPDLEPVLKHSIEHFNNNTDHSHLFTLRKVKSAHRQVVAGLNFDITYTIVQTNCSKERFPSLHGDCVALPNGDDGECRGNLFMDINNKIANFSQSCTLYSGDDLVEALPKPCPGCPRDIPVDSPELKEVLGHSIAQLNAENDHPFYYKIDTVKKATSQVVAGTKYVIEFIARETKCSKESNTELAEDCEIKHLGQSLDCNANVYMRPWENKVVPTVKCQALDMTEMARRPPGFSPFRSVTVQETKEGRTVSPPYIAREQEERDAETEQGPTHGHGWLHEKQIKANKNHRGHKHGHDHGHWSPRRHGLGHGHQKPHGLGHGHQLKLDYLRHQREDGDDHTHTVGHGHGHGHGHGHGHGHGHGHGHGHGHGHGHGKHTNKDKNSVKQTTQRTESLASSSEYSTTSTQMQGRTEGPTLTPPRAQPTVTSSGFQDSDFIEDVVATTPPYDTGAHDDLIPDIHVQPDSLSFKLISDFPEATSPKCPGRPWKPASWEDPNTETTEFSDFDLLDALS
| null | null |
blood coagulation [GO:0007596]; inflammatory response [GO:0006954]; negative regulation of blood coagulation [GO:0030195]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; vasodilation [GO:0042311]
|
blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; perikaryon [GO:0043204]
|
cysteine-type endopeptidase inhibitor activity [GO:0004869]; protease binding [GO:0002020]
|
PF00031;
|
3.10.450.10;
| null |
PTM: Bradykinin is released from kininogen by plasma kallikrein.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P01042}.; PTM: [Bradykinin]: Bradykinin is inactivated by ACE, which removes the dipeptide Arg-Phe from its C-terminus. {ECO:0000250|UniProtKB:P01042}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space.
| null | null | null | null | null |
FUNCTION: Kininogens are inhibitors of thiol proteases. HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes. LMW-kininogen inhibits the aggregation of thrombocytes. LMW-kininogen is in contrast to HMW-kininogen not involved in blood clotting.; FUNCTION: [Bradykinin]: The active peptide bradykinin is a potent vasodilatator that is released from HMW-kininogen shows a variety of physiological effects: (A) influence in smooth muscle contraction, (B) induction of hypotension, (C) natriuresis and diuresis, (D) decrease in blood glucose level, (E) it is a mediator of inflammation and causes (E1) increase in vascular permeability, (E2) stimulation of nociceptors (4E3) release of other mediators of inflammation (e.g. prostaglandins), (F) it has a cardioprotective effect (directly via bradykinin action, indirectly via endothelium-derived relaxing factor action). {ECO:0000250|UniProtKB:P01042}.
|
Mus musculus (Mouse)
|
O08678
|
MARK1_RAT
|
MSARTPLPTVNERDTENHTSVDGYTETHIPPTKSSSRQNIPRCRNSITSATDEQPHIGNYRLQKTIGKGNFAKVKLARHVLTGREVAVKIIDKTQLNPTSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKCIVHRDLKAENLLLDADMNIKIADFGFSNEFTVGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRVPFYMSTDCENLLKKLLVLNPIKRGSLEQIMKDRWMNVGHEEEELKPYSEPELDLNDAKRIDIMVTMGFARDEINDALVSQKYDEVMATYILLGRKPPEFEGGESLSSGNLCQRSRPSSDLNNSTLQSPAHLKVQRSISANQKQRRFSDHAGPSIPPAVSYTKRPQANSVESEQKEEWDKDTARRLGSTTVGSKSEVTASPLVGPDRKKSSAGPSNNVYSGGSMTRRNTYVCERSTDRYAALQNGRDSSLTEMSASSMSSTGSTVASAGPSARPRHQKSMSTSGHPIKVTLPTIKDGSEAYRPGTAQRVPAASPSAHSISASTPDRTRFPRGSSSRSTFHGEQLRERRSAAYSGPPASPSHDTAALAHARRGTSTGIISKITSKFVRRDPSEGEASGRTDTARGSSGEPKDKEEGKEAKPRSLRFTWSMKTTSSMDPNDMVREIRKVLDANTCDYEQRERFLLFCVHGDARQDSLVQWEMEVCKLPRLSLNGVRFKRISGTSIAFKNIASKIANELKL
|
2.7.11.1; 2.7.11.26
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
cytoskeleton organization [GO:0007010]; establishment of mitochondrion localization [GO:0051654]; intracellular signal transduction [GO:0035556]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; negative regulation of gene expression [GO:0010629]; neuron migration [GO:0001764]; positive regulation of gene expression [GO:0010628]; protein phosphorylation [GO:0006468]; regulation of dendrite development [GO:0050773]; regulation of neuron projection development [GO:0010975]; Wnt signaling pathway [GO:0016055]
|
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dendrite [GO:0030425]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; phosphatidic acid binding [GO:0070300]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [GO:0001786]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; tau-protein kinase activity [GO:0050321]
|
PF02149;PF00069;PF00627;
|
1.10.8.10;3.30.310.80;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily
|
PTM: Phosphorylation at Thr-613 by PRKCZ/aPKC in polarized epithelial cells inhibits the kinase activity (By similarity). Phosphorylated at Thr-215 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylation at Thr-215 by TAOK1 activates the kinase activity, leading to phosphorylation and detachment of MAPT/TAU from microtubules. Phosphorylation at Ser-219 by GSK3-beta (GSK3B) inhibits the kinase activity. {ECO:0000250, ECO:0000269|PubMed:14517247, ECO:0000269|PubMed:9108484}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9108484}. Cytoplasm {ECO:0000250|UniProtKB:Q9P0L2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9P0L2}. Note=Appears to localize to an intracellular network.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:9108484}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:9108484}; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-[tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703, Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.26;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase (By similarity). Involved in cell polarity and microtubule dynamics regulation. Phosphorylates DCX, MAP2 and MAP4. Phosphorylates the microtubule-associated protein MAPT/TAU (By similarity). Involved in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3) (PubMed:14517247, PubMed:14741102, PubMed:9108484). {ECO:0000250|UniProtKB:Q9P0L2, ECO:0000269|PubMed:14517247, ECO:0000269|PubMed:14741102, ECO:0000269|PubMed:9108484}.
|
Rattus norvegicus (Rat)
|
O08679
|
MARK2_RAT
|
MSSARTPLPTLNERDTEQPTLGHLDSKPSSKSNMLRGRNSATSADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPYVEPLPDYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGYKSSELEGDTITLKPRPSADLTNSSAPSPSHKVQRSVSANPKQRRSSDQAVPAIPTSNSYSKKTQSNNAENKRPEEETGRKASSTAKVPASPLPGLDRKKTTPTPSTNSVLSTSTNRSRNSPLLDRASLGQASIQNGKDSTAPQRVPVASPSAHNISSSSGAPDRTNFPRGVSSRSTFHAGQLRQVRDQQNLPFGVTPASPSGHSQGRRGASGSIFSKFTSKFVRRNLNEPESKDRVETLRPHVVGGGGTDKEKEEFREAKPRSLRFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHERYMLLCVHGTPGHENFVQWEMEVCKLPRLSLNGVRFKRISGTSMAFKNIASKIANELKL
|
2.7.11.1; 2.7.11.26
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q7KZI7};
|
axon development [GO:0061564]; establishment of cell polarity [GO:0030010]; establishment or maintenance of cell polarity regulating cell shape [GO:0071963]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; intracellular signal transduction [GO:0035556]; microtubule cytoskeleton organization [GO:0000226]; neuron migration [GO:0001764]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of neuron projection development [GO:0010976]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of axonogenesis [GO:0050770]; regulation of cytoskeleton organization [GO:0051493]; regulation of microtubule binding [GO:1904526]; regulation of microtubule cytoskeleton organization [GO:0070507]; regulation of postsynapse organization [GO:0099175]; Wnt signaling pathway [GO:0016055]
|
actin filament [GO:0005884]; basal cortex [GO:0045180]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; microtubule bundle [GO:0097427]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]
|
ATP binding [GO:0005524]; lipid binding [GO:0008289]; magnesium ion binding [GO:0000287]; molecular function activator activity [GO:0140677]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; tau protein binding [GO:0048156]; tau-protein kinase activity [GO:0050321]
|
PF02149;PF00069;PF00627;
|
1.10.8.10;3.30.310.80;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily
|
PTM: Autophosphorylated. Phosphorylated at Thr-208 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylation at Thr-208 by TAOK1 activates the kinase activity, leading to phosphorylation and detachment of MAPT/TAU from microtubules. Phosphorylation at Ser-212 by GSK3-beta (GSK3B) inhibits the kinase activity. Phosphorylation by CaMK1 promotes activity and is required to promote neurite outgrowth. Phosphorylation at Thr-539 by PRKCZ/aPKC in polarized epithelial cells inhibits the kinase activity and promotes binding to 14-3-3 protein YWHAZ, leading to relocation from cell membrane to cytoplasm. {ECO:0000269|PubMed:14517247, ECO:0000269|PubMed:16257959, ECO:0000269|PubMed:16717194, ECO:0000269|PubMed:17442826, ECO:0000269|PubMed:18424437}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14741102}; Peripheral membrane protein {ECO:0000269|PubMed:14741102}. Lateral cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:Q7KZI7}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q7KZI7}. Note=Phosphorylation at Thr-539 by PRKCZ/aPKC and subsequent interaction with 14-3-3 protein YWHAZ promotes relocation from the cell membrane to the cytoplasm. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q7KZI7}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q7KZI7}; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-[tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703, Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.26;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase. Involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4 and RAB11FIP2. Phosphorylates the microtubule-associated protein MAPT/TAU. Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Regulates axogenesis by phosphorylating KIF13B, promoting interaction between KIF13B and 14-3-3 and inhibiting microtubule-dependent accumulation of KIF13B. Also required for neurite outgrowth and establishment of neuronal polarity. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision to build a columnar versus a hepatic epithelial cell apparently by promoting a switch from a direct to a transcytotic mode of apical protein delivery. Essential for the asymmetric development of membrane domains of polarized epithelial cells. {ECO:0000250|UniProtKB:Q7KZI7, ECO:0000269|PubMed:14517247, ECO:0000269|PubMed:14741102, ECO:0000269|PubMed:15466480, ECO:0000269|PubMed:16717194, ECO:0000269|PubMed:18509032}.
|
Rattus norvegicus (Rat)
|
O08680
|
EPHA3_RAT
|
MDCHLSILILFGCCVLSCSRELSPQPSNEVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNSIPLVLGTCKETFNLYYMESDDDHGVKFLEHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGACVALVSVRVYFKKCPFTVKNLAMFPDTVPMDSQSLVEVRGSCVNNSKEEDPPRMYCSTEGEWLVPIGKCTCNAGYEERGFICQACRPGFYKALDGVAKCTKCPPHSSTQEDGSMNCRCENNYFRAEKDPPSMACTRPPSAPRNVISNINETSVILDWSWPLDTGGRKDITFNIICKKCGWNVRQCEPCSPNVRFLPRQLGLTNTTVTVTDLLAHTNYTFEIDAINGVSELSSPPRQFAAVSITTNQAAPSPVMTIKKDRTSRNSISLSWQEPEHPNGIILDYEVKYYEKQEQETSYTILRARGTNVTISSLKPDTTYVFQIRARTAAGYGTNSRKFEFENSPDSFSISGENSHVVMIAISAAVAIIVLTVVTYVLVGRFCGYHKSKHSSDEKRLHFGNGHLRLPGLRTYVDPHTYEDPTQAVHEFAKELDATNIAIDKVVGAGEFGEVCSGRLKLPSKKEISVAIKTLKVGYTEKQRRDFLGEASIMGQFDHPNIIRLEGVVTKSKPVMIVTEYMENGSLDSFLRKHDAQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPVRWTSPEATAYRKFTSASDVWSYGIVLWEVMSYGERPYWEMSNQDVIKAVDEGYRLPLPMDCPAALYQLMLDCWQKDRNNRPKFEQIVSILDKLIRNPGSLKIITSAAARPSNLLLDQSNVDIATFHTTGDWLNGMRTAHCKEIFTGVEYSSCDTIAKISTDDMKKVGVTVVGPQKKIISSIKALETQSKNGPVPV
|
2.7.10.1
| null |
axon guidance [GO:0007411]; cell migration [GO:0016477]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cellular response to retinoic acid [GO:0071300]; endocardial cushion development [GO:0003197]; ephrin receptor signaling pathway [GO:0048013]; fasciculation of motor neuron axon [GO:0097156]; fasciculation of sensory neuron axon [GO:0097155]; fever generation [GO:0001660]; negative regulation of endocytosis [GO:0045806]; negative regulation of neuron projection development [GO:0010977]; phosphorylation [GO:0016310]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein localization to plasma membrane [GO:1903078]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell migration [GO:0030334]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of focal adhesion assembly [GO:0051893]; regulation of GTPase activity [GO:0043087]; regulation of microtubule cytoskeleton organization [GO:0070507]; response to cytokine [GO:0034097]; response to lipopolysaccharide [GO:0032496]; synaptic membrane adhesion [GO:0099560]
|
dendrite [GO:0030425]; early endosome [GO:0005769]; GABA-ergic synapse [GO:0098982]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
|
ATP binding [GO:0005524]; ephrin receptor activity [GO:0005003]; GPI-linked ephrin receptor activity [GO:0005004]; growth factor binding [GO:0019838]; transmembrane-ephrin receptor activity [GO:0005005]
|
PF14575;PF01404;PF07699;PF00041;PF07714;PF07647;
|
2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10;
|
Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily
|
PTM: Autophosphorylates upon activation by EFNA5. Phosphorylation on Tyr-603 mediates interaction with NCK1. Dephosphorylated by PTPN1 (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P29320}; Single-pass type I membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O08686
|
BARX2_MOUSE
|
MHCHAELRLSSPGQLKAARRRYKTFMIDEILSKETCDYFEKLSLYSVCPSLVVRPKPLHSCTGSPSLRAYPLLSVITRQPTVISHLVPTGSGLTPVLTRHPVAAAEAAAAAAETPGGEALASSESETEQPTPRQKKPRRSRTIFTELQLMGLEKKFQKQKYLSTPDRLDLAQSLGLTQLQVKTWYQNRRMKWKKMVLKGGQEAPTKPKGRPKKNSIPTSEEIEAEEKMNSQAQSQELLESSERQEEPCDTQEPKACLVPLEVAEPIHQPQELSEASSEPPPLS
| null | null |
cartilage condensation [GO:0001502]; myotube differentiation [GO:0014902]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; skeletal muscle cell differentiation [GO:0035914]; transcription by RNA polymerase II [GO:0006366]
|
actin cytoskeleton [GO:0015629]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]
|
PF00046;
|
1.10.10.60;
|
BAR homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Transcription factor. Binds optimally to the DNA consensus sequence 5'-YYTAATGRTTTTY-3'. May control the expression of neural adhesion molecules such as L1 or Ng-CAM during embryonic development of both the central and peripherical nervous system. May be involved in controlling adhesive processes in keratinizing epithelia.
|
Mus musculus (Mouse)
|
O08689
|
GDF8_MOUSE
|
MMQKLQMYVYIYLFMLIAAGPVDLNEGSEREENVEKEGLCNACAWRQNTRYSRIEAIKIQILSKLRLETAPNISKDAIRQLLPRAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQADGKPKCCFFKFSSKIQYNKVVKAQLWIYLRPVKTPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMSPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS
| null | null |
cellular response to dexamethasone stimulus [GO:0071549]; cellular response to hypoxia [GO:0071456]; muscle cell cellular homeostasis [GO:0046716]; myoblast migration involved in skeletal muscle regeneration [GO:0014839]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of kinase activity [GO:0033673]; negative regulation of muscle hypertrophy [GO:0014741]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of myoblast proliferation [GO:2000818]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of satellite cell differentiation [GO:1902725]; negative regulation of skeletal muscle satellite cell proliferation [GO:1902723]; negative regulation of skeletal muscle tissue growth [GO:0048632]; ovulation cycle process [GO:0022602]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of macrophage chemotaxis [GO:0010759]; response to electrical stimulus [GO:0051602]; response to estrogen [GO:0043627]; response to ethanol [GO:0045471]; response to gravity [GO:0009629]; response to muscle activity [GO:0014850]; response to testosterone [GO:0033574]; skeletal muscle atrophy [GO:0014732]; skeletal muscle satellite cell differentiation [GO:0014816]; skeletal muscle tissue regeneration [GO:0043403]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102]
|
PF00019;PF00688;
|
2.60.120.970;2.10.90.10;
|
TGF-beta family
|
PTM: Synthesized as large precursor molecule that undergoes proteolytic cleavage to generate an N-terminal propeptide and a disulfide linked C-terminal dimer, which is the biologically active molecule. The circulating form consists of a latent complex of the C-terminal dimer and other proteins, including its propeptide, which maintain the C-terminal dimer in a latent, inactive state. Ligand activation requires additional cleavage of the prodomain by a tolloid-like metalloproteinase (PubMed:14671324). {ECO:0000269|PubMed:14671324}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14671324}.
| null | null | null | null | null |
FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth. {ECO:0000269|PubMed:14671324, ECO:0000269|PubMed:24076600, ECO:0000269|PubMed:9139826}.
|
Mus musculus (Mouse)
|
O08691
|
ARGI2_MOUSE
|
MFLRSSASRLLHGQIPCVLTRSVHSVAIVGAPFSRGQKKLGVEYGPAAIREAGLLKRLSRLGCHLKDFGDLSFTNVPQDDPYNNLVVYPRSVGLANQELAEVVSRAVSGGYSCVTMGGDHSLAIGTIIGHARHRPDLCVIWVDAHADINTPLTTVSGNIHGQPLSFLIKELQDKVPQLPGFSWIKPCLSPPNIVYIGLRDVEPPEHFILKNYDIQYFSMREIDRLGIQKVMEQTFDRLIGKRQRPIHLSFDIDAFDPKLAPATGTPVVGGLTYREGVYITEEIHNTGLLSALDLVEVNPHLATSEEEAKATARLAVDVIASSFGQTREGGHIVYDHLPTPSSPHESENEECVRI
|
3.5.3.1
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00742}; Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00742};
|
adaptive immune response [GO:0002250]; arginine catabolic process to ornithine [GO:0019547]; arginine metabolic process [GO:0006525]; innate immune response [GO:0045087]; negative regulation of activated CD8-positive, alpha-beta T cell apoptotic process [GO:1905403]; negative regulation of CD4-positive, alpha-beta T cell proliferation [GO:2000562]; negative regulation of chemokine (C-C motif) ligand 4 production [GO:0071644]; negative regulation of chemokine (C-C motif) ligand 5 production [GO:0071650]; negative regulation of defense response to bacterium [GO:1900425]; negative regulation of interleukin-13 production [GO:0032696]; negative regulation of interleukin-17 production [GO:0032700]; negative regulation of macrophage inflammatory protein 1 alpha production [GO:0071641]; negative regulation of striated muscle contraction [GO:0045988]; negative regulation of tumor necrosis factor production [GO:0032720]; negative regulation of type 2 immune response [GO:0002829]; positive regulation of cellular senescence [GO:2000774]; regulation of interleukin-1 beta production [GO:0032651]; regulation of L-arginine import across plasma membrane [GO:1905541]; regulation of reactive oxygen species biosynthetic process [GO:1903426]; striated muscle contraction [GO:0006941]; urea cycle [GO:0000050]; ureteric bud development [GO:0001657]
|
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]
|
arginase activity [GO:0004053]; manganese ion binding [GO:0030145]; nitric-oxide synthase binding [GO:0050998]
|
PF00491;
|
3.40.800.10;
|
Arginase family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25009204}.
|
CATALYTIC ACTIVITY: Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911; EC=3.5.3.1; Evidence={ECO:0000250|UniProtKB:P05089};
| null |
PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1. {ECO:0000250|UniProtKB:P05089}.
| null | null |
FUNCTION: May play a role in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailability to nitric oxid synthase (NOS). Arginine metabolism is a critical regulator of innate and adaptive immune responses. Seems to be involved in negative regulation of the survival capacity of activated CD4(+) and CD8(+) T cells (PubMed:25009204, PubMed:27745970). May suppress inflammation-related signaling in asthmatic airway epithelium (PubMed:27214549). May contribute to the immune evasion of H.pylori by restricting M1 macrophage activation and polyamine metabolism (PubMed:27074721). May play a role in promoting prenatal immune suppression (By similarity). Regulates RPS6KB1 signaling, which promotes endothelial cell senescence and inflammation and implicates NOS3/eNOS dysfunction (PubMed:22928666). Can inhibit endothelial autophagy independently of its enzymatic activity implicating mTORC2 signaling (PubMed:25484082). Involved in vascular smooth muscle cell senescence and apoptosis independently of its enzymatic activity (By similarity). {ECO:0000250|UniProtKB:P78540, ECO:0000269|PubMed:22928666, ECO:0000269|PubMed:25009204, ECO:0000269|PubMed:25484082, ECO:0000269|PubMed:27074721, ECO:0000269|PubMed:27214549, ECO:0000269|PubMed:27745970}.
|
Mus musculus (Mouse)
|
O08692
|
NGP_MOUSE
|
MAGLWKTFVLVVALAVVSCEALRQLRYEEIVDRAIEAYNQGRQGRPLFRLLSATPPSSQNPATNIPLQFRIKETECTSTQERQPKDCDFLEDGEERNCTGKFFRRRQSTSLTLTCDRDCSREDTQETSFNDKQDVSEKEKFEDVPPHIRNIYEDAKYDIIGNILKNF
| null | null |
antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response [GO:0045087]; negative regulation of angiogenesis [GO:0016525]; negative regulation of lymphangiogenesis [GO:1901491]
|
cytoplasmic vesicle [GO:0031410]; extracellular space [GO:0005615]
|
cysteine-type endopeptidase inhibitor activity [GO:0004869]; lipopolysaccharide binding [GO:0001530]
|
PF00666;
|
3.10.450.10;
|
Cathelicidin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21518852}. Cytoplasmic granule {ECO:0000269|PubMed:8749713}. Note=Localizes in cytoplasmic granules of neutrophilic precursors (PubMed:8749713). {ECO:0000269|PubMed:21518852, ECO:0000269|PubMed:8749713}.
| null | null | null | null | null |
FUNCTION: Acts as an inhibitor of cathepsin B (CTSB) activity. Plays a role as a negative regulator of tumor vascular development, cell invasion and metastasis. {ECO:0000269|PubMed:21518852}.
|
Mus musculus (Mouse)
|
O08696
|
FOXM1_MOUSE
|
MRTSPRRPLILKRRRLPLPVQNAPSETSEEEAKRSPAQPEPAPAQASQEVAESSSCKFPAGIKIINHPTTPNTQVVAIPSNADIQSIITALTAKGKESGTSGPNRFILISSGGPSSHPSQPQAHSSRDSKRAEVITETLGPKPAAKGVPVPKPPGAPPRQRQESYAGGEAAGCTLDNSLTNIQWLGKMSSDGLGPCSVKQELEEKENCHLEQNRVKVEEPSGVSTSWQDSVSERPPYSYMAMIQFAINSTERKRMTLKDIYTWIEDHFPYFKHIAKPGWKNSIRHNLSLHDMFVRETSANGKVSFWTIHPSANRHLTLDQVFKPLEPGSPQSPEHLESQQKRPNPELHRNVTIKTEIPLGARRKMKPLLPRVSSYLEPIQFPVNQSLVLQPSVKVPFRLAASLMSSELARHSKRVRIAPKVLLSSEGIAPLPATEPPKEEKPLLGGEGLLPLLPIQSIKEEEMQPEEDIAHLERPIKVESPPLEEWPSPCASLKEELSNSWEDSSCSPTPKPKKSYCGLKSPTRCVSEMLVTKRREKREVSRSRRKQHLQPPCLDEPDLFFPEDSSTFRPAVELLAESSEPAPHLSCPQEEGGPFKTPIKETLPVSSTPSKSVLSRDPESWRLTPPAKVGGLDFSPVRTPQGAFGLLPDSLGLMELNTTPLKSGPLFDSPRELLNSEPFDLASDPFGSPPPPHVEGPKPGSPELQIPSLSANRSLTEGLVLDTMNDSLSKILLDISFPGLEEDPLGPDNINWSQFIPELR
| null | null |
cell population proliferation [GO:0008283]; DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator [GO:0006978]; DNA repair [GO:0006281]; G2/M transition of mitotic cell cycle [GO:0000086]; liver development [GO:0001889]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell population proliferation [GO:0042127]; regulation of transcription by RNA polymerase II [GO:0006357]; stem cell proliferation [GO:0072089]; vasculogenesis [GO:0001570]
|
nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]
|
PF00250;
|
1.10.10.10;
| null |
PTM: Phosphorylated in M (mitotic) phase. Phosphorylation by the checkpoint kinase CHEK2 in response to DNA damage increases the FOXM1 protein stability probably stimulating the transcription of genes involved in DNA repair. Phosphorylated by CDK1 in late S and G2 phases, creating docking sites for the POLO box domains of PLK1. Subsequently, PLK1 binds and phosphorylates FOXM1, leading to activation of transcriptional activity and subsequent enhanced expression of key mitotic regulators (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
| null | null | null | null | null |
FUNCTION: Transcription factor regulating the expression of cell cycle genes essential for DNA replication and mitosis (By similarity). Plays a role in the control of cell proliferation (By similarity). Also plays a role in DNA break repair, participating in the DNA damage checkpoint response (PubMed:17101782). Promotes transcription of PHB2 (By similarity). {ECO:0000250|UniProtKB:Q08050, ECO:0000269|PubMed:17101782}.
|
Mus musculus (Mouse)
|
O08697
|
ARL2_RAT
|
MGLLTILKKMKQKERDVRLLMLGLDNAGKTTILKKFNGEDVDTISPTLGFNIKTLEHRGFKLNIWDVGGQKSLRSYWRNYFESTDGLIWVVDSADRQRMQDCQRELQSLLVEERLAGATLLIFANKQDLPGALSCNAIQEALELDSIRSHHWRIQGCSAVTGEDLLPGIDWLLDDISSRVFTAD
| null | null |
acetylcholine transport [GO:0015870]; bicellular tight junction assembly [GO:0070830]; centrosome cycle [GO:0007098]; maintenance of protein location in nucleus [GO:0051457]; negative regulation of GTPase activity [GO:0034260]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of microtubule polymerization [GO:0031116]; protein folding [GO:0006457]; regulation of aerobic respiration [GO:1903715]; regulation of glycolytic process [GO:0006110]; regulation of microtubule polymerization [GO:0031113]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; lateral plasma membrane [GO:0016328]; microtubule cytoskeleton [GO:0015630]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]
|
PF00025;
|
3.40.50.300;
|
Small GTPase superfamily, Arf family
|
PTM: Not N-myristoylated.
|
SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:11809823}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:11809823}. Nucleus {ECO:0000269|PubMed:11809823}. Cytoplasm {ECO:0000269|PubMed:11809823}. Note=The complex formed with ARL2BP, ARL2 and SLC25A6 is expressed in mitochondria. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules. The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Regulates formation of new microtubules and centrosome integrity. Prevents the TBCD-induced microtubule destruction. Participates in association with TBCD, in the disassembly of the apical junction complexes. Antagonizes the effect of TBCD on epithelial cell detachment and tight and adherens junctions disassembly. Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. Component of a regulated secretory pathway involved in Ca(2+)-dependent release of acetylcholine. Required for normal progress through the cell cycle (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O08699
|
PGDH_RAT
|
MHVNGKVALVTGAAQGIGKAFTEALLLHGAKVALVDWNLETGVKCKAALDEQFEPQKTLFIQCDVADQKQLRDTFRKVVDHFGRLDILVNNAGVNNEKNWEQTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINISSIAGLMPVAQQPVYCASKHGIIGFTRSAAMAANLMKSGVRLNVICPGFVKTPILESIEKEENMGQYIEYTDQIKAMMKFYGILDPSAIANGLINLIEDDALNGAIMKITASKGIHFQDYDLFPSFSKAP
|
1.1.1.-; 1.1.1.141; 1.1.1.232
| null |
ductus arteriosus closure [GO:0097070]; female pregnancy [GO:0007565]; kidney development [GO:0001822]; negative regulation of cell cycle [GO:0045786]; ovulation [GO:0030728]; parturition [GO:0007567]; positive regulation of apoptotic process [GO:0043065]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; prostaglandin metabolic process [GO:0006693]; regulation of prostaglandin catabolic process [GO:1905828]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to lipopolysaccharide [GO:0032496]; thrombin-activated receptor signaling pathway [GO:0070493]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]
|
15-hydroxyprostaglandin dehydrogenase (NAD+) activity [GO:0016404]; identical protein binding [GO:0042802]; NAD binding [GO:0051287]; NAD+ binding [GO:0070403]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]; prostaglandin E receptor activity [GO:0004957]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=NAD(+) + prostaglandin E2 = 15-oxoprostaglandin E2 + H(+) + NADH; Xref=Rhea:RHEA:11876, ChEBI:CHEBI:15378, ChEBI:CHEBI:57400, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:606564; EC=1.1.1.141; Evidence={ECO:0000305|PubMed:9099857}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11877; Evidence={ECO:0000305|PubMed:9099857}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + NAD(+) = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H(+) + NADH; Xref=Rhea:RHEA:23260, ChEBI:CHEBI:15378, ChEBI:CHEBI:57409, ChEBI:CHEBI:57410, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.232; Evidence={ECO:0000250|UniProtKB:P15428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23261; Evidence={ECO:0000250|UniProtKB:P15428}; CATALYTIC ACTIVITY: Reaction=(11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate + NAD(+) = 11-oxo-(5Z,8Z,12E,14Z)-eicosatetraenoate + H(+) + NADH; Xref=Rhea:RHEA:48640, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78836, ChEBI:CHEBI:90697; Evidence={ECO:0000250|UniProtKB:P15428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48641; Evidence={ECO:0000250|UniProtKB:P15428}; CATALYTIC ACTIVITY: Reaction=lipoxin A4 + NAD(+) = 15-oxo-(5S,6R)-dihydroxy-(7E,9E,11Z,13E)-eicosatetraenoate + H(+) + NADH; Xref=Rhea:RHEA:41572, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67026, ChEBI:CHEBI:78311; Evidence={ECO:0000250|UniProtKB:P15428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41573; Evidence={ECO:0000250|UniProtKB:P15428}; CATALYTIC ACTIVITY: Reaction=15-oxo-(5S,6R)-dihydroxy-(7E,9E,11Z)-eicosatrienoate + H(+) + NADH = (5S,6R,15S)-trihydroxy-(7E,9E,11Z)-eicosatrienoate + NAD(+); Xref=Rhea:RHEA:41596, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78325, ChEBI:CHEBI:78329; Evidence={ECO:0000250|UniProtKB:P15428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41597; Evidence={ECO:0000250|UniProtKB:P15428}; CATALYTIC ACTIVITY: Reaction=NAD(+) + prostaglandin A1 = 15-oxo-prostaglandin A1 + H(+) + NADH; Xref=Rhea:RHEA:41263, ChEBI:CHEBI:15378, ChEBI:CHEBI:57398, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:85072; Evidence={ECO:0000250|UniProtKB:P15428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41264; Evidence={ECO:0000250|UniProtKB:P15428}; CATALYTIC ACTIVITY: Reaction=NAD(+) + prostaglandin E1 = 15-oxoprostaglandin E1 + H(+) + NADH; Xref=Rhea:RHEA:16477, ChEBI:CHEBI:15378, ChEBI:CHEBI:57397, ChEBI:CHEBI:57401, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P15428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16478; Evidence={ECO:0000250|UniProtKB:P15428}; CATALYTIC ACTIVITY: Reaction=14-hydroxy-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate + NAD(+) = 14-oxo-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate + H(+) + NADH; Xref=Rhea:RHEA:48952, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90866, ChEBI:CHEBI:90867; Evidence={ECO:0000250|UniProtKB:P15428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48953; Evidence={ECO:0000250|UniProtKB:P15428}; CATALYTIC ACTIVITY: Reaction=NAD(+) + resolvin E1 = 18-oxo-resolvin E1 + H(+) + NADH; Xref=Rhea:RHEA:49244, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:91000, ChEBI:CHEBI:91001; Evidence={ECO:0000250|UniProtKB:P15428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49245; Evidence={ECO:0000250|UniProtKB:P15428}; CATALYTIC ACTIVITY: Reaction=NAD(+) + resolvin D1 = 8-oxoresolvin D1 + H(+) + NADH; Xref=Rhea:RHEA:50124, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132079, ChEBI:CHEBI:132080; Evidence={ECO:0000250|UniProtKB:P15428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50125; Evidence={ECO:0000250|UniProtKB:P15428}; CATALYTIC ACTIVITY: Reaction=NAD(+) + resolvin D1 = 17-oxoresolvin D1 + H(+) + NADH; Xref=Rhea:RHEA:50128, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132079, ChEBI:CHEBI:132081; Evidence={ECO:0000250|UniProtKB:P15428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50129; Evidence={ECO:0000250|UniProtKB:P15428}; CATALYTIC ACTIVITY: Reaction=NAD(+) + resolvin D2 = 7-oxoresolvin D2 + H(+) + NADH; Xref=Rhea:RHEA:53584, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:133367, ChEBI:CHEBI:137497; Evidence={ECO:0000250|UniProtKB:P15428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53585; Evidence={ECO:0000250|UniProtKB:P15428}; CATALYTIC ACTIVITY: Reaction=NAD(+) + resolvin D2 = 16-oxoresolvin D2 + H(+) + NADH; Xref=Rhea:RHEA:53588, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:133367, ChEBI:CHEBI:137498; Evidence={ECO:0000250|UniProtKB:P15428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53589; Evidence={ECO:0000250|UniProtKB:P15428};
| null | null | null | null |
FUNCTION: Catalyzes the NAD-dependent dehydrogenation (oxidation) of a broad array of hydroxylated polyunsaturated fatty acids (mainly eicosanoids and docosanoids, including prostaglandins, lipoxins and resolvins), yielding their corresponding keto (oxo) metabolites (By similarity) (PubMed:9099857). Decreases the levels of the pro-proliferative prostaglandins such as prostaglandin E2 (whose activity is increased in cancer because of an increase in the expression of cyclooxygenase 2) and generates oxo-fatty acid products that can profoundly influence cell function by abrogating pro-inflammatory cytokine expression. Converts resolvins E1, D1 and D2 to their oxo products, which represents a mode of resolvin inactivation. Resolvin E1 plays important roles during the resolution phase of acute inflammation, while resolvins D1 and D2 have a unique role in obesity-induced adipose inflammation (By similarity). {ECO:0000250|UniProtKB:P15428, ECO:0000269|PubMed:9099857}.
|
Rattus norvegicus (Rat)
|
O08701
|
ARGI2_RAT
|
MFLRSSVSRLLHGQIPCALTRSVHSVAVVGAPFSRGQKKKGVEYGPAAIREAGLLKRLSMLGCHIKDFGDLSFTNVPKDDPYNNLVVYPRSVGIANQELAEVVSRAVSGGYSCVTLGGDHSLAIGTISGHARHHPDLCVIWVDAHADINTPLTTVSGNIHGQPLSFLIRELQDKVPQLPGFSWIKPCLSPPNLVYIGLRDVEPAEHFILKSFDIQYFSMRDIDRLGIQKVMEQTFDRLIGKRKRPIHLSFDIDAFDPKLAPATGTPVVGGLTYREGLYITEEIHSTGLLSALDLVEVNPHLATSEEEAKATASLAVDVIASSFGQTREGGHIAYDHLPTPSSPHESEKEECVRI
|
3.5.3.1
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00742}; Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00742};
|
adaptive immune response [GO:0002250]; arginine catabolic process to ornithine [GO:0019547]; arginine metabolic process [GO:0006525]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to interleukin-4 [GO:0071353]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to type II interferon [GO:0071346]; lung development [GO:0030324]; maternal process involved in female pregnancy [GO:0060135]; midgut development [GO:0007494]; negative regulation of activated CD8-positive, alpha-beta T cell apoptotic process [GO:1905403]; negative regulation of CD4-positive, alpha-beta T cell proliferation [GO:2000562]; negative regulation of chemokine (C-C motif) ligand 4 production [GO:0071644]; negative regulation of chemokine (C-C motif) ligand 5 production [GO:0071650]; negative regulation of defense response to bacterium [GO:1900425]; negative regulation of interleukin-13 production [GO:0032696]; negative regulation of interleukin-17 production [GO:0032700]; negative regulation of macrophage inflammatory protein 1 alpha production [GO:0071641]; negative regulation of striated muscle contraction [GO:0045988]; negative regulation of tumor necrosis factor production [GO:0032720]; negative regulation of type 2 immune response [GO:0002829]; positive regulation of cellular senescence [GO:2000774]; regulation of interleukin-1 beta production [GO:0032651]; regulation of L-arginine import across plasma membrane [GO:1905541]; regulation of nitric oxide biosynthetic process [GO:0045428]; regulation of reactive oxygen species biosynthetic process [GO:1903426]; response to amine [GO:0014075]; response to amino acid [GO:0043200]; response to axon injury [GO:0048678]; response to cadmium ion [GO:0046686]; response to glucose [GO:0009749]; response to herbicide [GO:0009635]; response to hormone [GO:0009725]; response to hypoxia [GO:0001666]; response to mercury ion [GO:0046689]; response to nutrient [GO:0007584]; response to selenium ion [GO:0010269]; response to vitamin E [GO:0033197]; response to xenobiotic stimulus [GO:0009410]; striated muscle contraction [GO:0006941]; urea cycle [GO:0000050]; ureteric bud development [GO:0001657]
|
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]
|
arginase activity [GO:0004053]; manganese ion binding [GO:0030145]; nitric-oxide synthase binding [GO:0050998]
|
PF00491;
|
3.40.800.10;
|
Arginase family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O08691, ECO:0000250|UniProtKB:P78540}.
|
CATALYTIC ACTIVITY: Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911; EC=3.5.3.1; Evidence={ECO:0000250|UniProtKB:P05089};
| null |
PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1. {ECO:0000250|UniProtKB:P05089}.
| null | null |
FUNCTION: May play a role in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailability to nitric oxid synthase (NOS). Arginine metabolism is a critical regulator of innate and adaptive immune responses. Seems to be involved in negative regulation of the survival capacity of activated T cells. May suppress inflammation-related signaling in asthmatic airway epithelium. May play a role in promoting prenatal immune suppression. Regulates RPS6KB1 signaling, which promotes endothelial cell senescence and inflammation and implicates NOS3/eNOS dysfunction. Can inhibit endothelial autophagy independently of its enzymatic activity implicating mTORC2 signaling. Involved in vascular smooth muscle cell senescence and apoptosis independently of its enzymatic activity. {ECO:0000250|UniProtKB:O08691, ECO:0000250|UniProtKB:P78540}.
|
Rattus norvegicus (Rat)
|
O08705
|
NTCP_MOUSE
|
MEAHNVSAPFNFSLPPGFGHRATDTALSVILVVMLLLIMLSLGCTMEFSKIKAHFWKPKGVIIAIVAQYGIMPLSAFLLGKVFHLTSIEALAILICGCSPGGNLSNLFTLAMKGDMNLSIVMTTCSSFTALGMMPLLLYIYSKGIYDGDLKDKVPYKGIMLSLVMVLIPCAIGIFLKSKRPHYVPYVLKAGMIITFSLSVAVTVLSVINVGNSIMFVMTPHLLATSSLMPFTGFLMGYILSALFRLNPSCRRTISMETGFQNVQLCSTILNVTFPPEVIGPLFFFPLLYMIFQLAEGLLFIIIFRCYLKIKPQKDQTKITYKAAATEDATPAALEKGTHNGNNPPTQPGLSPNGLNSGQMAN
| null | null |
bile acid and bile salt transport [GO:0015721]; bile acid signaling pathway [GO:0038183]; cellular response to xenobiotic stimulus [GO:0071466]; regulation of bile acid secretion [GO:0120188]; response to estrogen [GO:0043627]; response to ethanol [GO:0045471]; response to nutrient levels [GO:0031667]; response to organic cyclic compound [GO:0014070]
|
basolateral plasma membrane [GO:0016323]; membrane [GO:0016020]
|
bile acid transmembrane transporter activity [GO:0015125]; bile acid:sodium symporter activity [GO:0008508]
|
PF01758;
|
1.20.1530.20;
|
Bile acid:sodium symporter (BASS) (TC 2.A.28) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14973}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q14973}.
|
CATALYTIC ACTIVITY: [Isoform 1]: Reaction=2 Na(+)(out) + taurocholate(out) = 2 Na(+)(in) + taurocholate(in); Xref=Rhea:RHEA:71875, ChEBI:CHEBI:29101, ChEBI:CHEBI:36257; Evidence={ECO:0000269|PubMed:10209268}; CATALYTIC ACTIVITY: [Isoform 2]: Reaction=2 Na(+)(out) + taurocholate(out) = 2 Na(+)(in) + taurocholate(in); Xref=Rhea:RHEA:71875, ChEBI:CHEBI:29101, ChEBI:CHEBI:36257; Evidence={ECO:0000269|PubMed:10209268}; CATALYTIC ACTIVITY: Reaction=estrone 3-sulfate(out) + 2 Na(+)(out) = estrone 3-sulfate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71083, ChEBI:CHEBI:29101, ChEBI:CHEBI:60050; Evidence={ECO:0000269|PubMed:34060352}; CATALYTIC ACTIVITY: Reaction=cholate(out) + 2 Na(+)(out) = cholate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71911, ChEBI:CHEBI:29101, ChEBI:CHEBI:29747; Evidence={ECO:0000250|UniProtKB:O97736}; CATALYTIC ACTIVITY: Reaction=2 Na(+)(out) + taurochenodeoxycholate(out) = 2 Na(+)(in) + taurochenodeoxycholate(in); Xref=Rhea:RHEA:71923, ChEBI:CHEBI:9407, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:O97736}; CATALYTIC ACTIVITY: Reaction=2 Na(+)(out) + tauroursodeoxycholate(out) = 2 Na(+)(in) + tauroursodeoxycholate(in); Xref=Rhea:RHEA:71927, ChEBI:CHEBI:29101, ChEBI:CHEBI:132028; Evidence={ECO:0000250|UniProtKB:O97736}; CATALYTIC ACTIVITY: Reaction=glycocholate(out) + 2 Na(+)(out) = glycocholate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71935, ChEBI:CHEBI:29101, ChEBI:CHEBI:29746; Evidence={ECO:0000250|UniProtKB:O97736}; CATALYTIC ACTIVITY: Reaction=2 Na(+)(out) + tauronorcholate(out) = 2 Na(+)(in) + tauronorcholate(in); Xref=Rhea:RHEA:71915, ChEBI:CHEBI:29101, ChEBI:CHEBI:191405; Evidence={ECO:0000250|UniProtKB:O97736}; CATALYTIC ACTIVITY: Reaction=2 Na(+)(out) + taurodeoxycholate(out) = 2 Na(+)(in) + taurodeoxycholate(in); Xref=Rhea:RHEA:72087, ChEBI:CHEBI:29101, ChEBI:CHEBI:36261; Evidence={ECO:0000250|UniProtKB:O97736}; CATALYTIC ACTIVITY: Reaction=2 Na(+)(out) + tauroallocholate(out) = 2 Na(+)(in) + tauroallocholate(in); Xref=Rhea:RHEA:51840, ChEBI:CHEBI:29101, ChEBI:CHEBI:191406; Evidence={ECO:0000250|UniProtKB:O97736}; CATALYTIC ACTIVITY: Reaction=2 Na(+)(out) + taurohyodeoxycholate(out) = 2 Na(+)(in) + taurohyodeoxycholate(in); Xref=Rhea:RHEA:72167, ChEBI:CHEBI:29101, ChEBI:CHEBI:191407; Evidence={ECO:0000250|UniProtKB:O97736}; CATALYTIC ACTIVITY: Reaction=2 Na(+)(out) + taurohyocholate(out) = 2 Na(+)(in) + taurohyocholate(in); Xref=Rhea:RHEA:72171, ChEBI:CHEBI:29101, ChEBI:CHEBI:58874; Evidence={ECO:0000250|UniProtKB:O97736}; CATALYTIC ACTIVITY: Reaction=2 Na(+)(out) + tauro-beta-muricholate(out) = 2 Na(+)(in) + tauro-beta-muricholate(in); Xref=Rhea:RHEA:72179, ChEBI:CHEBI:29101, ChEBI:CHEBI:133064; Evidence={ECO:0000250|UniProtKB:O97736};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=86 uM for taurocholate {ECO:0000269|PubMed:10209268}; KM=104 uM for estrone 3-sulfate {ECO:0000269|PubMed:34060352}; Vmax=3004 pmol/min/mg enzyme with estrone 3-sulfate as substrate {ECO:0000269|PubMed:34060352}; Kinetic parameters: KM=14 uM for taurocholate {ECO:0000269|PubMed:10209268};
| null | null | null |
FUNCTION: As a major transporter of conjugated bile salts from plasma into the hepatocyte, it plays a key role in the enterohepatic circulation of bile salts necessary for the solubilization and absorption of dietary fat and fat-soluble vitamins (PubMed:10209268). It is strictly dependent on the extracellular presence of sodium (PubMed:10209268, PubMed:34060352). It exhibits broad substrate specificity and transports various bile acids, such as taurocholate, cholate, as well as non-bile acid organic compounds, such as estrone sulfate (PubMed:10209268, PubMed:34060352). Works collaboratively with the ileal transporter (NTCP2), the organic solute transporter (OST), and the bile salt export pump (BSEP), to ensure efficacious biological recycling of bile acids during enterohepatic circulation (By similarity). {ECO:0000250|UniProtKB:Q14973, ECO:0000269|PubMed:10209268, ECO:0000269|PubMed:34060352}.
|
Mus musculus (Mouse)
|
O08707
|
ACKR2_MOUSE
|
MPTVASPLPLTTVGSENSSSIYDYDYLDDMTILVCRKDEVLSFGRVFLPVVYSLIFVLGLAGNLLLLVVLLHSAPRRRTMELYLLNLAVSNLLFVVTMPFWAISVAWHWVFGSFLCKVISTLYSINFYCGIFFITCMSLDKYLEIVHAQPLHRPKAQFRNLLLIVMVWITSLAISVPEMVFVQIHQTLDGVWHCYADFGGHATIWKLYLRFQLNLLGFLLPLLAMIFFYSRIGCVLVRLRPPGQGRALRMAAALVIVFFMLWFPYNLTLFLHSLLDLHVFGNCEISHRLDYTLQVTESLAFSHCCFTPVLYAFCSHRFRRYLKAFLSVMLRWHQAPGTPSSNHSESSRVTAQEDVVSMNDLGERQSEDSLNKGEMGNT
| null | null |
calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; immune response [GO:0006955]; inflammatory response [GO:0006954]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; signal transduction [GO:0007165]
|
actin filament [GO:0005884]; cytosol [GO:0005829]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]
|
C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; scavenger receptor activity [GO:0005044]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family, Atypical chemokine receptor subfamily
|
PTM: Phosphorylated on serine residues in the C-terminal cytoplasmic tail. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Cell membrane; Multi-pass membrane protein. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via clathrin-coated pits. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines including CCL2, CCL3, CCL3L1, CCL4, CCL5, CCL7, CCL8, CCL11, CCL13, CCL17, CCL22, CCL23, CCL24, SCYA2/MCP-1, SCY3/MIP-1-alpha, SCYA5/RANTES and SCYA7/MCP-3. Upon active ligand stimulation, activates a beta-arrestin 1 (ARRB1)-dependent, G protein-independent signaling pathway that results in the phosphorylation of the actin-binding protein cofilin (CFL1) through a RAC1-PAK1-LIMK1 signaling pathway. Activation of this pathway results in up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. By scavenging chemokines in tissues, on the surfaces of lymphatic vessels, and in placenta, plays an essential role in the resolution (termination) of the inflammatory response and in the regulation of adaptive immune responses. Plays a major role in the immune silencing of macrophages during the resolution of inflammation. Acts as a regulator of inflammatory leukocyte interactions with lymphatic endothelial cells (LECs) and is required for immature/mature dendritic cells discrimination by LECs. {ECO:0000269|PubMed:22651933}.
|
Mus musculus (Mouse)
|
O08709
|
PRDX6_MOUSE
|
MPGGLLLGDEAPNFEANTTIGRIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFAKRNVKLIALSIDSVEDHLAWSKDINAYNGETPTEKLPFPIIDDKGRDLAILLGMLDPVEKDDNNMPVTARVVFIFGPDKKLKLSILYPATTGRNFDEILRVVDSLQLTGTKPVATPVDWKKGESVMVVPTLSEEEAKQCFPKGVFTKELPSGKKYLRYTPQP
|
1.11.1.27; 2.3.1.23; 3.1.1.4
| null |
bleb assembly [GO:0032060]; cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; hydrogen peroxide catabolic process [GO:0042744]; lipid catabolic process [GO:0016042]; response to reactive oxygen species [GO:0000302]
|
cytosol [GO:0005829]; lysosome [GO:0005764]; mitochondrion [GO:0005739]
|
1-acylglycerophosphocholine O-acyltransferase activity [GO:0047184]; glutathione peroxidase activity [GO:0004602]; peroxidase activity [GO:0004601]; peroxiredoxin activity [GO:0051920]; phospholipase A2 activity [GO:0004623]
|
PF10417;PF00578;
|
3.40.30.10;
|
Peroxiredoxin family, Prx6 subfamily
|
PTM: Irreversibly inactivated by overoxidation of Cys-47 to sulfinic acid (Cys-SO(2)H) and sulfonic acid (Cys-SO(3)H) forms upon oxidative stress. {ECO:0000250|UniProtKB:P30041}.; PTM: Phosphorylation at Thr-177 by MAP kinases increases the phospholipase activity of the enzyme (By similarity). The phosphorylated form exhibits a greater lysophosphatidylcholine acyltransferase activity compared to the non-phosphorylated form (By similarity). {ECO:0000250|UniProtKB:O35244}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35244}. Lysosome {ECO:0000250|UniProtKB:O35244}. Note=Also found in lung secretory organelles (lamellar bodies). {ECO:0000250|UniProtKB:O35244}.
|
CATALYTIC ACTIVITY: Reaction=a hydroperoxide + 2 glutathione = an alcohol + glutathione disulfide + H2O; Xref=Rhea:RHEA:62632, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.27; Evidence={ECO:0000250|UniProtKB:P30041}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:26830860}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937, ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168, ChEBI:CHEBI:58342; EC=2.3.1.23; Evidence={ECO:0000269|PubMed:26830860}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:35983, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P30041}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35984; Evidence={ECO:0000250|UniProtKB:P30041}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P30041}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000250|UniProtKB:P30041};
| null | null | null | null |
FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity). Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (By similarity). Has phospholipase activity (PubMed:26830860). Can either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (By similarity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (By similarity). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (By similarity). Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (PubMed:26830860). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (By similarity). {ECO:0000250|UniProtKB:P30041, ECO:0000269|PubMed:26830860}.
|
Mus musculus (Mouse)
|
O08710
|
THYG_MOUSE
|
MTALVLWVSTLLSSVCLVAANIFEYQVDAQPLRPCELQREKAFLKQAEYVPQCSEDGSFQTVQCQNDGQSCWCVDSDGREVPGSRQLGRPTVCLSFCQLHKQRILLGSYINSTDALYLPQCQDSGNYAPVQCDLQRVQCWCVDTEGMEVYGTRQQGRPTRCPRSCEIRNRRLLHGVGDRSPPQCTADGEFMPVQCKFVNTTDMMIFDLIHNYNRFPDAFVTFSSFRGRFPEVSGYCYCADSQGRELAETGLELLLDEIYDTIFAGLDQASTFTQSTMYRILQRRFLAIQLVISGRFRCPTKCEVEQFAATRFGHSYIPRCHRDGHYQTVQCQTEGMCWCVDAQGREVPGTRQQGQPPSCAADQSCALERQQALSRFYFETPDYFSPQDLLSSEDRLAPVSGVRSDTSCPPRIKELFVDSGLLRSIAVEHYQRLSESRSLLREAIRAVFPSRELAGLALQFTTNPKRLQQNLFGGTFLANAAQFNLSGALGTRSTFNFSQFFQQFGLPGFLNRDRVTTLAKLLPVRLDSSSTPETLRVSEKTVAMNKRVVGNFGFKVNLQENQDALKFLVSLLELPEFLVFLQRAVSVPEDIARDLGDVMEMVFSAQACKQMPGKFFVPSCTAGGSYEDIQCYAGECWCVDSRGKELDGSRVRGGRPRCPTKCEKQRAQMQSLASAQPAGSSFFVPTCTREGYFLPVQCFNSECYCVDTEGQVIPGTQSTVGEAKQCPSVCQLQAEQAFLGVVGVLLSNSSMVPSISNVYIPQCSASGQWRHVQCDGPHEQVFEWYERWKTQNGDGQELTPAALLMKIVSYREVASRNFSLFLQSLYDAGQQRIFPVLAQYPSLQDVPQVVLEGATTPPGENIFLDPYIFWQILNGQLSQYPGPYSDFNMPLEHFNLRSCWCVDEAGQKLDGTQTKPGEIPACPGPCEEVKLRVLKFIKETEEIVSASNASSFPLGESFLVAKGIQLTSEELDLPPQFPSRDAFSEKFLRGGEYAIRLAAQSTLTFYQSLRASLGKSDGAASLLWSGPYMPQCNMIGGWEPVQCHAGTGQCWCVDGRGEFIPGSLMSRSSQMPQCPTNCELSRASGLISAWKQAGPQRNPGPGDLFIPVCLQTGEYVRKQTSGTGTWCVDPASGEGMPVNTNGSAQCPGLCDVLKSRALSRKVGLGYSPVCEALDGAFSPVQCDLAQGSCWCVLGSGEEVPGTRVVGTQPACESPQCPLPFSGSDVADGVIFCETASSSGVTTVQQCQLLCRQGLRSAFSPGPLICSLESQHWVTLPPPRACQRPQLWQTMQTQAHFQLLLPPGKMCSVDYSGLLQAFQVFILDELIARGFCQIQVKTFGTLVSSTVCDNSSIQVGCLTAERLGVNVTWKLQLEDISVGSLPDLYSIERAVTGQDLLGRFADLIQSGRFQLHLDSKTFSADTTLYFLNGDSFVTSPRTQLGCMEGFYRVPTTRQDALGCVKCPEGSFSQDGRCTPCPAGTYQEQAGSSACIPCPRGRTTITTGAFSKTHCVTDCQKNEAGLQCDQNGQYQASQKNRDSGEVFCVDSEGRKLQWLQTEAGLSESQCLMIRKFDKAPESKVIFDANSPVIVKSSVPSADSPLVQCLTDCANDEACSFLTVSTMESEVSCDFYSWTRDNFACVTSDQEQDAMGSLKATSFGSLRCQVKVRNSGKDSLAVYVKKGYESTAAGQKSFEPTGFQNVLSGLYSPVVFSASGANLTDTHTYCLLACDNDSCCDGFIITQVKGGPTICGLLSSPDILLCHINDWRDTSATQANATCAGVTYDQGSRQMTLSLGGQEFLQGLALLEGTQDSFTSFQQVYLWKDSDMGSRPESMGCERGMVPRSDFPGDMATELFSPVDITQVIVNTSHSLPSQQYWLFTHLFSAEQANLWCLSRCAQEPIFCQLADITKSSSLYFTCFLYPEAQVCDNVMESNAKNCSQILPHQPTALFRRKVVLNDRVKNFYTRLPFQKLTGISIRDKVPMSGKLISNGFFECERLCDRDPCCTGFGFLNVSQLQGGEVTCLTLNSMGIQTCNEESGATWRILDCGSEDTEVHTYPFGWYQKPAVWSDTPSFCPSAALQSLTEEKVTSDSWQTLALSSVIVDPSIKHFDVAHISTAATSNFSMAQDFCLQQCSRHQDCLVTTLQIQPGVVRCVFYPDIQNCIHSLRSHTCWLLLHEEATYIYRKSGIPLVQSDVTSTPSVRIDSFGQLQGGSQVIKVGTAWKQVYRFLGVPYAAPPLADNRFRAPEVLNWTGSWDATKPRASCWQPGTRTPTPPQINEDCLYLNVFVPENLVSNASVLVFFHNTMEMEGSGGQLTIDGSILAAVGNFIVVTANYRLGVFGFLSSGSDEVAGNWGLLDQVAALTWVQSHIGAFGGDPQRVTLAADRSGADVASIHLLISRPTRLQLFRKALLMGGSALSPAAIISPERAQQQAAALAKEVGCPTSSIQEVVSCLRQKPANILNDAQTKLLAVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLIGGSQDDGLINRAKAVKQFEESQGRTNSKTAFYQALQNSLGGEDSDARILAAAVWYYSLEHSTDDYASFSRALENATRDYFIICPMVNMASLWARRTRGNVFMYHVPESYGHGSLELLADVQYAFGLPFYSAYQGQFSTEEQSLSLKVMQYFSNFIRSGNPNYPHEFSRKAAEFATPWPDFIPGAGGESYKELSAQLPNRQGLKQADCSFWSKYIQTLKDADGAKDAQLTKSEEEDLEVGPGLEEDLSGSLEPVPKSYSK
| null | null |
hormone biosynthetic process [GO:0042446]; iodide transport [GO:0015705]; regulation of myelination [GO:0031641]; response to pH [GO:0009268]; thyroid gland development [GO:0030878]; thyroid hormone generation [GO:0006590]; thyroid hormone metabolic process [GO:0042403]; transcytosis [GO:0045056]
|
extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]
|
anion binding [GO:0043168]; hormone activity [GO:0005179]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877]; protein-folding chaperone binding [GO:0051087]; signaling receptor binding [GO:0005102]
|
PF00135;PF07699;PF00086;
|
3.40.50.1820;4.10.800.10;2.10.50.10;
|
Type-B carboxylesterase/lipase family
|
PTM: Iodinated on tyrosine residues by TPO (By similarity). There are 4 pairs of iodinated tyrosines used for coupling: acceptor Tyr-25 is coupled to donor Tyr-150 or Tyr-235, acceptor Tyr-2572 is coupled to donor Tyr-2539, acceptor Tyr-2764 in monomer 1 is coupled to donor Tyr-2764 in monomer 2 and acceptor Tyr-1310 in monomer 1 is coupled to donor Tyr-109 in monomer 2 (By similarity). {ECO:0000250|UniProtKB:F1RRV3, ECO:0000250|UniProtKB:P01266}.; PTM: Sulfated tyrosines are desulfated during iodination. {ECO:0000250|UniProtKB:P01266}.; PTM: Undergoes sequential proteolysis by cathepsins to release thyroxine (T4) and triiodothyronine (T3) hormones (PubMed:12782676). In the thyroid follicle lumen, cross-linked TG (storage form) is solubilized by limited proteolysis mediated by cathepsins CTSB and/or CTSL (PubMed:12782676). Partially cleaved TG is further processed by CTSK/cathepsin K and/or CTSL resulting in the release of T4 (PubMed:12782676). Following endocytosis, further processing occurs leading to the release of T3 and more T4 hormones (Probable). {ECO:0000269|PubMed:12782676, ECO:0000305|PubMed:12782676}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12782676, ECO:0000269|PubMed:19276074}. Note=Secreted into the thyroid follicle lumen (PubMed:12782676). Localizes to colloid globules, a structure formed in the thyroid follicle lumen consisting of cross-linked TG arranged in concentric layers (PubMed:12782676). {ECO:0000269|PubMed:12782676}.
| null | null | null | null | null |
FUNCTION: Acts as a substrate for the production of iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3) (By similarity). The synthesis of T3 and T4 involves iodination of selected tyrosine residues of TG/thyroglobulin followed by their oxidative coupling (By similarity). Following TG re-internalization and lysosomal-mediated proteolysis, T3 and T4 are released from the polypeptide backbone leading to their secretion into the bloodstream (Probable). One dimer produces 7 thyroid hormone molecules (By similarity). {ECO:0000250|UniProtKB:F1RRV3, ECO:0000250|UniProtKB:P01266, ECO:0000305|PubMed:12782676}.
|
Mus musculus (Mouse)
|
O08712
|
TR11B_MOUSE
|
MNKWLCCALLVLLDIIEWTTQETLPPKYLHYDPETGHQLLCDKCAPGTYLKQHCTVRRKTLCVPCPDHSYTDSWHTSDECVYCSPVCKELQSVKQECNRTHNRVCECEEGRYLEIEFCLKHRSCPPGSGVVQAGTPERNTVCKKCPDGFFSGETSSKAPCIKHTNCSTFGLLLIQKGNATHDNVCSGNREATQKCGIDVTLCEEAFFRFAVPTKIIPNWLSVLVDSLPGTKVNAESVERIKRRHSSQEQTFQLLKLWKHQNRDQEMVKKIIQDIDLCESSVQRHLGHSNLTTEQLLALMESLPGKKISPEEIERTRKTCKSSEQLLKLLSLWRIKNGDQDTLKGLMYALKHLKTSHFPKTVTHSLRKTMRFLHSFTMYRLYQKLFLEMIGNQVQSVKISCL
| null | null |
apoptotic process [GO:0006915]; extracellular matrix organization [GO:0030198]; negative regulation of bone resorption [GO:0045779]; negative regulation of odontogenesis of dentin-containing tooth [GO:0042489]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; response to arsenic-containing substance [GO:0046685]; response to estrogen [GO:0043627]; response to magnesium ion [GO:0032026]; response to nutrient [GO:0007584]; response to xenobiotic stimulus [GO:0009410]; signal transduction [GO:0007165]
|
extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; receptor complex [GO:0043235]
|
heparan sulfate binding [GO:1904399]
|
PF00531;PF00020;
|
1.10.533.10;2.10.50.10;
| null | null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Acts as a decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis. {ECO:0000269|PubMed:10952716}.
|
Mus musculus (Mouse)
|
O08715
|
AKAP1_MOUSE
|
MAIQLRSLFPLALPGMLALLGWWWFFSRKKDRLSSSDKQVETLKVGPAIKDRRLSEEACPGVLSVAPTVTQPPGREEQRCVDKPSTEPLALPRTRQVRRRSESSGNLPSVADTRSQPGPCRDEIAKVELSLMGDKAKSIPLGCPLLPKDASFPYEAVERCKQESALGKTPGRGWPSPYAASGEKARETGGTEGTGDAVLGENVSEEGLLSQECVSEVEKSEFPILAPGGGEGEEVSHGPPQVAELLKKEEYIVGKLPSSFVEPVHSEPVKDEDALEPQVKGSSNTSDRDLAGELDKDETVPENDQIKQAAFQLISQVILEATEEFRATTVGKTVAQVHPTSATQPKGKEESCVPASQETSLGQDTSDPASTRTGATASPSAEALPPKTYVSCLSSPLSGPTKDQKPKNSAHHISLAPCPPPVTPQRQSLEGASNPRGDDNFVACMANNSQSVLSVSSLGQCSDPVSTSGLEDSCTETISSSGDKAMTPPLPVSTQPFSNGVLKEELSDLGTEDGWTMDTEADHSGGSDGNSMDSVDSCCGLTKPDSPQSVQAGSNPKKVDLIIWEIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYTQNIQICHIEGSQHHVDKALNLIGKKFKELNLTNIYAPPLPSLALPSLPMTSWLMLPDGITVEVIVVNQVNAGHLFVQQHTHPTFHALRSLDQQMYLCYSQPGIPTLPTPVEITVICAAPGADGAWWRAQVVASYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLLDSVVPLSDDDHFSPEADAAMSEMTGNTALLAQVTSYSATGLPLIQLWSVVGDEVVLINRSLVERGLAQWVDSYYASL
| null | null |
antiviral innate immune response [GO:0140374]; apoptotic process [GO:0006915]; negative regulation of cardiac muscle hypertrophy [GO:0010614]; negative regulation of protein dephosphorylation [GO:0035308]; negative regulation of protein import into nucleus [GO:0042308]
|
endoplasmic reticulum [GO:0005783]; lipid droplet [GO:0005811]; membrane [GO:0016020]; mitochondrial crista [GO:0030061]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; neuromuscular junction [GO:0031594]; postsynaptic membrane [GO:0045211]; postsynaptic specialization, intracellular component [GO:0099091]
|
beta-tubulin binding [GO:0048487]; microtubule binding [GO:0008017]; molecular adaptor activity [GO:0060090]; protein kinase A regulatory subunit binding [GO:0034237]; protein kinase binding [GO:0019901]; protein phosphatase 2B binding [GO:0030346]; protein phosphatase binding [GO:0019903]; RNA binding [GO:0003723]
|
PF00013;PF00567;
|
2.30.30.140;2.40.50.90;3.30.1370.10;
| null | null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:24101730, ECO:0000269|PubMed:9182549}. Mitochondrion {ECO:0000269|PubMed:32072193}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum {ECO:0000269|PubMed:10352013}. Note=Does not contain the classic KDEL endoplasmic reticulum-targeting sequence. This explains how it is able to switch its localization, either being in the endoplasmic reticulum or in the mitochondria depending on which N-terminal part begins the isoform. The longest N-terminal part only present in isoform 2 acts as a suppressor of mitochondrial targeting and as an activator of recessive endoplasmic reticulum targeting motif. {ECO:0000269|PubMed:10352013}.; SUBCELLULAR LOCATION: [Isoform 4]: Endoplasmic reticulum {ECO:0000269|PubMed:10352013}. Note=Does not contain the classic KDEL endoplasmic reticulum-targeting sequence. This explains how it is able to switch its localization, either being in the endoplasmic reticulum or in the mitochondria depending on which N-terminal part begins the isoform. The longest N-terminal part only present in isoform 4 acts as a suppressor of mitochondrial targeting and as an activator of recessive endoplasmic reticulum targeting motif. {ECO:0000269|PubMed:10352013}.; SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion outer membrane {ECO:0000269|PubMed:10352013}. Note=Does not contain the classic KDEL endoplasmic reticulum-targeting sequence. This explains how it is able to switch its localization, either being in the endoplasmic reticulum or in the mitochondria depending on which N-terminal part begins the isoform. {ECO:0000269|PubMed:10352013}.; SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion outer membrane {ECO:0000269|PubMed:10352013}. Note=Does not contain the classic KDEL endoplasmic reticulum-targeting sequence. This explains how it is able to switch its localization, either being in the endoplasmic reticulum or in the mitochondria depending on which N-terminal part begins the isoform. {ECO:0000269|PubMed:10352013}.; SUBCELLULAR LOCATION: [Isoform 5]: Mitochondrion outer membrane {ECO:0000269|PubMed:10352013}. Note=Does not contain the classic KDEL endoplasmic reticulum-targeting sequence. This explains how it is able to switch its localization, either being in the endoplasmic reticulum or in the mitochondria depending on which N-terminal part begins the isoform. {ECO:0000269|PubMed:10352013}.; SUBCELLULAR LOCATION: [Isoform 6]: Mitochondrion outer membrane {ECO:0000269|PubMed:10352013}. Note=Does not contain the classic KDEL endoplasmic reticulum-targeting sequence. This explains how it is able to switch its localization, either being in the endoplasmic reticulum or in the mitochondria depending on which N-terminal part begins the isoform. {ECO:0000269|PubMed:10352013}.
| null | null | null | null | null |
FUNCTION: Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A (PubMed:9065479, PubMed:9182549). Anchors them to the cytoplasmic face of the mitochondrial outer membrane or allows them to reside in the endoplasmic reticulum (PubMed:9065479, PubMed:9182549). Involved in mitochondrial-mediated antiviral innate immunity (By similarity). Promotes translocation of NDUFS1 into mitochondria to regulate mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) activity (PubMed:32072193). Under diabetic conditions, myocardial AKAP1 expression decreases which blocks the translocation of NDUFS1 from the cytosol to mitochondria (PubMed:32072193). Reduction of NDUFS1 in mitochondria decreases ATP production and increases mitochondrial ROS level, which causes mitochondrial dysfunction and cell apoptosis, respectively, thereby leading to cardiac dysfunction (PubMed:32072193). {ECO:0000250|UniProtKB:Q92667, ECO:0000269|PubMed:32072193, ECO:0000269|PubMed:9065479, ECO:0000269|PubMed:9182549}.
|
Mus musculus (Mouse)
|
O08719
|
EVL_RAT
|
MFAFEEFSEQSICQARASVMVYDDTSKKWVPIKPGQQGFSRINIYHNTASNTFRVVGVKLQDQQVVINYSIVKGLKYNQATPTFHQWRDARQVYGLNFASKEEATTFSNAMLFALNIMNSQEGGPSTQRQVQNGPSPEEMDIQRRQVMEQQHRQESLERRISATGPILPPGHPSSAASATFSCSGPPPPPPPPVPPPPTGSTPPPPPPLPAGGAQGTNHDESSASGLAAALAGAKLRRVQRPEDASGGSSPSGTSKSDANRASSGGGGGGLMEEMNKLLAKRRKAASQTDKPADRKEDENQTEDPSTSPSPGSRATSQPPNSSEAGRKPWERSNSVEKPVSSLLSRTPSVAKSPEAKSPLQSQPHSRVKPAGSVNDVGLDALDLDRMKQEILEEVVRELHKVKEEIIDAIRQELSGISTT
| null | null |
actin polymerization or depolymerization [GO:0008154]; axon guidance [GO:0007411]; cellular response to type II interferon [GO:0071346]; central nervous system development [GO:0007417]; negative regulation of epithelial cell migration [GO:0010633]; negative regulation of ruffle assembly [GO:1900028]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of stress fiber assembly [GO:0051496]; protein homotetramerization [GO:0051289]
|
cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; phagocytic vesicle [GO:0045335]; stress fiber [GO:0001725]
|
actin binding [GO:0003779]; profilin binding [GO:0005522]; SH3 domain binding [GO:0017124]
|
PF08776;PF00568;
|
2.30.29.30;1.20.5.1160;
|
Ena/VASP family
|
PTM: Phosphorylated by PKA; phosphorylation abolishes binding to SH3 domains of ABL and SRC. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P70429}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:P70429}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P70429}. Note=Targeted to the leading edge of lamellipodia and the distal tip of stress fibers through interaction with a number of proteins. In activated T-cells, localizes to the F-actin collar and the distal tip of microspikes. {ECO:0000250|UniProtKB:P70429}.
| null | null | null | null | null |
FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O08721
|
UNC5A_RAT
|
MAVRPGLWPVLLGIVLAAWLRGSGAQQSATVANPVPGANPDLLPHFLVEPEDVYIVKNKPVLLVCKAVPATQIFFKCNGEWVRQVDHVIERSTDSSSGLPTMEVRINVSRQQVEKVFGLEEYWCQCVAWSSSGTTKSQKAYIRIAYLRKNFEQEPLAKEVSLEQGIVLPCRPPEGIPPAEVEWLRNEDLVDPSLDPNVYITREHSLVVRQARLADTANYTCVAKNIVARRRSTSAAVIVYVNGGWSTWTEWSVCSASCGRGWQKRSRSCTNPAPLNGGAFCEGQNVQKTACATLCPVDGSWSSWSKWSACGLDCTHWRSRECSDPAPRNGGEECRGADLDTRNCTSDLCLHTASCPEDVALYIGLVAVAVCLFLLLLALGLIYCRKKEGLDSDVADSSILTSGFQPVSIKPSKADNPHLLTIQPDLSTTTTTYQGSLCSRQDGPSPKFQLSNGHLLSPLGSGRHTLHHSSPTSEAEDFVSRLSTQNYFRSLPRGTSNMAYGTFNFLGGRLMIPNTGISLLIPPDAIPRGKIYEIYLTLHKPEDVRLPLAGCQTLLSPVVSCGPPGVLLTRPVILAMDHCGEPSPDSWSLRLKKQSCEGSWEDVLHLGEESPSHLYYCQLEAGACYVFTEQLGRFALVGEALSVAATKRLRLLLFAPVACTSLEYNIRVYCLHDTHDALKEVVQLEKQLGGQLIQEPRVLHFKDSYHNLRLSIHDVPSSLWKSKLLVSYQEIPFYHIWNGTQQYLHCTFTLERINASTSDLACKVWVWQVEGDGQSFNINFNITKDTRFAELLALESEGGVPALVGPSAFKIPFLIRQKIIASLDPPCSRGADWRTLAQKLHLDSHLSFFASKPSPTAMILNLWEARHFPNGNLGQLAAAVAGLGQPDAGLFTVSEAEC
| null | null |
anterior/posterior axon guidance [GO:0033564]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; netrin-activated signaling pathway [GO:0038007]; neuron projection development [GO:0031175]
|
membrane raft [GO:0045121]; neuron projection membrane [GO:0032589]; neuronal cell body membrane [GO:0032809]; plasma membrane [GO:0005886]
|
netrin receptor activity [GO:0005042]
|
PF00531;PF07679;PF00090;PF17217;PF00791;
|
2.60.220.30;1.10.533.10;2.60.40.10;2.20.100.10;
|
Unc-5 family
|
PTM: Phosphorylated on cytoplasmic tyrosine residues (By similarity). Phosphorylated by PKC in vitro. {ECO:0000250, ECO:0000269|PubMed:14672991}.; PTM: Proteolytically cleaved by caspases during apoptosis. The cleavage does not take place when the receptor is associated with netrin ligand. Its cleavage by caspases is required to induce apoptosis. {ECO:0000269|PubMed:11387206}.; PTM: The two extracellular TSRs of UNC5A contain WxxWxxWxxC motifs that can be C-mannosylated on all tryptophans. DPY19L1 preferentially mannosylates the first two tryptophans and DPY19L3 prefers the third. C-mannosylation by DPY19L1 is required for transport of UNC5A from the endoplasmic reticulum to the cell surface. {ECO:0000250|UniProtKB:Q8K1S4}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12598531, ECO:0000269|PubMed:19755150, ECO:0000269|PubMed:9126742}; Single-pass type I membrane protein {ECO:0000269|PubMed:12598531, ECO:0000269|PubMed:9126742, ECO:0000305}. Membrane raft {ECO:0000269|PubMed:18582460}. Cell projection, neuron projection {ECO:0000269|PubMed:19755150}. Note=The interaction with PRKCABP regulates its surface expression and leads to its removal from the surface of neurons and growth cones (PubMed:14672991). {ECO:0000269|PubMed:14672991}.
| null | null | null | null | null |
FUNCTION: Receptor for netrin required for axon guidance (PubMed:10399920, PubMed:9126742). Functions in the netrin signaling pathway and promotes neurite outgrowth in response to NTN1 (PubMed:19755150). Mediates axon repulsion of neuronal growth cones in the developing nervous system in response to netrin (PubMed:10399920). Axon repulsion in growth cones may be mediated by its association with DCC that may trigger signaling for repulsion (PubMed:10399920). It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (PubMed:11387206, PubMed:12598531). {ECO:0000269|PubMed:10399920, ECO:0000269|PubMed:11387206, ECO:0000269|PubMed:12598531, ECO:0000269|PubMed:9126742, ECO:0000305|PubMed:9126742}.
|
Rattus norvegicus (Rat)
|
O08722
|
UNC5B_RAT
|
MRARSGARGALLLALLLCWDPTPSLAGIDSGGQALPDSFPSAPAEQLPHFLLEPEDAYIVKNKPVELHCRAFPATQIYFKCNGEWVSQKGHVTQESLDEATGLRIREVQIEVSRQQVEELFGLEDYWCQCVAWSSSGTTKSRRAYIRIAYLRKNFDQEPLAKEVPLDHEVLLQCRPPEGVPVAEVEWLKNEDVIDPAQDTNFLLTIDHNLIIRQARLSDTANYTCVAKNIVAKRRSTTATVIVYVNGGWSSWAEWSPCSNRCGRGWQKRTRTCTNPAPLNGGAFCEGQACQKTACTTVCPVDGAWTEWSKWSACSTECAHWRSRECMAPPPQNGGRDCSGTLLDSKNCTDGLCVLNQRTLNDPKSRPLEPSGDVALYAGLVVAVFVVLAVLMAVGVIVYRRNCRDFDTDITDSSAALTGGFHPVNFKTARPSNPQLLHPSAPPDLTASAGIYRGPVYALQDSADKIPMTNSPLLDPLPSLKIKVYDSSTIGSGAGLADGADLLGVLPPGTYPGDFSRDTHFLHLRSASLGSQHLLGLPRDPSSSVSGTFGCLGGRLTIPGTGVSLLVPNGAIPQGKFYDLYLRINKTESTLPLSEGSQTVLSPSVTCGPTGLLLCRPVVLTVPHCAEVIAGDWIFQLKTQAHQGHWEEVVTLDEETLNTPCYCQLEAKSCHILLDQLGTYVFTGESYSRSAVKRLQLAIFAPALCTSLEYSLRVYCLEDTPAALKEVLELERTLGGYLVEEPKTLLFKDSYHNLRLSLHDIPHAHWRSKLLAKYQEIPFYHVWNGSQKALHCTFTLERHSLASTEFTCKVCVRQVEGEGQIFQLHTTLAETPAGSLDALCSAPGNAATTQLGPYAFKIPLSIRQKICNSLDAPNSRGNDWRLLAQKLSMDRYLNYFATKASPTGVILDLWEARQQDDGDLNSLASALEEMGKSEMLVAMTTDGDC
| null | null |
anterior/posterior axon guidance [GO:0033564]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of neuron apoptotic process [GO:0043524]; positive regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001241]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]
|
membrane raft [GO:0045121]; plasma membrane [GO:0005886]
|
netrin receptor activity [GO:0005042]
|
PF00531;PF07679;PF00090;PF17217;PF00791;
|
2.60.220.30;1.10.533.10;2.60.40.10;2.20.100.10;
|
Unc-5 family
|
PTM: Phosphorylated on cytoplasmic tyrosine residues. {ECO:0000250}.; PTM: Proteolytically cleaved by caspases during apoptosis. The cleavage does not take place when the receptor is associated with netrin ligand. Its cleavage by caspases is required to induce apoptosis. {ECO:0000269|PubMed:11387206}.; PTM: Palmitoylation is required for pro-apoptotic activity, but not for location at lipid rafts. {ECO:0000269|PubMed:18582460}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9126742}; Single-pass type I membrane protein {ECO:0000269|PubMed:9126742}. Membrane raft {ECO:0000269|PubMed:18582460}. Note=Associated with lipid rafts (PubMed:18582460). {ECO:0000269|PubMed:18582460}.
| null | null | null | null | null |
FUNCTION: Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding. Axon repulsion in growth cones may be caused by its association with DCC that may trigger signaling for repulsion (PubMed:10399920, PubMed:9126742). Functions as a netrin receptor that negatively regulates vascular branching during angiogenesis. Mediates retraction of tip cell filopodia on endothelial growth cones in response to netrin (By similarity). It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (PubMed:11387206). Mediates apoptosis by activating DAPK1 (PubMed:18582460). In the absence of NTN1, activates DAPK1 by reducing its autoinhibitory phosphorylation at Ser-308 thereby increasing its catalytic activity (PubMed:15729359). {ECO:0000250|UniProtKB:Q8K1S3, ECO:0000269|PubMed:10399920, ECO:0000269|PubMed:11387206, ECO:0000269|PubMed:15729359, ECO:0000269|PubMed:18582460, ECO:0000305|PubMed:9126742}.
|
Rattus norvegicus (Rat)
|
O08725
|
GHSR_RAT
|
MWNATPSEEPEPNVTLDLDWDASPGNDSLPDELLPLFPAPLLAGVTATCVALFVVGISGNLLTMLVVSRFRELRTTTNLYLSSMAFSDLLIFLCMPLDLVRLWQYRPWNFGDLLCKLFQFVSESCTYATVLTITALSVERYFAICFPLRAKVVVTKGRVKLVILVIWAVAFCSAGPIFVLVGVEHENGTDPRDTNECRATEFAVRSGLLTVMVWVSSVFFFLPVFCLTVLYSLIGRKLWRRRGDAAVGASLRDQNHKQTVKMLAVVVFAFILCWLPFHVGRYLFSKSFEPGSLEIAQISQYCNLVSFVLFYLSAAINPILYNIMSKKYRVAVFKLLGFESFSQRKLSTLKDESSRAWTKSSINT
| null | null |
actin polymerization or depolymerization [GO:0008154]; adult feeding behavior [GO:0008343]; cellular response to insulin stimulus [GO:0032869]; cellular response to insulin-like growth factor stimulus [GO:1990314]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to thyroid hormone stimulus [GO:0097067]; decidualization [GO:0046697]; female pregnancy [GO:0007565]; G protein-coupled receptor signaling pathway [GO:0007186]; ghrelin secretion [GO:0036321]; growth hormone secretion [GO:0030252]; hormone-mediated signaling pathway [GO:0009755]; insulin-like growth factor receptor signaling pathway [GO:0048009]; learning or memory [GO:0007611]; negative regulation of appetite [GO:0032099]; negative regulation of inflammatory response [GO:0050728]; negative regulation of insulin secretion [GO:0046676]; negative regulation of interleukin-1 beta production [GO:0032691]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of locomotion involved in locomotory behavior [GO:0090327]; negative regulation of macrophage apoptotic process [GO:2000110]; negative regulation of norepinephrine secretion [GO:0010700]; negative regulation of tumor necrosis factor production [GO:0032720]; positive regulation of appetite [GO:0032100]; positive regulation of eating behavior [GO:1904000]; positive regulation of fatty acid metabolic process [GO:0045923]; positive regulation of growth [GO:0045927]; positive regulation of insulin-like growth factor receptor signaling pathway [GO:0043568]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of small intestinal transit [GO:0120058]; positive regulation of small intestine smooth muscle contraction [GO:1904349]; positive regulation of sprouting angiogenesis [GO:1903672]; positive regulation of vascular endothelial cell proliferation [GO:1905564]; postsynaptic modulation of chemical synaptic transmission [GO:0099170]; regulation of feeding behavior [GO:0060259]; regulation of gastric motility [GO:1905333]; regulation of growth hormone secretion [GO:0060123]; regulation of hindgut contraction [GO:0043134]; regulation of neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0098696]; regulation of postsynapse organization [GO:0099175]; regulation of synapse assembly [GO:0051963]; regulation of transmission of nerve impulse [GO:0051969]; response to dexamethasone [GO:0071548]; response to estradiol [GO:0032355]; response to follicle-stimulating hormone [GO:0032354]; response to food [GO:0032094]; response to growth hormone [GO:0060416]; response to hormone [GO:0009725]; response to L-glutamate [GO:1902065]; spermatogenesis [GO:0007283]
|
cell surface [GO:0009986]; glutamatergic synapse [GO:0098978]; membrane raft [GO:0045121]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; Schaffer collateral - CA1 synapse [GO:0098685]; synaptic membrane [GO:0097060]
|
G protein-coupled receptor activity [GO:0004930]; growth hormone receptor binding [GO:0005131]; growth hormone secretagogue receptor activity [GO:0001616]; growth hormone-releasing hormone receptor activity [GO:0016520]; hormone binding [GO:0042562]; peptide hormone binding [GO:0017046]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor for ghrelin, coupled to G-alpha-11 proteins. Stimulates growth hormone secretion. Binds also other growth hormone releasing peptides (GHRP) (e.g. Met-enkephalin and GHRP-6) as well as non-peptide, low molecular weight secretagogues (e.g. L-692,429, MK-0677, adenosine) (By similarity). {ECO:0000250, ECO:0000269|PubMed:10604470}.
|
Rattus norvegicus (Rat)
|
O08726
|
GALR2_RAT
|
MNGSGSQGAENTSQEGGSGGWQPEAVLVPLFFALIFLVGTVGNALVLAVLLRGGQAVSTTNLFILNLGVADLCFILCCVPFQATIYTLDDWVFGSLLCKAVHFLIFLTMHASSFTLAAVSLDRYLAIRYPLHSRELRTPRNALAAIGLIWGLALLFSGPYLSYYRQSQLANLTVCHPAWSAPRRRAMDLCTFVFSYLLPVLVLSLTYARTLRYLWRTVDPVTAGSGSQRAKRKVTRMIIIVAVLFCLCWMPHHALILCVWFGRFPLTRATYALRILSHLVSYANSCVNPIVYALVSKHFRKGFRKICAGLLRPAPRRASGRVSILAPGNHSGSMLEQESTDLTQVSEAAGPLVPPPALPNCTASSRTLDPAC
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; G protein-coupled receptor signaling pathway [GO:0007186]; galanin-activated signaling pathway [GO:0090663]; inositol phosphate metabolic process [GO:0043647]; neuron projection development [GO:0031175]; neuropeptide signaling pathway [GO:0007218]; phosphatidylinositol metabolic process [GO:0046488]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of transcription by RNA polymerase II [GO:0045944]
|
cilium [GO:0005929]; plasma membrane [GO:0005886]
|
galanin receptor activity [GO:0004966]; neuropeptide binding [GO:0042923]; peptide hormone binding [GO:0017046]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor for the hormone galanin, GALP and spexin-1. The activity of this receptor is mediated by G proteins that activate the phospholipase C/protein kinase C pathway (via G(q)) and that inhibit adenylyl cyclase (via G(i)).
|
Rattus norvegicus (Rat)
|
O08727
|
TR11B_RAT
|
MNKWLCCALLVFLDIIEWTTQETFPPKYLHYDPETGRQLLCDKCAPGTYLKQHCTVRRKTLCVPCPDYSYTDSWHTSDECVYCSPVCKELQTVKQECNRTHNRVCECEEGRYLELEFCLKHRSCPPGLGVLQAGTPERNTVCKRCPDGFFSGETSSKAPCRKHTNCSSLGLLLIQKGNATHDNVCSGNREATQNCGIDVTLCEEAFFRFAVPTKIIPNWLSVLVDSLPGTKVNAESVERIKRRHSSQEQTFQLLKLWKHQNRDQEMVKKIIQDIDLCESSVQRHIGHANLTTEQLRILMESLPGKKISPDEIERTRKTCKPSEQLLKLLSLWRIKNGDQDTLKGLMYALKHLKAYHFPKTVTHSLRKTIRFLHSFTMYRLYQKLFLEMIGNQVQSVKISCL
| null | null |
apoptotic process [GO:0006915]; extracellular matrix organization [GO:0030198]; negative regulation of bone resorption [GO:0045779]; negative regulation of odontogenesis of dentin-containing tooth [GO:0042489]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; response to arsenic-containing substance [GO:0046685]; response to estrogen [GO:0043627]; response to inorganic substance [GO:0010035]; response to magnesium ion [GO:0032026]; response to nutrient [GO:0007584]; response to xenobiotic stimulus [GO:0009410]
|
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; receptor complex [GO:0043235]
|
cytokine activity [GO:0005125]; heparan sulfate binding [GO:1904399]
|
PF00531;PF00020;
|
1.10.533.10;2.10.50.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Acts as a decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O08730
|
GLYG_RAT
|
MTDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRTVVLASPQVSDSMRKVLETVFDEVIMVDVLDSGDSAHLTLMKRPELGITLTKLHCWSLTQYSKCVFMDADTLVLSNIDDLFEREELSAAPDPGWPDCFNSGVFVYQPSIETYNQLLHLASEQGSFDGGDQGLLNTYFSGWATTDITKHLPFVYNLSSLSIYSYLPAFKAFGKNAKVVHFLGRTKPWNYTYNPQTKSVKCESQDPIVSHPEFLNLWWDTFTTNVLPLLQHHGLVKDAGSYLMMEHVTGALSDLSFGEAPPASQPSLSSEERKERWEQGQADYMGADSFDNIKRKLDTYLQ
|
2.4.1.186
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P13280}; Note=Divalent metal ions. Required for self-glucosylation. Manganese is the most effective. {ECO:0000250|UniProtKB:P13280};
|
glycogen biosynthetic process [GO:0005978]
|
cytoplasm [GO:0005737]
|
glucose binding [GO:0005536]; glycogenin glucosyltransferase activity [GO:0008466]; glycosyltransferase activity [GO:0016757]; manganese ion binding [GO:0030145]; protein homodimerization activity [GO:0042803]; UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity [GO:0102751]
|
PF01501;
| null |
Glycosyltransferase 8 family, Glycogenin subfamily
|
PTM: Self-glycosylated by the transfer of glucose residues from UDP-glucose to itself, forming an alpha-1,4-glycan of around 10 residues attached to Tyr-195. {ECO:0000250|UniProtKB:P13280}.; PTM: Phosphorylated. {ECO:0000250|UniProtKB:P13280}.
| null |
CATALYTIC ACTIVITY: Reaction=L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-glucosyl-L-tyrosyl-[glycogenin] + H(+) + UDP; Xref=Rhea:RHEA:23360, Rhea:RHEA-COMP:14604, Rhea:RHEA-COMP:14605, ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:140573; EC=2.4.1.186; Evidence={ECO:0000250|UniProtKB:P46976}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23361; Evidence={ECO:0000250|UniProtKB:P13280, ECO:0000250|UniProtKB:P46976}; CATALYTIC ACTIVITY: Reaction=[1,4-alpha-D-glucosyl](n)-L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = [1,4-alpha-D-glucosyl](n+1)-L-tyrosyl-[glycogenin] + H(+) + UDP; Xref=Rhea:RHEA:56560, Rhea:RHEA-COMP:14606, Rhea:RHEA-COMP:14607, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:140574; EC=2.4.1.186; Evidence={ECO:0000250|UniProtKB:P46976}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56561; Evidence={ECO:0000250|UniProtKB:P13280, ECO:0000250|UniProtKB:P46976};
| null |
PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000250|UniProtKB:P46976}.
| null | null |
FUNCTION: Glycogenin participates in the glycogen biosynthetic process along with glycogen synthase and glycogen branching enzyme. It self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase. {ECO:0000250|UniProtKB:P13280, ECO:0000250|UniProtKB:P46976}.
|
Rattus norvegicus (Rat)
|
O08734
|
BAK_MOUSE
|
MASGQGPGPPKVGCDESPSPSEQQVAQDTEEVFRSYVFYLHQQEQETQGAAAPANPEMDNLPLEPNSILGQVGRQLALIGDDINRRYDTEFQNLLEQLQPTAGNAYELFTKIASSLFKSGISWGRVVALLGFGYRLALYVYQRGLTGFLGQVTCFLADIILHHYIARWIAQRGGWVAALNFRRDPILTVMVIFGVVLLGQFVVHRFFRS
| null | null |
animal organ regeneration [GO:0031100]; apoptotic process involved in blood vessel morphogenesis [GO:1902262]; B cell apoptotic process [GO:0001783]; B cell homeostasis [GO:0001782]; B cell negative selection [GO:0002352]; blood vessel remodeling [GO:0001974]; calcium ion transport into cytosol [GO:0060402]; cellular response to mechanical stimulus [GO:0071260]; cellular response to UV [GO:0034644]; endocrine pancreas development [GO:0031018]; epithelial cell proliferation [GO:0050673]; establishment of localization in cell [GO:0051649]; establishment or maintenance of transmembrane electrochemical gradient [GO:0010248]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; fibroblast apoptotic process [GO:0044346]; homeostasis of number of cells [GO:0048872]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; leukocyte homeostasis [GO:0001776]; limb morphogenesis [GO:0035108]; mitochondrial fusion [GO:0008053]; myeloid cell homeostasis [GO:0002262]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of endoplasmic reticulum calcium ion concentration [GO:0032471]; negative regulation of gene expression [GO:0010629]; negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901029]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; positive regulation of apoptotic process [GO:0043065]; positive regulation of calcium ion transport into cytosol [GO:0010524]; positive regulation of endoplasmic reticulum unfolded protein response [GO:1900103]; positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901030]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of proteolysis [GO:0045862]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; post-embryonic camera-type eye morphogenesis [GO:0048597]; regulation of cell cycle [GO:0051726]; regulation of mitochondrial membrane permeability [GO:0046902]; regulation of mitochondrial membrane potential [GO:0051881]; release of cytochrome c from mitochondria [GO:0001836]; response to ethanol [GO:0045471]; response to fungus [GO:0009620]; response to gamma radiation [GO:0010332]; response to hydrogen peroxide [GO:0042542]; response to mycotoxin [GO:0010046]; response to organic cyclic compound [GO:0014070]; response to UV-C [GO:0010225]; response to xenobiotic stimulus [GO:0009410]; thymocyte apoptotic process [GO:0070242]; vagina development [GO:0060068]
|
BAK complex [GO:0097145]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; pore complex [GO:0046930]
|
BH domain binding [GO:0051400]; heat shock protein binding [GO:0031072]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; porin activity [GO:0015288]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; protein-folding chaperone binding [GO:0051087]; transmembrane transporter binding [GO:0044325]
|
PF00452;
|
1.10.437.10;
|
Bcl-2 family
| null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q16611}; Single-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2. {ECO:0000250}.
|
Mus musculus (Mouse)
|
O08736
|
CASPC_MOUSE
|
MAARRTHERDPIYKIKGLAKDMLDGVFDDLVEKNVLNGDELLKIGESASFILNKAENLVENFLEKTDMAGKIFAGHIANSQEQLSLQFSNDEDDGPQKICTPSSPSESKRKVEDDEMEVNAGLAHESHLMLTAPHGLQSSEVQDTLKLCPRDQFCKIKTERAKEIYPVMEKEGRTRLALIICNKKFDYLFDRDNADTDILNMQELLENLGYSVVLKENLTAQEMETELMQFAGRPEHQSSDSTFLVFMSHGILEGICGVKHRNKKPDVLHDDTIFKIFNNSNCRSLRNKPKILIMQACRGRYNGTIWVSTNKGIATADTDEERVLSCKWNNSITKAHVETDFIAFKSSTPHNISWKVGKTGSLFISKLIDCFKKYCWCYHLEEIFRKVQHSFEVPGELTQMPTIERVSMTRYFYLFPGN
|
3.4.22.-
| null |
endoplasmic reticulum unfolded protein response [GO:0030968]; fibroblast apoptotic process [GO:0044346]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; positive regulation of apoptotic process [GO:0043065]; positive regulation of inflammatory response [GO:0050729]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of striated muscle cell apoptotic process [GO:0010663]; protein autoprocessing [GO:0016540]; protein catabolic process [GO:0030163]; self proteolysis [GO:0097264]
|
AIM2 inflammasome complex [GO:0097169]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; IPAF inflammasome complex [GO:0072557]; NLRP1 inflammasome complex [GO:0072558]; NLRP3 inflammasome complex [GO:0072559]
|
cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; endopeptidase activity [GO:0004175]; protease binding [GO:0002020]
|
PF00619;PF00656;
|
3.40.50.1460;3.30.70.1470;1.10.533.10;
|
Peptidase C14A family
| null | null | null | null | null | null | null |
FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. {ECO:0000250}.
|
Mus musculus (Mouse)
|
O08738
|
CASP6_MOUSE
|
MTETDGFYKSREVFDPAEQYKMDHKRRGVALIFNHERFFWHLTLPERRGTNADRDNLTRRFSDLGFEVKCFNDLRAEELLLKIHEVSTSSHIDADCFICVFLSHGEGNHVYAYDAKIEIQTLTGLFKGDKCQSLVGKPKIFIIQACRGSQHDVPVVPLDMVDHQTDKLDNVTQVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLCEMLARYGSSLEFTELLTLVNRKVSQRRVDFCKDPDAIGKKQVPCFASMLTKKLHFCPKPSK
|
3.4.22.59
| null |
activation of innate immune response [GO:0002218]; acute inflammatory response to non-antigenic stimulus [GO:0002525]; axonal fasciculation [GO:0007413]; cellular response to staurosporine [GO:0072734]; epithelial cell differentiation [GO:0030855]; hepatocyte apoptotic process [GO:0097284]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; positive regulation of apoptotic process [GO:0043065]; positive regulation of necroptotic process [GO:0060545]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of retinal cell programmed cell death [GO:0046670]; protein autoprocessing [GO:0016540]; pyroptosis [GO:0070269]; response to cytokine [GO:0034097]; response to glucose [GO:0009749]; response to hydrogen peroxide [GO:0042542]; response to iron ion [GO:0010039]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
cysteine-type endopeptidase activity [GO:0004197]; cysteine-type endopeptidase activity involved in apoptotic process [GO:0097153]; cysteine-type endopeptidase activity involved in execution phase of apoptosis [GO:0097200]; endopeptidase activity [GO:0004175]; identical protein binding [GO:0042802]
|
PF00656;
|
3.40.50.1460;
|
Peptidase C14A family
|
PTM: Phosphorylated by NUAK1; phosphorylation inhibits self-activation. Phosphorylation at Ser-239 by AMP-activated protein kinase (PRKAA1 or PRKAA2) inhibits autocleavage, preventing caspase activation, thereby preventing hepatocyte apoptosis. {ECO:0000250|UniProtKB:P55212}.; PTM: Palmitoylation by ZDHHC17 blocks dimerization and subsequent activation, leading to inhibit the cysteine protease activity. {ECO:0000250|UniProtKB:P55212}.; PTM: Can be cleaved and activated by different caspases, depending on the context. Cleaved and activated by caspase-8 (CASP8) and subsequently by caspase-3 (CASP3). Can also undergo autoactivation by mediating autocleavage at Asp-162 and Asp-175, while it is not able to cleave its N-terminal disordered prodomain. Cleaved and activated by CASP1, possibly in the context of inflammation. {ECO:0000250|UniProtKB:P55212}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P55212}. Nucleus {ECO:0000250|UniProtKB:P55212}.
|
CATALYTIC ACTIVITY: Reaction=Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|-.; EC=3.4.22.59; Evidence={ECO:0000269|PubMed:22555455, ECO:0000269|PubMed:25231987};
| null | null | null | null |
FUNCTION: Cysteine protease that plays essential roles in programmed cell death, axonal degeneration, development and innate immunity (PubMed:18981099, PubMed:22555455, PubMed:23695670, PubMed:32298652). Acts as a non-canonical executioner caspase during apoptosis: localizes in the nucleus and cleaves the nuclear structural protein NUMA1 and lamin A/LMNA thereby inducing nuclear shrinkage and fragmentation (By similarity). Lamin-A/LMNA cleavage is required for chromatin condensation and nuclear disassembly during apoptotic execution (By similarity). Acts as a regulator of liver damage by promoting hepatocyte apoptosis: in absence of phosphorylation by AMP-activated protein kinase (AMPK), catalyzes cleavage of BID, leading to cytochrome c release, thereby participating in nonalcoholic steatohepatitis (PubMed:32029622). Cleaves PARK7/DJ-1 in cells undergoing apoptosis (PubMed:22555455). Involved in intrinsic apoptosis by mediating cleavage of RIPK1 (By similarity). Furthermore, cleaves many transcription factors such as NF-kappa-B and cAMP response element-binding protein/CREBBP (By similarity). Cleaves phospholipid scramblase proteins XKR4 and XKR9 (PubMed:25231987). In addition to apoptosis, involved in different forms of programmed cell death (PubMed:32298652). Plays an essential role in defense against viruses by acting as a central mediator of the ZBP1-mediated pyroptosis, apoptosis, and necroptosis (PANoptosis), independently of its cysteine protease activity (PubMed:32298652). PANoptosis is a unique inflammatory programmed cell death, which provides a molecular scaffold that allows the interactions and activation of machinery required for inflammasome/pyroptosis, apoptosis and necroptosis (PubMed:32298652). Mechanistically, interacts with RIPK3 and enhances the interaction between RIPK3 and ZBP1, leading to ZBP1-mediated inflammasome activation and cell death (PubMed:32298652). Plays an essential role in axon degeneration during axon pruning which is the remodeling of axons during neurogenesis but not apoptosis (PubMed:23695670). Regulates B-cell programs both during early development and after antigen stimulation (PubMed:18981099, PubMed:29863787). {ECO:0000250|UniProtKB:P55212, ECO:0000269|PubMed:18981099, ECO:0000269|PubMed:22555455, ECO:0000269|PubMed:23695670, ECO:0000269|PubMed:25231987, ECO:0000269|PubMed:29863787, ECO:0000269|PubMed:32029622, ECO:0000269|PubMed:32298652}.; FUNCTION: (Microbial infection) Proteolytically cleaves the N protein of coronaviruses. The cleavage leads to two fragments and modulates coronavirus replication by regulating IFN signaling. The two fragments produced by the cleavage interact with IRF3 inhibiting its nuclear translocation after activation and reduce the expression of IFNB and IFN-stimulated genes. {ECO:0000269|PubMed:35922005}.
|
Mus musculus (Mouse)
|
O08739
|
AMPD3_MOUSE
|
MPRQFPKLNMSDLDEHVRLLAEKVFAKVLREEDSKDVMSLFTVPEDCPIGQKEAKERELQKELAEQKSVETAKRKKSFKMIRSQSLSLQMPTQQDWKGPPTASPAMSPATPLVPGATSKPGPAPYAMPEYQRVTISGDYCAGITVEDYEQAAKSLAKALMIREKYARLAYHRFPRTTAQYLAHQGESVPLEEGLPDFHPPPLPQEDPYCLDDAPPNLGYLVRMHGGVLFVYDNQTMLERQEPHSLPYPDLETYIVDMSHILALITDGPTKTYCHRRLNFLESKFSLHEMLNEMSEFKELKSNPHRDFYNVRKVDTHIHAAACMNQKHLLRFIKHTYQTEPDRTVAEKLGRKITLRQVFDSLHMDPYDLTVDSLDVHAGRQTFHRFDKFNSKYNPVGASELRDLYLKTENYLGGEYFARMVKEVARELEDSKYQYSEPRLSIYGRSPKEWSSLARWFIQHKVYSPNMRWIIQVPRIYDIFRSKKLLPNFGKMLENIFLPLFKATINPQDHRELHLFLKYVTGFDSVDDESKHSDHMFSDKSPSPDLWTSEQNPPYSYYLYYMYANIMVLNNLRRERGLSTFLFRPHCGEAGSITHLVSAFLTADNISHGLLLKKSPVLQYLYYLAQIPIAMSPLSNNSLFLEYSKNPLREFLHKGLHVSLSTDDPMQFHYTKEALMEEYAIAAQVWKLSTCDLCEIARNSVLQSGLSHQEKQKFLGQNYYKEGPEGNDIRKTNVAQIRMAFRYETLCNELSFLSDAMKSEEITALTK
|
3.5.4.6
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
ADP catabolic process [GO:0046032]; ADP metabolic process [GO:0046031]; AMP catabolic process [GO:0006196]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; energy homeostasis [GO:0097009]; erythrocyte homeostasis [GO:0034101]; GTP metabolic process [GO:0046039]; IMP biosynthetic process [GO:0006188]; IMP salvage [GO:0032264]
|
cytosol [GO:0005829]
|
AMP deaminase activity [GO:0003876]; metal ion binding [GO:0046872]
|
PF19326;
|
4.10.800.20;3.20.20.140;
|
Metallo-dependent hydrolases superfamily, Adenosine and AMP deaminases family
| null | null |
CATALYTIC ACTIVITY: Reaction=AMP + H(+) + H2O = IMP + NH4(+); Xref=Rhea:RHEA:14777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; EC=3.5.4.6; Evidence={ECO:0000269|PubMed:9133604}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14778; Evidence={ECO:0000305|PubMed:9133604};
| null |
PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1. {ECO:0000305|PubMed:9133604}.
| null | null |
FUNCTION: AMP deaminase plays a critical role in energy metabolism. {ECO:0000305|PubMed:9133604}.
|
Mus musculus (Mouse)
|
O08746
|
MATN2_MOUSE
|
MEKMLVGCLLMLGQLFLVLPVDGRERPQARFPSRGRHVRMYPQTALLESSCENKRADLVFIIDSSRSVNTYDYAKVKEFILDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTGTMTGLAIQYALNIAFSEAEGARPLRENVPRIIMIVTDGRPQDSVAEVAAKARNTGILIFAIGVGQVDLNTLKAIGSEPHKDHVFLVANFSQIESLTSVFQNKLCTVHMCSVLEHNCAHFCLNTPGSYICKCKQGYILSTDQKTCRIQDLCATEDHGCEQLCVNMLGSFVCQCYSGYTLAEDGKRCTAVDYCASENHGCEHECVNAESSYLCRCHEGFALNSDKKTCSKIDYCASSNHGCQHECVNAQTSALCRCLKGFMLNPDRKTCRRINYCALNKPGCEHECVNTEEGHYCRCRQGYNLDPNGKTCSRVDHCAQQDHGCEQLCLNTEESFVCQCSEGFLINDDLKTCSRADYCLLSNHGCEYSCVNTDKSFACQCPEGHVLRSDGKTCAKLDSCALGDHGCEHSCVSSEDSFVCQCFEGYILRDDGKTCRRKDVCQDVNHGCEHLCVNSGESYVCKCLEGFRLAEDGKRCRRKNVCKSTQHGCEHMCVNNGNSYLCRCSEGFVLAEDGKHCKRCTEGPIDLVFVIDGSKSLGEENFETVKHFVTGIIDSLAVSPKAARVGLLQYSTQVRTEFTLRGFSSAKEMKKAVTHMKYMGKGSMTGLALKHMFERSFTQVEGARPPSTQVPRVAIVFTDGRAQDDVSEWASKAKANGITMYAVGVGKAIEEELQEIASEPIDKHLFYAEDFSTMGEISEKLKEGICEALEDSGGRQDSAAWDLPQQAHQPTEPEPVTIKIKDLLSCSNFAVQHRFLFEEDNLSRSTQKLFHSTKSSGNPLEESQDQCKCENLILFQNVANEEVRKLTQRLEEMTQRMEALENRLKYR
| null | null |
axon guidance [GO:0007411]; dendrite regeneration [GO:0031104]; extracellular matrix organization [GO:0030198]; glial cell migration [GO:0008347]; neuron migration [GO:0001764]; neuron projection development [GO:0031175]; response to axon injury [GO:0048678]
|
basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; matrilin complex [GO:0120216]
|
calcium ion binding [GO:0005509]
|
PF07645;PF14670;PF10393;PF00092;
|
1.20.5.30;2.10.25.10;3.40.50.410;
| null | null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Involved in matrix assembly. {ECO:0000250}.
|
Mus musculus (Mouse)
|
O08747
|
UNC5C_MOUSE
|
MRKGLRATAARCGLGLGYLLQMLVLPALALLSASGTGSAAQDDEFFHELPETFPSDPPEPLPHFLIEPEEAYIVKNKPVNLYCKASPATQIYFKCNSEWVHQKDHVVDERVDETSGLIVREVSIEISRQQVEELFGPEDYWCQCVAWSSAGTTKSRKAYVRIAYLRKTFEQEPLGKEVSLEQEVLLQCRPPEGIPVAEVEWLKNEDIIDPAEDRNFYITIDHNLIIKQARLSDTANYTCVAKNIVAKRKSTTATVIVYVNGGWSTWTEWSVCNSRCGRGYQKRTRTCTNPAPLNGGAFCEGQSVQKIACTTLCPVDGRWTSWSKWSTCGTECTHWRRRECTAPAPKNGGKDCDGLVLQSKNCTDGLCMQAAPDSDDVALYVGIVIAVTVCLAITVVVALFVYRKNHRDFESDIIDSSALNGGFQPVNIKAARQDLLAVPPDLTSAAAMYRGPVYALHDVSDKIPMTNSPILDPLPNLKIKVYNSSGAVTPQDDLAEFSSKLSPQMTQSLLENEALNLKNQSLARQTDPSCTAFGTFNSLGGHLIIPNSGVSLLIPAGAIPQGRVYEMYVTVHRKENMRPPMEDSQTLLTPVVSCGPPGALLTRPVILTLHHCADPSTEDWKIQLKNQAVQGQWEDVVVVGEENFTTPCYIQLDAEACHILTENLSTYALVGQSTTKAAAKRLKLAIFGPLCCSSLEYSIRVYCLDDTQDALKEVLQLERQMGGQLLEEPKALHFKGSIHNLRLSIHDIAHSLWKSKLLAKYQEIPFYHIWSGSQRNLHCTFTLERLSLNTVELVCKLCVRQVEGEGQIFQLNCTVSEEPTGIDLPLLDPASTITTVTGPSAFSIPLPIRQKLCSSLDAPQTRGHDWRMLAHKLNLDRYLNYFATKSSPTGVILDLWEAQNFPDGNLSMLAAVLEEMGRHETVVSLAAEGQY
| null | null |
anterior/posterior axon guidance [GO:0033564]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; brain development [GO:0007420]; chemorepulsion of axon [GO:0061643]; dorsal root ganglion development [GO:1990791]; ectopic germ cell programmed cell death [GO:0035234]; netrin-activated signaling pathway [GO:0038007]; positive regulation of apoptotic process [GO:0043065]; positive regulation of developmental process [GO:0051094]; positive regulation of reproductive process [GO:2000243]; regulation of cell migration [GO:0030334]; regulation of neuron migration [GO:2001222]
|
axon [GO:0030424]; cell surface [GO:0009986]; dendrite [GO:0030425]; filopodium [GO:0030175]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; synapse [GO:0045202]
|
netrin receptor activity [GO:0005042]; netrin receptor activity involved in chemorepulsion [GO:0005043]; protein kinase binding [GO:0019901]; tubulin binding [GO:0015631]
|
PF00531;PF07679;PF00090;PF17217;PF00791;
|
2.60.220.30;1.10.533.10;2.60.40.10;2.20.100.10;
|
Unc-5 family
|
PTM: Phosphorylated on different cytoplasmic tyrosine residues (PubMed:11533026). Phosphorylation of Tyr-568 leads to an interaction with PTPN11 phosphatase, suggesting that its activity is regulated by phosphorylation/dephosphorylation (PubMed:11533026). Tyrosine phosphorylation is netrin-dependent (PubMed:11533026, PubMed:22685302). {ECO:0000269|PubMed:11533026, ECO:0000269|PubMed:22685302}.; PTM: Proteolytically cleaved by caspases during apoptosis. The cleavage does not take place when the receptor is associated with netrin ligand. Its cleavage by caspases is required to induce apoptosis. {ECO:0000250|UniProtKB:Q761X5}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22405201}; Single-pass type I membrane protein {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:O95185}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q761X5}. Cell projection, dendrite {ECO:0000269|PubMed:22685302}. Cell projection, axon {ECO:0000269|PubMed:22685302}. Cell projection, growth cone {ECO:0000269|PubMed:22685302, ECO:0000269|PubMed:28483977}. Cell projection, lamellipodium {ECO:0000269|PubMed:28483977}. Cell projection, filopodium {ECO:0000269|PubMed:28483977}.
| null | null | null | null | null |
FUNCTION: Receptor for netrin required for axon guidance (PubMed:10399920, PubMed:22685302). Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding (PubMed:10399920, PubMed:22685302). NTN1/Netrin-1 binding might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion (PubMed:28483977). Axon repulsion in growth cones may also be caused by its association with DCC that may trigger signaling for repulsion (PubMed:10399920). Might also collaborate with DSCAM in NTN1-mediated axon repulsion independently of DCC (PubMed:22685302). Also involved in corticospinal tract axon guidance independently of DCC (PubMed:12451134, PubMed:9126743, PubMed:9389662). Involved in dorsal root ganglion axon projection towards the spinal cord (By similarity). It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (By similarity). {ECO:0000250|UniProtKB:O95185, ECO:0000250|UniProtKB:Q761X5, ECO:0000269|PubMed:10399920, ECO:0000269|PubMed:12451134, ECO:0000269|PubMed:22685302, ECO:0000269|PubMed:28483977, ECO:0000269|PubMed:9126743, ECO:0000269|PubMed:9389662}.
|
Mus musculus (Mouse)
|
O08749
|
DLDH_MOUSE
|
MQSWSRVYRSLAKKGHFNRISHGLQGVSSVPLRTYADQPIEADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEIPEVRLNLEKMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATKADGSTQVIDTKNILVATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQRQGFKFKLNTKVTGATKKSDGKIDVSVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRAKTNADTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAAFGKPINF
|
1.8.1.4
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P09622}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P09622};
|
2-oxoglutarate metabolic process [GO:0006103]; acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; branched-chain amino acid catabolic process [GO:0009083]; dihydrolipoamide metabolic process [GO:0051068]; gastrulation [GO:0007369]; histone succinylation [GO:0106077]; lipoate metabolic process [GO:0009106]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; proteolysis [GO:0006508]; regulation of membrane potential [GO:0042391]; sperm capacitation [GO:0048240]
|
acetyltransferase complex [GO:1902493]; acrosomal matrix [GO:0043159]; cilium [GO:0005929]; mitochondrial matrix [GO:0005759]; mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739]; motile cilium [GO:0031514]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; oxoglutarate dehydrogenase complex [GO:0045252]; pyruvate dehydrogenase complex [GO:0045254]
|
branched-chain alpha-keto acid dehydrogenase activity [GO:0047101]; dihydrolipoyl dehydrogenase activity [GO:0004148]; flavin adenine dinucleotide binding [GO:0050660]; lipoamide binding [GO:0043544]; NAD binding [GO:0051287]; pyruvate dehydrogenase (NAD+) activity [GO:0034604]
|
PF07992;PF02852;
|
3.30.390.30;3.50.50.60;
|
Class-I pyridine nucleotide-disulfide oxidoreductase family
|
PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q811C4}.
|
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:36854377, ECO:0000305|PubMed:9169128}. Nucleus {ECO:0000250|UniProtKB:P09622}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q811C4}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:15888450}. Note=Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation. {ECO:0000250|UniProtKB:P09622}.
|
CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4; Evidence={ECO:0000250|UniProtKB:P09622};
| null | null | null | null |
FUNCTION: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (By similarity). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (By similarity). In monomeric form may have additional moonlighting function as serine protease (PubMed:17404228). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity). {ECO:0000250|UniProtKB:P09622, ECO:0000250|UniProtKB:Q811C4, ECO:0000269|PubMed:17404228}.
|
Mus musculus (Mouse)
|
O08750
|
NFIL3_MOUSE
|
MQLRKMQTIKKEPAPLDPTSSSDKMLLLNSALAEVAEDLASGEDLLLNEGSMGKNKSSACRRKREFIPDEKKDAMYWEKRRKNNEAAKRSREKRRLNDLVLENKLIALGEENATLKAELLSLKLKFGLISSTAYAQEIQKLSNSTAVYFQDYQTSKAAVSSFVDEHEPAMVAGSCISVIKHSPQSSLSDVSEVSSVEHTQESPAQGGCRSPENKFPVIKQEPVELESFAREAREERGTYSTSIYQSYMGSSFSTYSHSPPLLQVHGSTSNSPRTSEADEGVVGKSSDGEDEQQVPKGPIHSPVELQRVHATVVKVPEVNPSALPHKLRIKAKAMQVKVEALDSEFEGMQKLSSPADAIAKRHFDLEKHGTSGMAHSSLPPFSVQVTNIQDWSLKSEHWHHKELSSKTQSSFKTGVVEVKDGGYKVSEAENLYLKQGIANLSAEVVSLKRFIATQPISASDSR
| null | null |
cellular response to interleukin-4 [GO:0071353]; circadian rhythm [GO:0007623]; immune response [GO:0006955]; natural killer cell differentiation [GO:0001779]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; regulation of DNA-templated transcription [GO:0006355]; transcription by RNA polymerase II [GO:0006366]
|
nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; identical protein binding [GO:0042802]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF07716;PF06529;
|
1.20.5.170;
|
BZIP family, NFIL3 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:11316793}.
| null | null | null | null | null |
FUNCTION: Acts as a transcriptional regulator that recognizes and binds to the sequence 5'-[GA]TTA[CT]GTAA[CT]-3', a sequence present in many cellular and viral promoters. Represses transcription from promoters with activating transcription factor (ATF) sites (By similarity). Represses promoter activity in osteoblasts. Represses transcriptional activity of PER1. Represses transcriptional activity of PER2 via the B-site on the promoter. Activates transcription from the interleukin-3 promoter in T-cells (By similarity). Competes for the same consensus-binding site with PAR DNA-binding factors (DBP, HLF and TEF). Component of the circadian clock that acts as a negative regulator for the circadian expression of PER2 oscillation in the cell-autonomous core clock. Protects pro-B cells from programmed cell death. Represses the transcription of CYP2A5 (PubMed:30555544). Positively regulates the expression and activity of CES2 by antagonizing the repressive action of NR1D1 on CES2 (PubMed:29653076). Required for the development of natural killer cell precursors (PubMed:32190943). {ECO:0000250|UniProtKB:Q16649, ECO:0000269|PubMed:11316793, ECO:0000269|PubMed:15087429, ECO:0000269|PubMed:17182630, ECO:0000269|PubMed:29653076, ECO:0000269|PubMed:30555544, ECO:0000269|PubMed:32190943, ECO:0000269|PubMed:9122243}.
|
Mus musculus (Mouse)
|
O08755
|
HNF6_MOUSE
|
MNAQLTMEAIGELHGVSHEPVPAPADLLGGSPHARSSVGHRGSHLPPAHPRSMGMASLLDGGSGGSDYHHHHRAPEHSLAGPLHPTMTMACETPPGMSMPTTYTTLTPLQPLPPISTVSDKFPHHHHHHHHHHHPHHHQRLAGNVSGSFTLMRDERGLASMNNLYTPYHKDVAGMGQSLSPLSGSGLGSIHNSQQGLPHYAHPGAAMPTDKMLTPNGFEAHHPAMLGRHGEQHLTPTSAGMVPINGLPPHHPHAHLNAQGHGQLLGTAREPNPSVTGAQVSNGSNSGQMEEINTKEVAQRITTELKRYSIPQAIFAQRVLCRSQGTLSDLLRNPKPWSKLKSGRETFRRMWKWLQEPEFQRMSALRLAACKRKEQEHGKDRGNTPKKPRLVFTDVQRRTLHAIFKENKRPSKELQITISQQLGLELSTVSNFFMNARRRSLDKWQDEGGSNSGSSSSSSSTCTKA
| null | null |
anatomical structure morphogenesis [GO:0009653]; B cell differentiation [GO:0030183]; cell fate commitment [GO:0045165]; cell migration [GO:0016477]; cilium assembly [GO:0060271]; endocrine pancreas development [GO:0031018]; endoderm development [GO:0007492]; enteroendocrine cell differentiation [GO:0035883]; epithelial cell development [GO:0002064]; glucose metabolic process [GO:0006006]; liver development [GO:0001889]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; Notch signaling pathway [GO:0007219]; pancreas development [GO:0031016]; pancreatic A cell differentiation [GO:0003310]; pancreatic D cell differentiation [GO:0003311]; positive regulation of cell migration [GO:0030335]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell-matrix adhesion [GO:0001952]; regulation of transcription by RNA polymerase II [GO:0006357]; spleen development [GO:0048536]; transforming growth factor beta receptor signaling pathway [GO:0007179]; type B pancreatic cell differentiation [GO:0003309]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF02376;PF00046;
|
1.10.10.60;1.10.260.40;
|
CUT homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Transcriptional activator. Binds the consensus sequence 5'-DHWATTGAYTWWD-3' on a variety of gene promoters such as those of HNF3B and TTR. Important for liver genes transcription. Stimulates the expression of Onecut3 in the developing endoderm. {ECO:0000269|PubMed:15381696}.
|
Mus musculus (Mouse)
|
O08756
|
HCD2_MOUSE
|
MAAAVRSVKGLVAVVTGGASGPWLATAKRLVGQGATAVLLDVPDSEGESQAKKLGESCIFAPANVTSEKEIQAALTLAKEKFGRIDVAVNCAGIAVAIKTYHQKKNKIHTLEDFQRVINVNLIGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIDGMTLPIARDLAPTGIRVVTIAPGLFATPLLTTLPEKVRNFLASQVPFPSRLGDPAEYAHLVQTIIENPFLNGEVIRLDGAIRMQP
|
1.1.1.159; 1.1.1.178; 1.1.1.239; 1.1.1.35; 1.1.1.53; 1.1.1.62
| null |
androgen metabolic process [GO:0008209]; bile acid biosynthetic process [GO:0006699]; brexanolone metabolic process [GO:0062173]; C21-steroid hormone metabolic process [GO:0008207]; estrogen metabolic process [GO:0008210]; fatty acid beta-oxidation [GO:0006635]; fatty acid metabolic process [GO:0006631]; isoleucine catabolic process [GO:0006550]; mitochondrial tRNA 3'-end processing [GO:1990180]; mitochondrial tRNA 5'-end processing [GO:0097745]; mitochondrial tRNA methylation [GO:0070901]; protein homotetramerization [GO:0051289]; steroid catabolic process [GO:0006706]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrial inner membrane [GO:0005743]; mitochondrial nucleoid [GO:0042645]; mitochondrial ribonuclease P complex [GO:0030678]; mitochondrion [GO:0005739]
|
17-beta-hydroxysteroid dehydrogenase (NAD+) activity [GO:0044594]; 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity [GO:0047015]; 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; acetoacetyl-CoA reductase activity [GO:0018454]; amyloid-beta binding [GO:0001540]; androstan-3-alpha,17-beta-diol dehydrogenase activity [GO:0047044]; chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity [GO:0106281]; cholate 7-alpha-dehydrogenase activity [GO:0008709]; estradiol 17-beta-dehydrogenase [NAD(P)] activity [GO:0004303]; identical protein binding [GO:0042802]; isoursodeoxycholate 7-beta-dehydrogenase (NAD+) activity [GO:0106282]; NAD binding [GO:0051287]; nuclear estrogen receptor binding [GO:0030331]; steroid binding [GO:0005496]; testosterone dehydrogenase (NAD+) activity [GO:0047035]; testosterone dehydrogenase [NAD(P)] activity [GO:0030283]; tRNA binding [GO:0000049]; ursodeoxycholate 7-beta-dehydrogenase (NAD+) activity [GO:0106283]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q99714}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q99714}.
|
CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22433; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22434; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=(2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD(+) = 2-methyl-3-oxobutanoyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:13281, ChEBI:CHEBI:15378, ChEBI:CHEBI:57312, ChEBI:CHEBI:57335, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.178; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13282; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=NAD(+) + testosterone = androst-4-ene-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:14929, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422, ChEBI:CHEBI:17347, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.239; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14930; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=5alpha-androstane-3alpha,17beta-diol + NAD(+) = 17beta-hydroxy-5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42004, ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.53; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42006; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH; Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24613; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=cholate + NAD(+) = 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate + H(+) + NADH; Xref=Rhea:RHEA:19409, ChEBI:CHEBI:11893, ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.159; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19410; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=(3S)-3-hydroxybutanoyl-CoA + NAD(+) = acetoacetyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:30799, ChEBI:CHEBI:15378, ChEBI:CHEBI:57286, ChEBI:CHEBI:57316, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30800; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30801; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=(3S)-hydroxyoctanoyl-CoA + NAD(+) = 3-oxooctanoyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:31195, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62617, ChEBI:CHEBI:62619; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31196; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31197; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=(3S)-hydroxyhexadecanoyl-CoA + NAD(+) = 3-oxohexadecanoyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:31159, ChEBI:CHEBI:15378, ChEBI:CHEBI:57349, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62613; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31160; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31161; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=17beta-hydroxy-5alpha-androstan-3-one + NAD(+) = 5alpha-androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:41992, ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16330, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41993; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=5alpha-pregnan-20beta-ol-3-one + NAD(+) = 5alpha-pregnane-3,20-dione + H(+) + NADH; Xref=Rhea:RHEA:42008, ChEBI:CHEBI:15378, ChEBI:CHEBI:28952, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78594; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42009; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=3alpha-hydroxy-5alpha-pregnan-20-one + NAD(+) = 5alpha-pregnane-3,20-dione + H(+) + NADH; Xref=Rhea:RHEA:41980, ChEBI:CHEBI:15378, ChEBI:CHEBI:28952, ChEBI:CHEBI:50169, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41981; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=cortisone + NAD(+) = 17alpha-hydroxypregn-4-en-3,11,20-trione-21-al + H(+) + NADH; Xref=Rhea:RHEA:42016, ChEBI:CHEBI:15378, ChEBI:CHEBI:16962, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78596; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42017; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=11-dehydrocorticosterone + NAD(+) = H(+) + NADH + pregn-4-ene-3,11,20,21-tetraone; Xref=Rhea:RHEA:42020, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78600, ChEBI:CHEBI:78601; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42021; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=cortisol + NAD(+) = 11beta,17alpha-dihydroxypregn-4-ene-3,20,21-trione + H(+) + NADH; Xref=Rhea:RHEA:42012, ChEBI:CHEBI:15378, ChEBI:CHEBI:17650, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78595; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42013; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=chenodeoxycholate + NAD(+) = 7-oxolithocholate + H(+) + NADH; Xref=Rhea:RHEA:42036, ChEBI:CHEBI:15378, ChEBI:CHEBI:36234, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78605; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42037; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=NAD(+) + ursodeoxycholate = 7-oxolithocholate + H(+) + NADH; Xref=Rhea:RHEA:42028, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78604, ChEBI:CHEBI:78605; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42029; Evidence={ECO:0000250|UniProtKB:Q99714}; CATALYTIC ACTIVITY: Reaction=3beta,7beta-dihydroxy-5beta-cholan-24-oate + NAD(+) = 3beta-hydroxy-7-oxo-5beta-cholan-24-oate + H(+) + NADH; Xref=Rhea:RHEA:42024, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78602, ChEBI:CHEBI:78603; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42025; Evidence={ECO:0000250|UniProtKB:Q99714};
| null |
PATHWAY: Amino-acid degradation; L-isoleucine degradation. {ECO:0000250|UniProtKB:Q99714}.; PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000250|UniProtKB:Q99714}.; PATHWAY: Steroid metabolism. {ECO:0000250|UniProtKB:Q99714}.; PATHWAY: Lipid metabolism; bile acid biosynthesis. {ECO:0000250|UniProtKB:Q99714}.
| null | null |
FUNCTION: Mitochondrial dehydrogenase involved in pathways of fatty acid, branched-chain amino acid and steroid metabolism (By similarity). Acts as (S)-3-hydroxyacyl-CoA dehydrogenase in mitochondrial fatty acid beta-oxidation, a major degradation pathway of fatty acids. Catalyzes the third step in the beta-oxidation cycle, namely the reversible conversion of (S)-3-hydroxyacyl-CoA to 3-ketoacyl-CoA. Preferentially accepts straight medium- and short-chain acyl-CoA substrates with highest efficiency for (3S)-hydroxybutanoyl-CoA (By similarity). Acts as 3-hydroxy-2-methylbutyryl-CoA dehydrogenase in branched-chain amino acid catabolic pathway. Catalyzes the oxidation of 3-hydroxy-2-methylbutanoyl-CoA into 2-methyl-3-oxobutanoyl-CoA, a step in isoleucine degradation pathway (By similarity). Has hydroxysteroid dehydrogenase activity toward steroid hormones and bile acids. Catalyzes the oxidation of 3alpha-, 17beta-, 20beta- and 21-hydroxysteroids and 7alpha- and 7beta-hydroxy bile acids. Oxidizes allopregnanolone/brexanolone at the 3alpha-hydroxyl group, which is known to be critical for the activation of gamma-aminobutyric acid receptors (GABAARs) chloride channel. Has phospholipase C-like activity toward cardiolipin and its oxidized species (By similarity). Likely oxidizes the 2'-hydroxyl in the head group of cardiolipin to form a ketone intermediate that undergoes nucleophilic attack by water and fragments into diacylglycerol, dihydroxyacetone and orthophosphate. Has higher affinity for cardiolipin with oxidized fatty acids and may degrade these species during the oxidative stress response to protect cells from apoptosis (By similarity). By interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD) (By similarity). Essential for structural and functional integrity of mitochondria (PubMed:20077426). {ECO:0000250|UniProtKB:Q99714, ECO:0000269|PubMed:20077426}.; FUNCTION: In addition to mitochondrial dehydrogenase activity, moonlights as a component of mitochondrial ribonuclease P, a complex that cleaves tRNA molecules in their 5'-ends. Together with TRMT10C/MRPP1, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; HSD17B10/MRPP2 acting as a non-catalytic subunit. The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme. Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly. {ECO:0000250|UniProtKB:Q99714}.
|
Mus musculus (Mouse)
|
O08759
|
UBE3A_MOUSE
|
MATACKRSPGESQSEDIEASRMKRAAAKHLIERYYHQLTEGCGNEACTNEFCASCPTFLRMDNNAAAIKALELYKINAKLCDPHPSKKGASSAYLENSKGASNNSEIKMNKKEGKDFKDVIYLTEEKVYEIYEFCRESEDYSPLIRVIGRIFSSAEALVLSFRKVKQHTKEELKSLQEKDEDKDEDEKEKAACSAAAMEEDSEASSSRMGDSSQGDNNVQKLGPDDVTVDIDAIRRVYSSLLANEKLETAFLNALVYLSPNVECDLTYHNVYTRDPNYLNLFIIVMENSNLHSPEYLEMALPLFCKAMCKLPLEAQGKLIRLWSKYSADQIRRMMETFQQLITYKVISNEFNSRNLVNDDDAIVAASKCLKMVYYANVVGGDVDTNHNEEDDEEPIPESSELTLQELLGDERRNKKGPRVDPLETELGVKTLDCRKPLISFEEFINEPLNDVLEMDKDYTFFKVETENKFSFMTCPFILNAVTKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALVRLEMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDEATKLFWFNPSSFETEGQFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQSLKDLLEYEGSVEDDMMITFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDYILNKSVEKQFKAFRRGFHMVTNESPLKYLFRPEEIELLICGSRNLDFQALEETTEYDGGYTRESVVIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLGKLKMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGML
|
2.3.2.26
| null |
androgen receptor signaling pathway [GO:0030521]; cellular response to brain-derived neurotrophic factor stimulus [GO:1990416]; locomotory exploration behavior [GO:0035641]; modulation of chemical synaptic transmission [GO:0050804]; motor learning [GO:0061743]; negative regulation of dendritic spine morphogenesis [GO:0061002]; negative regulation of TORC1 signaling [GO:1904262]; ovarian follicle development [GO:0001541]; positive regulation of Golgi lumen acidification [GO:1905528]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of transcription by RNA polymerase II [GO:0045944]; progesterone receptor signaling pathway [GO:0050847]; prostate gland growth [GO:0060736]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autoubiquitination [GO:0051865]; protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; regulation of circadian rhythm [GO:0042752]; regulation of synaptic plasticity [GO:0048167]; regulation of ubiquitin-dependent protein catabolic process [GO:2000058]; response to cocaine [GO:0042220]; response to hydrogen peroxide [GO:0042542]; response to progesterone [GO:0032570]; rhythmic process [GO:0048511]; sperm entry [GO:0035037]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; nucleus [GO:0005634]; proteasome complex [GO:0000502]
|
metal ion binding [GO:0046872]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]
|
PF16558;PF00632;
|
3.30.2160.10;3.30.2410.10;3.90.1750.10;6.10.130.10;
| null |
PTM: Phosphorylation at Tyr-654 by ABL1 impairs E3 ligase activity. {ECO:0000250|UniProtKB:Q05086}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9182527}. Nucleus {ECO:0000269|PubMed:9182527}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; Evidence={ECO:0000269|PubMed:20211139, ECO:0000269|PubMed:30020076};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:20211139, ECO:0000269|PubMed:30020076}.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and transfers it to its substrates (PubMed:20211139, PubMed:24728990, PubMed:30020076). Several substrates have been identified including the BMAL1, ARC, LAMTOR1, RAD23A and RAD23B, MCM7 (which is involved in DNA replication), annexin A1, the PML tumor suppressor, and the cell cycle regulator CDKN1B (PubMed:20211139, PubMed:24728990, PubMed:30020076). Additionally, may function as a cellular quality control ubiquitin ligase by helping the degradation of the cytoplasmic misfolded proteins. Finally, UBE3A also promotes its own degradation in vivo (By similarity). Plays an important role in the regulation of the circadian clock: involved in the ubiquitination of the core clock component BMAL1, leading to its proteasomal degradation (PubMed:24728990). Acts as a regulator of synaptic development by mediating ubiquitination and degradation of ARC (PubMed:20211139). Required for synaptic remodeling in neurons by mediating ubiquitination and degradation of LAMTOR1, thereby limiting mTORC1 signaling and activity-dependent synaptic remodeling (PubMed:30020076). Synergizes with WBP2 in enhancing PGR activity (By similarity). {ECO:0000250|UniProtKB:Q05086, ECO:0000269|PubMed:20211139, ECO:0000269|PubMed:24728990, ECO:0000269|PubMed:30020076}.
|
Mus musculus (Mouse)
|
O08760
|
OGG1_MOUSE
|
MLFRSWLPSSMRHRTLSSSPALWASIPCPRSELRLDLVLASGQSFRWKEQSPAHWSGVLADQVWTLTQTEDQLYCTVYRGDDSQVSRPTLEELETLHKYFQLDVSLAQLYSHWASVDSHFQRVAQKFQGVRLLRQDPTECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHGFPNLHALAGPEAETHLRKLGLGYRARYVRASAKAILEEQGGPAWLQQLRVAPYEEAHKALCTLPGVGAKVADCICLMALDKPQAVPVDVHVWQIAHRDYGWHPKTSQAKGPSPLANKELGNFFRNLWGPYAGWAQAVLFSADLRQPSLSREPPAKRKKGSKRPEG
|
3.2.2.-; 4.2.99.18
| null |
base-excision repair [GO:0006284]; base-excision repair, AP site formation [GO:0006285]; cellular response to cadmium ion [GO:0071276]; cellular response to reactive oxygen species [GO:0034614]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; negative regulation of apoptotic process [GO:0043066]; negative regulation of double-strand break repair via single-strand annealing [GO:1901291]; nucleotide-excision repair [GO:0006289]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to folic acid [GO:0051593]; response to light stimulus [GO:0009416]; response to oxidative stress [GO:0006979]; response to radiation [GO:0009314]; response to xenobiotic stimulus [GO:0009410]
|
mitochondrion [GO:0005739]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
8-oxo-7,8-dihydroguanine DNA N-glycosylase activity [GO:0034039]; class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; DNA N-glycosylase activity [GO:0019104]; enzyme binding [GO:0019899]; microtubule binding [GO:0008017]; oxidized base lesion DNA N-glycosylase activity [GO:0000702]; oxidized purine DNA binding [GO:0032357]; oxidized purine nucleobase lesion DNA N-glycosylase activity [GO:0008534]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00730;PF07934;
|
3.30.310.40;1.10.1670.10;
|
Type-1 OGG1 family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus speckle {ECO:0000250}. Nucleus matrix {ECO:0000250}. Note=Together with APEX1 is recruited to nuclear speckles in UVA-irradiated cells. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18;
| null | null | null | null |
FUNCTION: DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.
|
Mus musculus (Mouse)
|
O08762
|
NETR_MOUSE
|
MALARCVLAVILGALSVVARADPVSRSPLHRPHPSPPRSQHAHYLPSSRRPPRTPRFPLPLRIPAAQRPQVLSTGHTPPTIPRRCGAGESWGNATNLGVPCLHWDEVPPFLERSPPASWAELRGQPHNFCRSPDGSGRPWCFYRNAQGKVDWGYCDCGQGPALPVIRLVGGNSGHEGRVELYHAGQWGTICDDQWDNADADVICRQLGLSGIAKAWHQAHFGEGSGPILLDEVRCTGNELSIEQCPKSSWGEHNCGHKEDAGVSCVPLTDGVIRLAGGKSTHEGRLEVYYKGQWGTVCDDGWTEMNTYVACRLLGFKYGKQSSVNHFDGSNRPIWLDDVSCSGKEVSFIQCSRRQWGRHDCSHREDVGLTCYPDSDGHRLSPGFPIRLVDGENKKEGRVEVFVNGQWGTICDDGWTDKHAAVICRQLGYKGPARARTMAYFGEGKGPIHMDNVKCTGNEKALADCVKQDIGRHNCRHSEDAGVICDYLEKKASSSGNKEMLSSGCGLRLLHRRQKRIIGGNNSLRGAWPWQASLRLRSAHGDGRLLCGATLLSSCWVLTAAHCFKRYGNNSRSYAVRVGDYHTLVPEEFEQEIGVQQIVIHRNYRPDRSDYDIALVRLQGPGEQCARLSTHVLPACLPLWRERPQKTASNCHITGWGDTGRAYSRTLQQAAVPLLPKRFCKERYKGLFTGRMLCAGNLQEDNRVDSCQGDSGGPLMCEKPDESWVVYGVTSWGYGCGVKDTPGVYTRVPAFVPWIKSVTSL
|
3.4.21.-
| null |
exocytosis [GO:0006887]; proteolysis [GO:0006508]; zymogen activation [GO:0031638]
|
axon [GO:0030424]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; plasma membrane [GO:0005886]; synapse [GO:0045202]; synaptic cleft [GO:0043083]; terminal bouton [GO:0043195]
|
peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]
|
PF00051;PF00530;PF00089;
|
2.40.20.10;3.10.250.10;2.40.10.10;
|
Peptidase S1 family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations.
|
Mus musculus (Mouse)
|
O08773
|
RGS14_RAT
|
MPGKPKHLGVPNGRMVLAVSDGELTSTSGSQAQGEGRGSSLSIHSLPSGPSSPFSTDEQPVASWAQSFERLLQDPRGLAYFTEFLKKEFSAENVTFWQACERFQQIPASDTKQLAQEAHNIYHEFLSSQALSPVNIDRQAWLSEEVLAQPRPDMFRAQQLQIFNLMKFDSYARFVKSPLYQECLLAEAEGRPLREPGSSHLGSPDTARKKPKLKPGKSLPLGVEELGQLPLAEGRPLRKSFRREMPGGAVNSALRRESQGSLNSSASLDLGFLAFVSSKSESHRKSLGSGEGESESRPGKYCCVYLPDGTASLALARPGLTIRDMLAGICEKRGLSLPDIKVYLVGKEQKALVLDQDCTVLADQEVRLENRITFQLELVGLERVVRISAKPTKRLQEALQPILAKHGLSLDQVVLHRPGEKQLVDLENLVSSVASQTLVLDTLPDAKTREASSIPPCRSQGCLPRTQTKDSHLPPLSSSLSVEDASGSTGKRQTCDIEGLVELLNRVQSSGAHDQRGLLRKEDLVLPEFLQLPSQRPGSQEAPP
| null | null |
cell division [GO:0051301]; chromosome segregation [GO:0007059]; learning [GO:0007612]; long-term memory [GO:0007616]; long-term synaptic potentiation [GO:0060291]; mitotic cell cycle [GO:0000278]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of G protein-coupled receptor signaling pathway [GO:0045744]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of synaptic plasticity [GO:0031914]; nucleocytoplasmic transport [GO:0006913]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of neurogenesis [GO:0050769]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; response to oxidative stress [GO:0006979]; spindle organization [GO:0007051]; visual learning [GO:0008542]; zygote asymmetric cell division [GO:0010070]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; microtubule [GO:0005874]; nuclear body [GO:0016604]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; PML body [GO:0016605]; postsynaptic density [GO:0014069]; spindle [GO:0005819]; spindle pole [GO:0000922]
|
G-protein alpha-subunit binding [GO:0001965]; GDP-dissociation inhibitor activity [GO:0005092]; GTPase activating protein binding [GO:0032794]; GTPase activator activity [GO:0005096]; microtubule binding [GO:0008017]; protein kinase binding [GO:0019901]; signaling receptor complex adaptor activity [GO:0030159]
|
PF02188;PF02196;PF00615;
|
1.10.196.10;1.10.167.10;
| null |
PTM: Phosphorylated by PKC. Phosphorylation is increased in presence of forskolin and may enhance the GDI activity on G(i) alpha subunit GNAI1. {ECO:0000269|PubMed:12534294}.
|
SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body {ECO:0000250}. Cytoplasm. Membrane. Cell membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Postsynaptic density {ECO:0000250}. Note=Associates with the perinuclear sheaths of microtubules (MTs) surrounding the pronuclei, prior to segregating to the anastral mitotic apparatus and subsequently the barrel-shaped cytoplasmic bridge between the nascent nuclei of the emerging 2-cell embryo. Localizes to a perinuclear compartment near the microtubule-organizing center (MTOC). Expressed in the nucleus during interphase and segregates to the centrosomes and astral MTs during mitosis. Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner. Relocalizes to the nucleus in PML nuclear bodies in respons to heat stress. Colocalizes with RIC8A in CA2 hippocampal neurons (By similarity). Localizes with spindle poles during metaphase. Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner. Recruited from the cytosol to the plasma membrane by the inactive GDP-bound forms of G(i) alpha subunits GNAI1 and GNAI3. Recruited from the cytosol to membranes by the active GTP-bound form of HRAS. Colocalizes with G(i) alpha subunit GNAI1 and RIC8A at the plasma membrane. Colocalizes with BRAF and RAF1 in both the cytoplasm and membranes. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Besides, modulates signal transduction via G protein alpha subunits by functioning as a GDP-dissociation inhibitor (GDI) (PubMed:11976690). Has GDI activity on G(i) alpha subunits GNAI1 and GNAI3, but not on GNAI2 and G(o)-alpha subunit GNAO1. Has GAP activity on GNAI0, GNAI2 and GNAI3. May act as a scaffold integrating G protein and Ras/Raf MAPkinase signaling pathways. Inhibits platelet-derived growth factor (PDGF)-stimulated ERK1/ERK2 phosphorylation; a process depending on its interaction with HRAS and that is reversed by G(i) alpha subunit GNAI1. Acts as a positive modulator of microtubule polymerisation and spindle organization through a G(i)-alpha-dependent mechanism. Plays a role in cell division; required for completion of the first mitotic division of the embryo. Involved in visual memory processing capacity; when overexpressed in the V2 secondary visual cortex area. Involved in hippocampal-based learning and memory; acts as a suppressor of synaptic plasticity in CA2 neurons. Required for the nerve growth factor (NGF)-mediated neurite outgrowth. Involved in stress resistance. {ECO:0000269|PubMed:11387333, ECO:0000269|PubMed:11976690, ECO:0000269|PubMed:15337739, ECO:0000269|PubMed:19319189, ECO:0000269|PubMed:19574389, ECO:0000269|PubMed:19878719, ECO:0000269|PubMed:21158412, ECO:0000269|PubMed:21255223}.
|
Rattus norvegicus (Rat)
|
O08774
|
RGS12_RAT
|
MYRAGEPGKRQSGPAPPRVRSVEVARGRAGYGFTLSGQAPCVLSCVMRGSPADFVGLRAGDQILAINEINVKKASHEDVVKLIGKCSGVLRMVISEGSSHVEPSSSDEEGGLCEGKGWLRPKLDSKALGINRAERVVEEVQSGGIFNMIFESPSLCASGSEPLKLKQRSLSESAALRLDVGQDSLCTPHPSMLSKEEISKVINDDSVFTVGLDNHDDFGLDASILNVAMVVGYLGSIELPSTSSNLEHDSLQAIRGCMRRLRAEQKIHSLVTMKVMHDCVQLVTDRAGVVAEYPAEKLAFSAVCPDDRRFFGLVTMQTNDDGCLAQEDEGALRTSCHVFMVDPDLFHHKIHQGIARRFGFACTADPDTSGCLEFPASSLPVLQFISVLYRDMGELIEGVRARAFLDGDADAHQNNSTSSNSDSGIGNFNQEEKSNRVLVVDLGGGSSRHGQGSSPGWESVSGRGSQPWSAPWNGTFCHDSEAGSPLETSPNTDRFWDLTKHSGPVFHMEVPPATLRSSIPPSKRGATGSSCGFNQRWLPVHVLQEWQCGHASDQESYTDSTDGWSSVNCGTLPPPMSKIPADRYRVEGSFAQAPLSTQKRDWSRKAFGMQNLFGPHRNVRKTKEDKKSSKLGRGVALAQTSQRTSARRSFGRSRRFSLTRSLDDLESATVSDGELTGADLKDCISNNSLSSNASLPSVQSCRRLRERRVASWAVSFERLLQDPVGVRYFSDFLRKEFSEENILFWQACECFSHVPAHDKKELSYRAREIFSKFLCSKATTPVNIDSQAQLADDILNAPHPDMFKEQQLQIFNLMKFDSYTRFLKSQLYQECVLAEVEGRTLPDSQQVPSSPASKHSISSDHSNVSTPKKLSGKSKSGRSLNEDVGEEDSEKKRKGAFFSWSRSRSTGRSQKKKDHGDHAHDALHANGGLCRRESQGSVSSAGSLDLSEACRTSALERDKAAKHCCVHLPDGTSCVVAVKSGFSIKEILSGLCERHGINGAAVDLFLVGGDKPLVLHQDSSILATRDLRLGKRTLFRLDLVPINRSVGLKAKPTKPVTEVLRPVVAKYGLDLGSLLVRLSGEKEPLDLGAPISSLDGQRVILEERDPSRGKVSTEKQKGAPVKQSSAVNSSPRNHSAMGEERTLGKSNSIKIRGENGKSARDPRLSKREESIAKIGKKKYQKINLDEAEEFFELISKAQSNRADDQRGLLRKEDLVLPEFLRLPPGSSELALSSPPPVKGFSKRAVTSHGQEGAVQTEESYSDSPATSPASAQSPCSAYSPGSAHSPGSAHSPGSAHSTPGPPGTAQPGEKPTKPSCISTVQEGTTQAWRRLSPELEAGGIQTVEEEQVADLTLMGEGDISSPNSTLLPPPPLPQDTPGPTRPGTSRF
| null | null |
negative regulation of G protein-coupled receptor signaling pathway [GO:0045744]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; signal transduction [GO:0007165]; termination of G protein-coupled receptor signaling pathway [GO:0038032]
|
apical dendrite [GO:0097440]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; synapse [GO:0045202]
|
G-protein alpha-subunit binding [GO:0001965]; GTPase activator activity [GO:0005096]; GTPase regulator activity [GO:0030695]
|
PF02188;PF00595;PF02196;PF00615;PF16613;PF16611;PF16612;
|
1.10.196.10;2.30.42.10;2.30.29.30;1.10.167.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16819986}. Cytoplasm {ECO:0000269|PubMed:16819986}. Cell projection, dendrite {ECO:0000269|PubMed:16819986}. Synapse {ECO:0000269|PubMed:16819986}.
| null | null | null | null | null |
FUNCTION: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. {ECO:0000269|PubMed:11387333, ECO:0000269|PubMed:9651375}.
|
Rattus norvegicus (Rat)
|
O08775
|
VGFR2_RAT
|
MESRALLAVALWFCVETRAASVGLPGDSLHPPKLSTQKDILTILANTTLQITCRGQRDLDWLWPNTPRDSEERVLVTECGDSIFCKTLTVPRVVGNDTGAYKCFYRDTDVSSIVYVYVQDHRSPFIASVSDEHGIVYITENKNKTVVIPCRGSISNLNVSLCARYPEKRFVPDGNRISWDSEKGFTIPSYMISYAGMVFCEAKINDETYQSIMYIVLVVGYRIYDVVLSPPHEIELSAGEKLVLNCTARTELNVGLDFSWQFPSSKHQHKKIVNRDVKSLPGTVAKMFLSTLTIDSVTKSDQGEYTCTAYSGLMTKKNKTFVRVHTKPFIAFGSGMKSLVEATVGSQVRIPVKYLSYPAPDIKWYRNGRPIESNYTMIVGDELTIMEVSERDAGNYTVILTNPISMEKQSHMVSLVVNVPPQIGEKALISPMDSYQYGTMQTLTCTVYANPPLHHIQWYWQLEEACSYRPSQTNPYTCKEWRHVKDFQGGNKIEVTKNQYALIEGKNKTVSTLVIQAAYVSALYKCEAINKAGRGERVISFHVIRGPEITVQPATQPTERESMSLLCTADRNTFENLTWYKLGSQATSVHMGESLTPVCKNLDALWKLNGTVFSNSTNDILIVAFQNASLQDQGNYVCSAQDKKTKKRHCLVKQLVILERMAPMITGNLENQTTTIGETIEVVCPTSGNPTPLITWFKDNETLVEDSGIVLKDGNRNLTIRRVRKEDGGLYTCQACNVLGCARAETLFIIEGVQEKTNLEVIILVGTAVIAMFFWLLLVILVRTVKRANEGELKTGYLSIVMDPDELPLDERCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCKTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIVEFCKFGNLSTYLRGKRNEFVPYKSKGARFRSGKDYVGELSVDLKRRLDSITSSQSSASSGFVEEKSLSDVEEEEASEELYKDFLTLEHLICYSFQVAKGMEFLASRKCIHRDLAARNILLSEKNVVKICDFGLARDIYKDPDYVRKGDPRLPLKWMAPETIFDRIYTIQSGVWSFGVLLWEIFSLGASPYPGVKIDEKFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHEDPNQRPAFSELVEHLGNLLQANAQQDGKDYIVLPMSETLSMEEDSGLSLPTSPVSCMEEEEVCDPKFHYDNTAGISHYLQNSKRKSRPVSVKTFEDIPLEEPEVKVIPDDSQTDSGMVLASEELKTLEDRNKLSPSFGGMMPSKSRESVASEGSNQTSGYQSGYHSDDTDTTVYSSDEAGLLKLVDVAGHVDSGTTLRSSPV
|
2.7.10.1
| null |
angiogenesis [GO:0001525]; blood vessel endothelial cell differentiation [GO:0060837]; branching involved in blood vessel morphogenesis [GO:0001569]; branching morphogenesis of an epithelial tube [GO:0048754]; calcium ion homeostasis [GO:0055074]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cell fate commitment [GO:0045165]; cell migration [GO:0016477]; cell migration involved in sprouting angiogenesis [GO:0002042]; cellular response to hydrogen sulfide [GO:1904881]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; embryonic hemopoiesis [GO:0035162]; endocardium development [GO:0003157]; endochondral bone growth [GO:0003416]; endothelial cell differentiation [GO:0045446]; endothelial tube morphogenesis [GO:0061154]; endothelium development [GO:0003158]; epithelial cell maturation [GO:0002070]; epithelial cell proliferation [GO:0050673]; hemopoiesis [GO:0030097]; lung alveolus development [GO:0048286]; lung development [GO:0030324]; lymph vessel development [GO:0001945]; male gonad development [GO:0008584]; mesenchymal cell proliferation [GO:0010463]; negative regulation of apoptotic process [GO:0043066]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of gene expression [GO:0010629]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of systemic arterial blood pressure [GO:0003085]; neuron projection morphogenesis [GO:0048812]; ovarian follicle development [GO:0001541]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of angiogenesis [GO:0045766]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulation of cell migration [GO:0030335]; positive regulation of cell migration involved in sprouting angiogenesis [GO:0090050]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway [GO:0038033]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of long-term neuronal synaptic plasticity [GO:0048170]; positive regulation of macroautophagy [GO:0016239]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of mitochondrial depolarization [GO:0051901]; positive regulation of mitochondrial fission [GO:0090141]; positive regulation of neurogenesis [GO:0050769]; positive regulation of nitric-oxide synthase biosynthetic process [GO:0051770]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of positive chemotaxis [GO:0050927]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of TOR signaling [GO:0032008]; positive regulation of vasculogenesis [GO:2001214]; post-embryonic camera-type eye morphogenesis [GO:0048597]; regulation of bone development [GO:1903010]; regulation of cell shape [GO:0008360]; regulation of hematopoietic progenitor cell differentiation [GO:1901532]; regulation of MAPK cascade [GO:0043408]; response to axon injury [GO:0048678]; response to hypoxia [GO:0001666]; response to oxygen levels [GO:0070482]; response to xenobiotic stimulus [GO:0009410]; semaphorin-plexin signaling pathway [GO:0071526]; stem cell proliferation [GO:0072089]; surfactant homeostasis [GO:0043129]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; vascular endothelial growth factor receptor-2 signaling pathway [GO:0036324]; vascular endothelial growth factor signaling pathway [GO:0038084]; vascular wound healing [GO:0061042]; vasculogenesis [GO:0001570]; vasodilation [GO:0042311]
|
anchoring junction [GO:0070161]; cell junction [GO:0030054]; cell periphery [GO:0071944]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; sorting endosome [GO:0097443]
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ATP binding [GO:0005524]; cadherin binding [GO:0045296]; coreceptor activity [GO:0015026]; growth factor binding [GO:0019838]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; protein tyrosine kinase activity [GO:0004713]; vascular endothelial growth factor binding [GO:0038085]; vascular endothelial growth factor receptor activity [GO:0005021]
|
PF07679;PF00047;PF13927;PF07714;PF21339;PF17988;
|
2.60.40.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily
|
PTM: N-glycosylated. {ECO:0000250}.; PTM: Ubiquitinated. Tyrosine phosphorylation of the receptor promotes its poly-ubiquitination, leading to its degradation via the proteasome or lysosomal proteases (By similarity). {ECO:0000250}.; PTM: Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-947 is important for interaction with SH2D2A/TSAD and VEGFA-mediated reorganization of the actin cytoskeleton. Phosphorylation at Tyr-1171 is important for interaction with PLCG1 and SHB. Phosphorylation at Tyr-1210 is important for interaction with NCK1 and FYN. Dephosphorylated by PTPRB. Dephosphorylated by PTPRJ at Tyr-797, Tyr-947, Tyr-992, Tyr-1050, Tyr-1055, Tyr-1171 and Tyr-1210 (By similarity). {ECO:0000250|UniProtKB:P35968}.; PTM: The inhibitory disulfide bond between Cys-1020 and Cys-1041 may serve as a specific molecular switch for H(2)S-induced modification that regulates KDR/VEGFR2 function. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35968}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Early endosome {ECO:0000250}. Cell junction {ECO:0000250}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P35968}. Note=Detected on caveolae-enriched lipid rafts at the cell surface. Is recycled from the plasma membrane to endosomes and back again. Phosphorylation triggered by VEGFA binding promotes internalization and subsequent degradation. VEGFA binding triggers internalization and translocation to the nucleus. Localized with RAP1A at cell-cell junctions. Colocalizes with ERN1 and XBP1 in the endoplasmic reticulum in endothelial cells in a vascular endothelial growth factor (VEGF)-dependent manner (By similarity). {ECO:0000250|UniProtKB:P35968}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol-1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC (By similarity). {ECO:0000250}.
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Rattus norvegicus (Rat)
|
O08785
|
CLOCK_MOUSE
|
MVFTVSCSKMSSIVDRDDSSIFDGLVEEDDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKETTAQSDASEIRQDWKPTFLSNEEFTQLMLEALDGFFLAIMTDGSIIYVSESVTSLLEHLPSDLVDQSIFNFIPEGEHSEVYKILSTHLLESDSLTPEYLKSKNQLEFCCHMLRGTIDPKEPSTYEYVRFIGNFKSLTSVSTSTHNGFEGTIQRTHRPSYEDRVCFVATVRLATPQFIKEMCTVEEPNEEFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLENLAKCHEHLMQYGKGKSCYYRFLTKGQQWIWLQTHYYITYHQWNSRPEFIVCTHTVVSYAEVRAERRRELGIEESLPETAADKSQDSGSDNRINTVSLKEALERFDHSPTPSASSRSSRKSSHTAVSDPSSTPTKIPTDTSTPPRQHLPAHEKMTQRRSSFSSQSINSQSVGPSLTQPAMSQAANLPIPQGMSQFQFSAQLGAMQHLKDQLEQRTRMIEANIHRQQEELRKIQEQLQMVHGQGLQMFLQQSNPGLNFGSVQLSSGNSNIQQLTPVNMQGQVVPANQVQSGHISTGQHMIQQQTLQSTSTQQSQQSVMSGHSQQTSLPSQTPSTLTAPLYNTMVISQPAAGSMVQIPSSMPQNSTQSATVTTFTQDRQIRFSQGQQLVTKLVTAPVACGAVMVPSTMLMGQVVTAYPTFATQQQQAQTLSVTQQQQQQQQQPPQQQQQQQQSSQEQQLPSVQQPAQAQLGQPPQQFLQTSRLLHGNPSTQLILSAAFPLQQSTFPPSHHQQHQPQQQQQLPRHRTDSLTDPSKVQPQ
|
2.3.1.48
| null |
cellular response to ionizing radiation [GO:0071479]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; DNA damage checkpoint signaling [GO:0000077]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of glucocorticoid receptor signaling pathway [GO:2000323]; positive regulation of circadian rhythm [GO:0042753]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of inflammatory response [GO:0050729]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein acetylation [GO:0006473]; regulation of circadian rhythm [GO:0042752]; regulation of DNA-templated transcription [GO:0006355]; regulation of hair cycle [GO:0042634]; regulation of insulin secretion [GO:0050796]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of type B pancreatic cell development [GO:2000074]; response to redox state [GO:0051775]; spermatogenesis [GO:0007283]
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chromatoid body [GO:0033391]; CLOCK-BMAL transcription complex [GO:1990513]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perichromatin fibrils [GO:0005726]; transcription regulator complex [GO:0005667]
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chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; histone acetyltransferase activity [GO:0004402]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
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PF00010;PF00989;PF14598;
|
4.10.280.10;3.30.450.20;
| null |
PTM: Ubiquitinated, leading to its proteasomal degradation. {ECO:0000269|PubMed:16980631}.; PTM: O-glycosylated; contains O-GlcNAc. O-glycosylation by OGT prevents protein degradation by inhibiting ubiquitination. It also stabilizes the CLOCK-BMAL1 heterodimer thereby increasing CLOCK-BMAL1-mediated transcriptional activation of PER1/2/3 and CRY1/2. {ECO:0000269|PubMed:23395175, ECO:0000269|PubMed:23395176}.; PTM: Phosphorylation is dependent on the CLOCK-BMAL1 heterodimer formation. Phosphorylation enhances the transcriptional activity, alters the subcellular localization and decreases the stability of the heterodimer by promoting its degradation. Phosphorylation shows circadian variations in the liver: the hyperphosphorylated form peaks at midnight (CT18), while the hypophosphorylated form is abundant throughout the day. May be phosphorylated by CSNK1D and CKSN1E. {ECO:0000269|PubMed:11779462, ECO:0000269|PubMed:12897057, ECO:0000269|PubMed:19414601, ECO:0000269|PubMed:19946213, ECO:0000269|PubMed:21930935, ECO:0000269|PubMed:24235147}.; PTM: Sumoylation enhances its transcriptional activity and interaction with ESR1, resulting in up-regulation of ESR1 activity. Estrogen stimulates sumoylation. Desumoylation by SENP1 negatively regulates its transcriptional activity. {ECO:0000269|PubMed:23160374}.; PTM: Undergoes lysosome-mediated degradation in a time-dependent manner in the liver. {ECO:0000269|PubMed:29937374}.
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SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11779462, ECO:0000269|PubMed:12897057, ECO:0000269|PubMed:16980631, ECO:0000269|PubMed:17310242, ECO:0000269|PubMed:18662546, ECO:0000269|PubMed:19414601}. Cytoplasm {ECO:0000269|PubMed:12897057, ECO:0000269|PubMed:16980631}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15516}. Note=Localizes to sites of DNA damage in a H2AX-independent manner (By similarity). Shuttling between the cytoplasm and the nucleus is under circadian regulation and is BMAL1-dependent. Phosphorylated form located in the nucleus predominantly between CT12 and CT21. Nonphosphorylated form found only in the cytoplasm. Sequestered to the cytoplasm in the presence of ID2. {ECO:0000250|UniProtKB:O15516, ECO:0000269|PubMed:11779462, ECO:0000269|PubMed:16980631, ECO:0000269|PubMed:20861012}.
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CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:16678094};
| null | null | null | null |
FUNCTION: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Regulates the circadian expression of ICAM1, VCAM1, CCL2, THPO and MPL and also acts as an enhancer of the transactivation potential of NF-kappaB. Plays an important role in the homeostatic regulation of sleep. The CLOCK-BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. May play a role in spermatogenesis; contributes to the chromatoid body assembly and physiology. The CLOCK-BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence (By similarity). CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3' (By similarity). The CLOCK-BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3'. CLOCK has an intrinsic acetyltransferase activity, which enables circadian chromatin remodeling by acetylating histones and nonhistone proteins, including its own partner BMAL1. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) via the acetylation of multiple lysine residues located in its hinge region. The acetyltransferase activity of CLOCK is as important as its transcription activity in circadian control. Acetylates metabolic enzymes IMPDH2 and NDUFA9 in a circadian manner (By similarity). Facilitated by BMAL1, rhythmically interacts and acetylates argininosuccinate synthase 1 (ASS1) leading to enzymatic inhibition of ASS1 as well as the circadian oscillation of arginine biosynthesis and subsequent ureagenesis (PubMed:28985504). Drives the circadian rhythm of blood pressure through transcriptional activation of ATP1B1 (PubMed:30012868). {ECO:0000250|UniProtKB:O15516, ECO:0000269|PubMed:12738229, ECO:0000269|PubMed:14672706, ECO:0000269|PubMed:16678094, ECO:0000269|PubMed:17417633, ECO:0000269|PubMed:18075593, ECO:0000269|PubMed:18316400, ECO:0000269|PubMed:19141540, ECO:0000269|PubMed:19286518, ECO:0000269|PubMed:19299583, ECO:0000269|PubMed:19605937, ECO:0000269|PubMed:20385766, ECO:0000269|PubMed:20430893, ECO:0000269|PubMed:20562852, ECO:0000269|PubMed:20658528, ECO:0000269|PubMed:20956306, ECO:0000269|PubMed:21768648, ECO:0000269|PubMed:22284746, ECO:0000269|PubMed:22653727, ECO:0000269|PubMed:22895791, ECO:0000269|PubMed:22900038, ECO:0000269|PubMed:22981862, ECO:0000269|PubMed:23291174, ECO:0000269|PubMed:23785138, ECO:0000269|PubMed:24089055, ECO:0000269|PubMed:24270424, ECO:0000269|PubMed:24333415, ECO:0000269|PubMed:24378737, ECO:0000269|PubMed:24385426, ECO:0000269|PubMed:24395244, ECO:0000269|PubMed:24442997, ECO:0000269|PubMed:28985504, ECO:0000269|PubMed:30012868}.
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Mus musculus (Mouse)
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O08786
|
CCKAR_MOUSE
|
MDVVDSLLMNGSNITPPCELGLENETLFCLDQPQPSKEWQSAVQILLYSFIFLLSVLGNTLVITVLIRNKRMRTVTNIFLLSLAVSDLMLCLFCMPFNLIPNLLKDFIFGSAVCKTTTYFMGTSVSVSTFNLVAISLERYGAICRPLQSRVWQTKSHALKVIAATWCLSFTIMTPYPIYSNLVPFTKNNNQTANMCRFLLPSDAMQQSWQTFLLLILFLIPGVVMVVAYGLISLELYQGIKFDASQKKSAKEKRLSSGGGGGGGSSSSRYEDSDGCYLQKSRPPRKLELQQLSTSSSGGRINRIRSSGSAANLIAKKRVIRMLIVIVVLFFLCWMPIFSANAWRAYDTVSAEKHLSGTPISFILLLSYTSSCVNPIIYCFMNKRFRLGFMATFPCCPNPGPTGVRGEVGEEEDGRTIRASLSRYSYSHMSTSAPPH
| null | null |
axonogenesis [GO:0007409]; cellular response to hormone stimulus [GO:0032870]; eating behavior [GO:0042755]; feeding behavior [GO:0007631]; forebrain development [GO:0030900]; G protein-coupled receptor signaling pathway [GO:0007186]; gastric acid secretion [GO:0001696]; insulin secretion [GO:0030073]; neuron migration [GO:0001764]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of somatostatin secretion [GO:0090274]; reduction of food intake in response to dietary excess [GO:0002023]; regulation of calcium ion transport [GO:0051924]; regulation of hormone secretion [GO:0046883]; regulation of potassium ion transport [GO:0043266]; response to starvation [GO:0042594]; temperature homeostasis [GO:0001659]
|
cytosol [GO:0005829]; endosome [GO:0005768]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; terminal bouton [GO:0043195]
|
cholecystokinin receptor activity [GO:0004951]; neuropeptide receptor activity [GO:0008188]; peptide binding [GO:0042277]; peptide hormone binding [GO:0017046]
|
PF00001;PF09193;
|
4.10.670.10;1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor for cholecystokinin. Mediates pancreatic growth and enzyme secretion, smooth muscle contraction of the gall bladder and stomach. Has a 1000-fold higher affinity for CCK rather than for gastrin. It modulates feeding and dopamine-induced behavior in the central and peripheral nervous system. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O08788
|
DCTN1_MOUSE
|
MAQSRRHMSSRTPSGSRMSTEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLKREGADAAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGPSSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDSTMQLADHIKFTQSALDCMGVEVGRLRAFLQGGQEATDIALLLRDLETSCSDTRQFCKKIRRRMPGTDAPGIPAALAFGSQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLPVAALEELAFKASEQIYGSPSSSPYECLRQSCTILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLDETQTLLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEGLRGPPPSGIATLVSGIAGEEPQRGGAPGQAPGALPGPGLVKDSPLLLQQISAMRLHISQLQHENSILRGAQMKASLAALPPLHVAKLSLPPHEGPGGNLVAGALYRKTSQLLEKLNQLSTHTHVVDITRSSPAAKSPSAQLMEQVAQLKSLSDTIEKLKDEVLKETVTQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGLGQRHRLVLTQEQLHQLHSRLIS
| null | null |
cell division [GO:0051301]; centriole-centriole cohesion [GO:0010457]; cytoplasmic microtubule organization [GO:0031122]; establishment of mitotic spindle orientation [GO:0000132]; melanosome transport [GO:0032402]; microtubule anchoring at centrosome [GO:0034454]; motor behavior [GO:0061744]; neuromuscular junction development [GO:0007528]; neuromuscular process [GO:0050905]; neuron cellular homeostasis [GO:0070050]; neuron projection maintenance [GO:1990535]; non-motile cilium assembly [GO:1905515]; nuclear membrane disassembly [GO:0051081]; nuclear migration [GO:0007097]; positive regulation of intracellular protein transport [GO:0090316]; positive regulation of microtubule nucleation [GO:0090063]; positive regulation of microtubule polymerization [GO:0031116]; positive regulation of neuromuscular junction development [GO:1904398]; regulation of mitotic spindle organization [GO:0060236]; retrograde transport, endosome to Golgi [GO:0042147]; ventral spinal cord development [GO:0021517]
|
axon [GO:0030424]; cell cortex [GO:0005938]; cell cortex region [GO:0099738]; cell leading edge [GO:0031252]; cell tip [GO:0051286]; centriolar subdistal appendage [GO:0120103]; centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytoplasmic dynein complex [GO:0005868]; cytosol [GO:0005829]; intercellular bridge [GO:0045171]; kinetochore [GO:0000776]; microtubule associated complex [GO:0005875]; microtubule plus-end [GO:0035371]; mitotic spindle [GO:0072686]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; protein-containing complex [GO:0032991]; retromer complex [GO:0030904]; spindle [GO:0005819]; spindle pole [GO:0000922]
|
identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; microtubule plus-end binding [GO:0051010]; molecular adaptor activity [GO:0060090]; protein kinase binding [GO:0019901]
|
PF01302;PF12455;
|
2.30.30.190;
|
Dynactin 150 kDa subunit family
|
PTM: Ubiquitinated by a SCF complex containing FBXL5, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q14203}.; PTM: Phosphorylation by SLK at Thr-145, Thr-146 and Thr-147 targets DCTN1 to the centrosome. It is uncertain if SLK phosphorylates all three threonines or one or two of them. PLK1-mediated phosphorylation at Ser-179 is essential for its localization in the nuclear envelope and promotes its dissociation from microtubules during early mitosis and positively regulates nuclear envelope breakdown during prophase. {ECO:0000250|UniProtKB:Q14203}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16954346}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23386061}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q14203}. Nucleus envelope {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q14203}. Note=Localizes to microtubule plus ends. Localizes preferentially to the ends of tyrosinated microtubules (PubMed:16954346). Localization at centrosome is regulated by SLK-dependent phosphorylation. Localizes to centrosome in a PARKDA-dependent manner. PLK1-mediated phosphorylation at Ser-179 is essential for its localization in the nuclear envelope (By similarity). Localizes to the subdistal appendage region of the centriole in a KIF3A-dependent manner (PubMed:23386061). {ECO:0000250|UniProtKB:Q14203, ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:23386061}.
| null | null | null | null | null |
FUNCTION: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule. Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon. Plays a role in metaphase spindle orientation. Plays a role in centriole cohesion and subdistal appendage organization and function. Its recruitment to the centriole in a KIF3A-dependent manner is essential for the maintenance of centriole cohesion and the formation of subdistal appendage. Also required for microtubule anchoring at the mother centriole. Plays a role in primary cilia formation (By similarity). {ECO:0000250|UniProtKB:A0A287B8J2, ECO:0000250|UniProtKB:Q14203}.
|
Mus musculus (Mouse)
|
O08789
|
MNT_MOUSE
|
MSIETLLEAARFLEWQAQQQQRAREEQERLRLEREREREQEQKRASNLARLAHALPVEEPRIEAPPLPLSPPAPPPAPPPPLATPAPLTVIPIPVVTNSPQSLPPPPPLPPAAQPLPLAPRQPALVSTPGLSIKEPVTLPTRPQVPTPAPLLPDAKTTVAPTGSPKPLQPLPAPILTIAPHPGVQPQLAPQQPPPPTLGTLKLAPAEEAKSSEQKKRPGGIGTREVHNKLEKNRRAHLKECFETLKRNIPNVDDKKTSNLSVLRTALRYIQSLKRKEKEYEHEMERLAREKIATQQRLAELKHELSQWMDVLEIDRVLRQTGQPEDDQASTSTASEGEDNVDEEMEGDRAGLGPPKLNHRPQPELLKSALPTPSTAPAPLPTHPHPHPHPVALSPAHLPVQQQQPPQQKTPLPAPPPPPATPTQTLVPAPAHLVATAGGGSTVIAHTATTHASVIQTVNHVLQGPGGKHIAHIAPSAPSPAVQLAPATPPIGHITVHPATLNHVAHLGSQLPLYPQPVAVSQPVAVSHIAHTLSHQQVNGTAGLGPPATVMAKPAVGAQVVHHPQLVGQTVLNPVTMVTMPSFPVSTLKLA
| null | null |
cellular senescence [GO:0090398]; negative regulation of apoptotic signaling pathway [GO:2001234]; regulation of cell cycle [GO:0051726]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; identical protein binding [GO:0042802]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00010;
|
4.10.280.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Binds DNA as a heterodimer with MAX and represses transcription. Binds to the canonical E box sequence 5'-CACGTG-3' and, with higher affinity, to 5'-CACGCG-3'.
|
Mus musculus (Mouse)
|
O08790
|
FPRS1_MOUSE
|
METNYSIPLNGSDVVIYDSTISRVLWILSMVVVSITFFLGVLGNGLVIWVAGFRMPHTVTTIWYLNLALADFSFTATLPFLLVEMAMKEKWPFGWFLCKLVHIAVDVNLFGSVFLIAVIALDRCICVLHPVWAQNHRTVSLARNVVVGSWIFALILTLPLFLFLTTVRDARGDVHCRLSFVSWGNSVEERLNTAITFVTTRGIIRFIVSFSLPMSFVAICYGLITTKIHKKAFVNSSRPFRVLTGVVASFFICWFPFQLVALLGTVWLKEMQFSGSYKIIGRLVNPTSSLAFFNSCLNPILYVFMGQDFQERLIHSLSSRLQRALSEDSGHISDTRTNLASLPEDIEIKAI
| null | null |
chemotaxis [GO:0006935]; complement receptor mediated signaling pathway [GO:0002430]; G protein-coupled receptor signaling pathway [GO:0007186]; inflammatory response [GO:0006954]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of cytosolic calcium ion concentration [GO:0007204]
|
plasma membrane [GO:0005886]
|
complement receptor activity [GO:0004875]; N-formyl peptide receptor activity [GO:0004982]; RAGE receptor binding [GO:0050786]; signaling receptor activity [GO:0038023]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Low affinity receptor for N-formyl-methionyl peptides. Receptor for lipoxin A4. May have an olfactory function associated with the identification of pathogens or of pathogenic states. {ECO:0000269|PubMed:19387439}.
|
Mus musculus (Mouse)
|
O08791
|
COE3_MOUSE
|
MFGIQENIPRGGTTMKEEPLGSGMNPVRSWMHTAGVVDANTAAQSGVGLARAHFEKQPPSNLRKSNFFHFVLALYDRQGQPVEIERTAFVDFVEKEKEPNNEKTNNGIHYKLQLLYSNGVRTEQDLYVRLIDSMTKQAIVYEGQDKNPEMCRVLLTHEIMCSRCCDKKSCGNRNETPSDPVIIDRFFLKFFLKCNQNCLKNAGNPRDMRRFQVVVSTTVNVDGHVLAVSDNMFVHNNSKHGRRARRLDPSEGTAPSYLENATPCIKAISPSEGWTTGGATVIIIGDNFFDGLQVVFGTMLVWSELITPHAIRVQTPPRHIPGVVEVTLSYKSKQFCKGAPGRFVYTALNEPTIDYGFQRLQKVIPRHPGDPERLPKEVLLKRAADLVEALYGMPHNNQEIILKRAADIAEALYSVPRNHNQIPTLGNTPAHTGMMGVNSFSSQLAVNVSETSQANDQVGYSRNTSSVSPRGYVPSSTPQQSNYNTVSTSMNGYGSGAMANLGVPGSPGFLNGSSANSPYGIVPSSPTMAASSVTLPSNCSSTHGIFSFSPANVISAVKQKSAFAPVVRPQASPPPSCTSANGNGLQAMSGLVVPPM
| null | null |
positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF16422;PF16423;PF01833;
|
1.10.287.4280;2.60.40.10;2.60.40.3180;
|
COE family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H4W6}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator (PubMed:9151732). Recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3' (By similarity). {ECO:0000250|UniProtKB:Q07802, ECO:0000269|PubMed:9151732}.
|
Mus musculus (Mouse)
|
O08792
|
COE2_MOUSE
|
MFGIQDTLGRGPALKDKSLGAEMDSVRSWVRNVGVVDANVAAQSGVALSRAHFEKQPPSNLRKSNFFHFVLALYDRQGQPVEIERTAFVDFVENDKEQGNEKTNNGTHYKLQLLYSNGVRTEQDLYVRLIDSVTKQPIAYEGQNKNPEMCRVLLTHEVMCSRCCEKKSCGNRNETPSDPVIIDRFFLKFFLKCNQNCLKTAGNPRDMRRFQVVLSTTVNVDGHVLAVSDNMFVHNNSKHGRRARRLDPSEATPCIKAISPSEGWTTGGAMVIIIGDNFFDGLQVVFGTMLVWSELITPHAIRVQTPPRHIPGVVEVTLSYKSKQFCKGAPGRFIYTALNEPTIDYGFQRLQKVIPRHPGDPERLAKEMLLKRAADLVEALYGTPHNNQDIILKRAADIAEALYSVPRNPSQIPALSSSPAHSGMMGINSYGSQLGVSISESTQGNNQGYIRNTSSISPRGYSSSSTPQQSNYSTSSNSMNGYSNVPMANLGVPGSPGFLNGSPTGSPYGIMSSSPTVGSSSTSSILPFSSSVFPAVKQKSAFAPVIRPQGSPSPACSSGNGNGFRAMTGLVVPPM
| null | null |
adipose tissue development [GO:0060612]; brown fat cell differentiation [GO:0050873]; cell fate determination [GO:0001709]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF16422;PF16423;PF01833;
|
1.10.287.4280;2.60.40.10;2.60.40.3180;
|
COE family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Transcription factor that, in osteoblasts, activates the decoy receptor for RANKL, TNFRSF11B, which in turn regulates osteoclast differentiation. Acts in synergy with the Wnt-responsive LEF1/CTNNB1 pathway. Recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3'. {ECO:0000269|PubMed:16326388}.
|
Mus musculus (Mouse)
|
O08795
|
GLU2B_MOUSE
|
MLLLLLLLLPLCWAVEVKRPRGVSLSNHHFYEESKPFTCLDGTATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYILSSRVNDGVCDCCDGTDEYNSGTVCENTCREKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAERPEKEAKDQHRKLWEEQQAAAKARREQERAASAFQELDDNMDGMVSLAELQTHPELDTDGDGALSEEEAQALLSGDTQTDTTSFYDRVWAAIRDKYRSEVPPTDIPVPEETEPKEEKPPVLPPTEEEEEEEEEPEEEEEEEEEEEEAPPPLQPPQPPSPTEDEKMPPYDEETQAIIDAAQEARSKFEEVERSLKEMEESIRSLEQEISFDFGPSGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPKHGGSPTSLGTWGSWAGPDHDKFSAMKYEQGTGCWQGPNRSTTVRLLCGKETVVTSTTEPSRCEYLMELMTPAACPEPPPEAPSDGDHDEL
| null | null |
in utero embryonic development [GO:0001701]; liver development [GO:0001889]; N-glycan processing [GO:0006491]; negative regulation of neuron projection development [GO:0010977]
|
endoplasmic reticulum [GO:0005783]; glucosidase II complex [GO:0017177]; intracellular membrane-bounded organelle [GO:0043231]
|
calcium ion binding [GO:0005509]; protein-containing complex binding [GO:0044877]; RNA binding [GO:0003723]
|
PF13202;PF12999;PF13015;
|
1.10.238.10;4.10.400.10;2.70.130.10;
| null | null |
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138}.
| null | null |
PATHWAY: Glycan metabolism; N-glycan metabolism. {ECO:0000269|PubMed:27462106}.
| null | null |
FUNCTION: Regulatory subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (PubMed:27462106, PubMed:9148925). Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane of the primary cilia (PubMed:21685914). {ECO:0000269|PubMed:21685914, ECO:0000269|PubMed:27462106, ECO:0000269|PubMed:9148925}.
|
Mus musculus (Mouse)
|
O08796
|
EF2K_MOUSE
|
MADEDLIFCLEGVDGGRCSRAGHNADSDTDSDDDEGYFICPITDDHMSNQNVSSKVQSYYSNLTKTECGSTGSPASSFHFKEAWKHAIEKAKHMPDPWAEFHLEDIATEHATRHRYNAVTGEWLKDEVLIKMASQPFGRGAMRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRSVYFEDVQLQMEAKLWGEDYNRHKPPKQVDIMQMCIIELKDRPGQPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTEKGTDFGDGNLGVRGMALFFYSHACNRICQSMGLTPFDLSPREQDAVNQSTRLLQSAKTILRGTEEKCGSPRIRTLSSSRPPLLLRLSENSGDENMSDVTFDSLPSSPSSATPHSQKLDHLHWPVFGDLDNMGPRDHDRMDNHRDSENSGDSGYPSEKRSDLDDPEPREHGHSNGNRRHESDEDSLGSSGRVCVETWNLLNPSRLHLPRPSAVALEVQRLNALDLGRKIGKSVLGKVHLAMVRYHEGGRFCEKDEEWDRESAIFHLEHAADLGELEAIVGLGLMYSQLPHHILADVSLKETEENKTKGFDYLLKAAEAGDRHSMILVARAFDTGLNLSPDRCQDWSEALHWYNTALETTDCDEGGEYDGIQDEPQYALLAREAEMLLTGGFGLDKNPQRSGDLYTQAAEAAMEAMKGRLANQYYEKAEEAWAQMEE
|
2.7.11.20
| null |
cellular response to anoxia [GO:0071454]; cellular response to brain-derived neurotrophic factor stimulus [GO:1990416]; cellular response to calcium ion [GO:0071277]; cellular response to cAMP [GO:0071320]; cellular response to insulin stimulus [GO:0032869]; myosin II filament disassembly [GO:0031037]; negative regulation of apoptotic process [GO:0043066]; phosphorylation [GO:0016310]; positive regulation of dendritic spine morphogenesis [GO:0061003]; positive regulation of endocytosis [GO:0045807]; positive regulation of synapse assembly [GO:0051965]; regulation of protein autophosphorylation [GO:0031952]; regulation of translation at postsynapse [GO:0140245]; response to differentiation-inducing factor 1 [GO:1903013]; response to ischemia [GO:0002931]; response to prolactin [GO:1990637]; translational elongation [GO:0006414]
|
actomyosin contractile ring [GO:0005826]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; postsynaptic density [GO:0014069]
|
ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; elongation factor-2 kinase activity [GO:0004686]; myosin heavy chain kinase activity [GO:0016905]; translation factor activity, RNA binding [GO:0008135]
|
PF02816;
|
3.20.200.10;1.25.40.10;
|
Protein kinase superfamily, Alpha-type protein kinase family
|
PTM: Autophosphorylated at multiple residues, Thr-347 being the major site. Phosphorylated by AMP-activated protein kinase AMPK at Ser-397 leading to EEF2K activation and protein synthesis inhibition. Phosphorylated by TRPM7 at Ser-77 resulting in improved protein stability, higher EE2F phosphorylated and subsequently reduced rate of protein synthesis. Phosphorylation by other kinases such as CDK1 and MAPK13 at Ser-358 or RPS6KA1 and RPS6KB1 at Ser-365 instead decrease EEF2K activity and promote protein synthesis (By similarity). {ECO:0000250}.
| null |
CATALYTIC ACTIVITY: Reaction=[translation elongation factor 2] + ATP = [translation elongation factor 2]-phosphate + ADP + H(+); Xref=Rhea:RHEA:21436, Rhea:RHEA-COMP:11268, Rhea:RHEA-COMP:11269, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.20; Evidence={ECO:0000269|PubMed:34815424, ECO:0000269|PubMed:9144159};
| null | null | null | null |
FUNCTION: Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation (PubMed:34815424, PubMed:9144159). Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive (PubMed:34815424, PubMed:9144159). In turn, the rate of protein synthesis is reduced (PubMed:34815424, PubMed:9144159). {ECO:0000269|PubMed:34815424, ECO:0000269|PubMed:9144159}.
|
Mus musculus (Mouse)
|
O08807
|
PRDX4_MOUSE
|
MEARSKLLDGTTASRRWTRKLVLLLPPLLLFLLRTESLQGLESDERFRTRENECHFYAGGQVYPGEASRVSVADHSLHLSKAKISKPAPYWEGTAVINGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRIEEFKSINTEVVACSVDSQFTHLAWINTPRRQGGLGPIRIPLLSDLNHQISKDYGVYLEDSGHTLRGLFIIDDKGVLRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWKPGSETIIPDPAGKLKYFDKLN
|
1.11.1.24
| null |
cell redox homeostasis [GO:0045454]; cellular response to stress [GO:0033554]; extracellular matrix organization [GO:0030198]; hydrogen peroxide catabolic process [GO:0042744]; male gonad development [GO:0008584]; negative regulation of male germ cell proliferation [GO:2000255]; protein maturation by protein folding [GO:0022417]; reactive oxygen species metabolic process [GO:0072593]; response to oxidative stress [GO:0006979]; spermatogenesis [GO:0007283]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; smooth endoplasmic reticulum [GO:0005790]
|
identical protein binding [GO:0042802]; molecular sequestering activity [GO:0140313]; thioredoxin peroxidase activity [GO:0008379]
|
PF10417;PF00578;
|
3.40.30.10;
|
Peroxiredoxin family, AhpC/Prx1 subfamily
|
PTM: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) and sulphonic acid (C(P)-SO3H) instead of its condensation to a disulfide bond. {ECO:0000250|UniProtKB:Q13162}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13162}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q13162}. Note=Not secreted. {ECO:0000269|PubMed:11229364}.
|
CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000250|UniProtKB:Q13162};
| null | null | null | null |
FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events (PubMed:11229364). Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q13162, ECO:0000269|PubMed:11229364}.
|
Mus musculus (Mouse)
|
O08808
|
DIAP1_MOUSE
|
MEPSGGGLGPGRGTRDKKKGRSPDELPATGGDGGKHKKFLERFTSMRIKKEKEKPNSAHRNSSASYGDDPTAQSLQDISDEQVLVLFEQMLVDMNLNEEKQQPLREKDIVIKREMVSQYLHTSKAGMNQKESSRSAMMYIQELRSGLRDMHLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLHDEKEETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDAAKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTSIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQELREIENEDMKVQLCVFDEQGDEDFFDLKGRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEECVSQIVLHKNGTDPDFKCRHLQIDIERLVDQMIDKTKVEKSEAKATELEKKLDSELTARHELQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASLSAVVVAPSVSSSAAVPPAPPLPGDSGTVIPPPPPPPPLPGGVVPPSPPLPPGTCIPPPPPLPGGACIPPPPQLPGSAAIPPPPPLPGVASIPPPPPLPGATAIPPPPPLPGATAIPPPPPLPGGTGIPPPPPPLPGSVGVPPPPPLPGGPGLPPPPPPFPGAPGIPPPPPGMGVPPPPPFGFGVPAAPVLPFGLTPKKVYKPEVQLRRPNWSKFVAEDLSQDCFWTKVKEDRFENNELFAKLTLAFSAQTKTSKAKKDQEGGEEKKSVQKKKVKELKVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEEYDDLAESEQFGVVMGTVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLRDTKSADQKMTLLHFLAELCENDHPEVLKFPDELAHVEKASRVSAENLQKSLDQMKKQIADVERDVQNFPAATDEKDKFVEKMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRRETEEKMRRAKLAKEKAEKERLEKQQKREQLIDMNAEGDETGVMDSLLEALQSGAAFRRKRGPRQVNRKAGCAVTSLLASELTKDDAMAPGPVKVPKKSEGVPTILEEAKELVGRAS
| null | null |
actin cytoskeleton organization [GO:0030036]; actin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; axon midline choice point recognition [GO:0016199]; brain development [GO:0007420]; cytoskeleton organization [GO:0007010]; ephrin receptor signaling pathway [GO:0048013]; gene expression [GO:0010467]; multicellular organismal locomotion [GO:0071965]; negative regulation of neuron projection regeneration [GO:0070571]; neuron projection development [GO:0031175]; neuron projection retraction [GO:0106028]; positive regulation of cell migration [GO:0030335]; protein localization [GO:0008104]; regulation of cell shape [GO:0008360]; regulation of microtubule-based process [GO:0032886]; sensory perception of sound [GO:0007605]; synaptic vesicle endocytosis [GO:0048488]
|
actin filament [GO:0005884]; brush border [GO:0005903]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; neuron projection [GO:0043005]; nucleus [GO:0005634]; presynapse [GO:0098793]; ruffle membrane [GO:0032587]; spindle [GO:0005819]
|
actin binding [GO:0003779]; identical protein binding [GO:0042802]; profilin binding [GO:0005522]; small GTPase binding [GO:0031267]; transmembrane transporter binding [GO:0044325]
|
PF06346;PF06367;PF06371;PF02181;
|
1.20.1170.10;1.20.58.630;6.10.30.30;1.10.20.40;1.20.58.2220;1.10.238.150;1.25.10.10;
|
Formin homology family, Diaphanous subfamily
|
PTM: Phosphorylation at Thr-751 is stimulated by cAMP and regulates stability, complex formation and mitochondrial movement (By similarity). {ECO:0000250|UniProtKB:O60610}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9214622}. Cell projection, ruffle membrane {ECO:0000269|PubMed:9214622}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9214622}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O60610}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O60610}. Cytoplasm {ECO:0000269|PubMed:23558171}. Nucleus {ECO:0000269|PubMed:23558171}. Note=Membrane ruffles, especially at the tip of ruffles, of motile cells. {ECO:0000269|PubMed:9214622}.
| null | null | null | null | null |
FUNCTION: Actin nucleation and elongation factor required for the assembly of F-actin structures, such as actin cables and stress fibers (PubMed:10678165, PubMed:15044801, PubMed:18572016, PubMed:23558171). Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization (PubMed:10678165, PubMed:15044801, PubMed:18572016). Required for cytokinesis, and transcriptional activation of the serum response factor (PubMed:10678165, PubMed:15044801, PubMed:18572016). DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics (PubMed:10678165, PubMed:15044801, PubMed:18572016). Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration (PubMed:15311282). Has neurite outgrowth promoting activity (PubMed:10678165, PubMed:15044801, PubMed:18572016). Acts in a Rho-dependent manner to recruit PFY1 to the membrane (PubMed:9214622). The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (By similarity). It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity (By similarity). In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Required in the control of cell shape (By similarity). Also acts as an actin nucleation and elongation factor in the nucleus by promoting nuclear actin polymerization inside the nucleus to drive serum-dependent SRF-MRTFA activity (PubMed:23558171). {ECO:0000250|UniProtKB:O60610, ECO:0000269|PubMed:10678165, ECO:0000269|PubMed:15044801, ECO:0000269|PubMed:15311282, ECO:0000269|PubMed:18572016, ECO:0000269|PubMed:23558171, ECO:0000269|PubMed:9214622}.
|
Mus musculus (Mouse)
|
O08811
|
ERCC2_MOUSE
|
MKLNVDGLLVYFPYDYIYPEQFSYMLELKRTLDAKGHGVLEMPSGTGKTVSLLALIVAYQRAYPLEVTKLIYCSRTVPEIEKVIEELRKLLSFYEQQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQQDASLPHCRFYEEFDIHGRQMPLPAGIYNLDDLKALGQRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQSNLDTLQKTVLRIKETDEQRLRDEYRRLVEGLREASVARETDAHLANPVLPDEVLQEAVPGSIRTAEHFLGFLRRLLEYVKWRLRVQHVVQESPPAFLSGLAQRVCIQRKPLRFCAERLRSLLHTLEIADLADFSPLTLLANFATLVSTYAKGFTIIIEPFDDRTPTIANPVLHFSCMDASLAIKPVFERFQSVIITSGTLSPLDIYPKILDFHPVTMATFTMTLARVCLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFTSYQYMESTVASWYEQGILENIQRNKLLFIETQDGAETSVALEKYQEACENGRGAILLSVARGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKARLEYLRDQFQIRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFARADKRGKLPRWIQEHLTDSNLNLTVDEGVQVAKYFLRQMAQPFHREDQLGLSLLSLEQLQSEETLQRIEQIAQQL
|
3.6.4.12
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
|
apoptotic process [GO:0006915]; bone mineralization [GO:0030282]; central nervous system myelin formation [GO:0032289]; chromosome segregation [GO:0007059]; determination of adult lifespan [GO:0008340]; DNA repair [GO:0006281]; embryonic cleavage [GO:0040016]; embryonic organ development [GO:0048568]; erythrocyte maturation [GO:0043249]; extracellular matrix organization [GO:0030198]; hair cell differentiation [GO:0035315]; hair cycle process [GO:0022405]; hair follicle maturation [GO:0048820]; hematopoietic stem cell differentiation [GO:0060218]; hematopoietic stem cell proliferation [GO:0071425]; in utero embryonic development [GO:0001701]; insulin-like growth factor receptor signaling pathway [GO:0048009]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; multicellular organism growth [GO:0035264]; nucleotide-excision repair [GO:0006289]; positive regulation of mitotic recombination [GO:0045951]; post-embryonic development [GO:0009791]; regulation of mitotic cell cycle phase transition [GO:1901990]; regulation of transcription by RNA polymerase II [GO:0006357]; response to hypoxia [GO:0001666]; response to oxidative stress [GO:0006979]; response to UV [GO:0009411]; ribosomal small subunit biogenesis [GO:0042274]; skin development [GO:0043588]; spinal cord development [GO:0021510]; transcription by RNA polymerase II [GO:0006366]; transcription elongation by RNA polymerase I [GO:0006362]; transcription initiation at RNA polymerase II promoter [GO:0006367]; transcription-coupled nucleotide-excision repair [GO:0006283]; UV protection [GO:0009650]
|
CAK-ERCC2 complex [GO:0070516]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; MMXD complex [GO:0071817]; nucleus [GO:0005634]; spindle [GO:0005819]; transcription factor TFIID complex [GO:0005669]; transcription factor TFIIH core complex [GO:0000439]; transcription factor TFIIH holo complex [GO:0005675]
|
4 iron, 4 sulfur cluster binding [GO:0051539]; 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; damaged DNA binding [GO:0003684]; DNA helicase activity [GO:0003678]; metal ion binding [GO:0046872]; protein-macromolecule adaptor activity [GO:0030674]
|
PF06733;PF06777;PF13307;
|
3.40.50.300;
|
Helicase family, RAD3/XPD subfamily
|
PTM: ISGylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
| null | null | null | null |
FUNCTION: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/ERCC2 is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. XPD/ERCC2 acts by forming a bridge between CAK and the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers. {ECO:0000250|UniProtKB:P18074}.
|
Mus musculus (Mouse)
|
O08812
|
CTR3_RAT
|
MLWQALRRFGQKLVRRRLLELGMGETRLARCLSTLDLVALGVGSTLGAGVYVLAGEVAKEKAGPSIVICFLVAALSSVLAGLCYAEFGARVPGSGSAYLYSYVTVGELWAFTTGWNLILSYVIGTASVARAWSSAFDNLIGNHISQTLKGTILLNMPHVLAEYPDFFALALVLLLTGLLVLGANESGLVTKVFTGMNLLVLGFVIISGFIKGELRNWKLTKEDYCLTMSESNGTCSLDSMGSGGFMPFGLEGILRGAATCFYAFVGFDCIATTGEEAQNPQRSIPMGIVISLSICFLAYFGVSSALTLMMPYYKLQPESPLPEAFTYVGWEPARYLVAIGSLCALSTSLLGSMFPMPRVIYAMAEDGLLFRVLARVHNGTHTPIVATVVSGVIAAFMAFLFELTDLVDLMSIGTLLAYSLVSICVLILRYQPDQEMKNGEEEVELQEERTLEAEKLTVQALFCQVDSIPTLLSGRIVYVCSSLLAVLLTVLCLVLTWWTTPLHSGDPVWVTVVVLILGLILGISGVIWRQPQNRTPLHFKVPVVPLLPLVSIFVNVYLMMQMTADTWARFGVWMLIGFAIYFGYGIQHSVEEVKNHQTLPKTRPQTIDLDLTTSCVHSI
| null | null |
basic amino acid transmembrane transport [GO:1990822]; L-arginine import across plasma membrane [GO:0097638]; L-arginine transmembrane transport [GO:1903826]; L-lysine import across plasma membrane [GO:0097639]; L-lysine transmembrane transport [GO:1903401]; L-ornithine import across plasma membrane [GO:0097640]; L-ornithine transmembrane transport [GO:1903352]; lysine transport [GO:0015819]; ornithine transport [GO:0015822]; regulation of TOR signaling [GO:0032006]
|
plasma membrane [GO:0005886]
|
basic amino acid transmembrane transporter activity [GO:0015174]; L-arginine transmembrane transporter activity [GO:0061459]; L-lysine transmembrane transporter activity [GO:0015189]; L-ornithine transmembrane transporter activity [GO:0000064]
|
PF13520;PF13906;
|
1.20.1740.10;
|
Amino acid-polyamine-organocation (APC) superfamily, Cationic amino acid transporter (CAT) (TC 2.A.3.3) family
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8WY07}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=L-arginine(in) = L-arginine(out); Xref=Rhea:RHEA:32143, ChEBI:CHEBI:32682; Evidence={ECO:0000269|PubMed:9079705}; CATALYTIC ACTIVITY: Reaction=L-lysine(in) = L-lysine(out); Xref=Rhea:RHEA:70935, ChEBI:CHEBI:32551; Evidence={ECO:0000269|PubMed:9079705}; CATALYTIC ACTIVITY: Reaction=L-ornithine(in) = L-ornithine(out); Xref=Rhea:RHEA:71199, ChEBI:CHEBI:46911; Evidence={ECO:0000269|PubMed:9079705};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=103 uM for L-arginine {ECO:0000269|PubMed:9079705}; KM=147 uM for L-lysine {ECO:0000269|PubMed:9079705}; KM=219 uM for L-ornithine {ECO:0000269|PubMed:9079705};
| null | null | null |
FUNCTION: Uniporter that mediates the uptake of cationic L-amino acids such as L-arginine, L-lysine and L-ornithine (PubMed:9079705). The transport is sodium ions- and pH-independent, moderately trans-stimulated and is mediated by passive diffusion (PubMed:9079705). {ECO:0000269|PubMed:9079705}.
|
Rattus norvegicus (Rat)
|
O08815
|
SLK_RAT
|
MSFFNFRKIFKLGSEKKKKQYEHVKRDLNPEEFWEIIGELGDGAFGKVYKAQNKETNVLAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVDAVMLELERPLTESQIQVVCKQTLEALNYLHDNKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTIQRRDSFIGTPYWMAPEVVMCETSKDRPYDYKADVWSLGITLIEMAEIEPPHHELNPMRVLLKIAKSEPPTLAQPSRWSSNFKDFLKKCLEKNVDARWTTSQLLQHPFVTVDSNKPVRELIAEAKAEVTEEVEDGKEEDDDDETESALPIPANKRASSDLSIASSEEDKLSQNACILESVSERTEHNTSGDKFSNKVLSEKPTPEGPEKTVDVDGPANDVNLETVAEPNDQAVGFHENGREKKRPQLESQPDTEDQQTVDVNLVGEGNDSNIVILETNTDCLKPEEDRNEENQEIIENKLTQSEEIKDIHIQTMDLVSQETGEKEADFQAIDNEVGFTKEETQEKLGKDDKTHKVVISDITSEVGTDEPPGDTQKSAEQSQDAEGGAGEEAPEPAQTLTEKATEGPEAHGAEEEPRSGERVEDKQLEQQSAVCEGEGQVTSTSESTRATTEEPETDEVDQVSESNSIEELERLGVTGAEEQALGSKGEAATELDLEREENAQELPVKAEPQAPAASQASEPPPVLIPSINIHSENTENKGEMGALPKPETILPPEPENGKGNDTDSGTGSTVENSSSDLNLSISSFLSKTKDSGSVSLQETRRQKKTLKKTRKFIVDGVEVSVTTSKIVTDSDSKTEELRFLRRQELRELRLLQKEEQKAQQQLNGKLQQQREQIFRRFEQEMLSKKRQYDQEIENLEKQQKQTIERLEQEHTNRLRDEAKRIKGEQEKELSKFQNMLRNRKKEEQEFVQKQQQELDGALKKIIQQQKAELANIERECLNNKQQLLRAREAAIWELEERHLQEKHQLLKQQLKDQYFIQRHQLLKRHEKETEQMQRYNQRLIEELKNRQTQERARLPKIQRSEAKTRMAMFKKSLRINSTATPDQDREKIKQFAAQEEKRQKNERMAQHQKHESQMRDLQLQCEANVRELHQLQNEKCHLLVEHETQKLKELDEEHSQELKEWREKLRPRKKTLEEEFARKLQEQEVFFKMTGESECLNPSAQSRGCLQTSHPSSTRAPAWAG
|
2.7.11.1
| null |
apoptotic process [GO:0006915]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; cytoplasmic microtubule organization [GO:0031122]; phosphorylation [GO:0016310]; positive regulation of apoptotic process [GO:0043065]; regulation of apoptotic process [GO:0042981]; regulation of cell migration [GO:0030334]; regulation of focal adhesion assembly [GO:0051893]
|
cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; perinuclear region of cytoplasm [GO:0048471]
|
ATP binding [GO:0005524]; histone kinase activity [GO:0035173]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;PF12474;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
|
PTM: Proteolytically cleaved by caspase-3. {ECO:0000250}.; PTM: Autophosphorylated.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Mediates apoptosis and actin stress fiber dissolution. {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O08816
|
WASL_RAT
|
MSSGQQPPRRVTNVGSLLLTPQENESLFSFLGKKCVTMSSAVVQLYAADRNCMWSKKCSGVACLVKDNPQRSYFLRIFDIKDGKLLWEQELYNNFVYNSPRGYFHTFAGDTCQVALNFANEEEAKKFRKAVTDLLGRRQRKSEKRRDAPNGPNLPMATVDIKNPEITTNRFYSSQVNNISHTKEKKKGKAKKKRLTKADIGTPSNFQHIGHVGWDPNTGFDLNNLDPELKNLFDMCGISEAQLKDRETSKVIYDFIEKTGGVEAVKNELRRQAPPPPPPSRGGPPPPPPPPHSSGPPPPPARGRGAPPPPPSRAPTAAPPPPPPSRPGVVVPPPPPNRMYPPPPPALPSSAPSGPPPPPPLSMAGSTAPPPPPPPPPPPGPPPPPGLPSDGDHQVPASSGNKAALLDQIREGAQLKKVEQNSRPVSCSGRDALLDQIRQGIQLKSVSDGQESTPPTPAPTSGIVGALMEVMQKRSKAIHSSDEDEDDDDEEDFQDDDEWED
| null | null |
actin cytoskeleton organization [GO:0030036]; actin filament polymerization [GO:0030041]; cell division [GO:0051301]; dendritic spine morphogenesis [GO:0060997]; membrane invagination [GO:0010324]; negative regulation of lymphocyte migration [GO:2000402]; negative regulation of membrane tubulation [GO:1903526]; plasma membrane tubulation [GO:0097320]; positive regulation of chemotaxis [GO:0050921]; positive regulation of clathrin-dependent endocytosis [GO:2000370]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of transcription by RNA polymerase II [GO:0045944]; postsynapse organization [GO:0099173]; postsynaptic actin cytoskeleton organization [GO:0098974]; protein-containing complex localization [GO:0031503]; regulation of cell projection assembly [GO:0060491]; regulation of postsynapse organization [GO:0099175]; regulation of protein localization [GO:0032880]; response to bacterium [GO:0009617]; spindle localization [GO:0051653]; vesicle budding from membrane [GO:0006900]; vesicle organization [GO:0016050]; vesicle transport along actin filament [GO:0030050]
|
actin cap [GO:0030478]; cell leading edge [GO:0031252]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; Golgi membrane [GO:0000139]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; postsynapse [GO:0098794]
|
actin binding [GO:0003779]; cytoskeletal protein binding [GO:0008092]; identical protein binding [GO:0042802]
|
PF00786;PF00568;PF02205;
|
3.90.810.10;2.30.29.30;
| null |
PTM: Phosphorylation at Ser-239, Tyr-253, Ser-480 and Ser-481 enhances actin polymerization activity. {ECO:0000250|UniProtKB:O00401}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14676198}. Nucleus {ECO:0000269|PubMed:14676198}. Cytoplasm {ECO:0000250|UniProtKB:Q91YD9}. Note=Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated (By similarity). Exported from the nucleus by an nuclear export signal (NES)-dependent mechanism to the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q91YD9}.
| null | null | null | null | null |
FUNCTION: Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Involved in various processes, such as mitosis and cytokinesis, via its role in the regulation of actin polymerization. Together with CDC42, involved in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. In addition to its role in the cytoplasm, also plays a role in the nucleus by regulating gene transcription, probably by promoting nuclear actin polymerization (By similarity). Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. Plays a role in dendrite spine morphogenesis (By similarity). {ECO:0000250|UniProtKB:O00401, ECO:0000250|UniProtKB:Q91YD9}.
|
Rattus norvegicus (Rat)
|
O08832
|
GALT4_MOUSE
|
MAVRWTWAGKSCLLLALLTLAYILVEFSVSTLYASPGAGGARELGPRRLPDLDTREEDLSQPLYIKPPADSHALGEWGRASKLQLNEGELKQQEELIERYAINIYLSDRISLHRHIEDKRMYECKAKKFHYRSLPTTSVIIAFYNEAWSTLLRTIHSVLETSPAVLLKEIILVDDLSDRIYLKAQLETYISNLERVRLIRTNKREGLVRARLIGATFATGDVLTFLDCHCECNTGWLEPLLERISRDETAIVCPVIDTIDWNTFEFYMQTGEPMIGGFDWRLTFQWHSVPKHERDRRTSRIDPIRSPTMAGGLFAVSKKYFQYLGTYDTGMEVWGGENLELSFRVWQCGGKLEIHPCSHVGHVFPKRAPYARPNFLQNTARAAEVWMDEYKEHFYNRNPPARKEAYGDLSERKLLRERLKCKSFDWYLKNVFSNLHVPEDRPGWHGAIRSMGISSECLDYNAPDNNPTGANLSLFGCHGQGGNQFFEYTSNKEIRFNSVTELCAEVPQQKDYVGMQNCPKDGLPVPVNIIWHFKEDGTIFHPHTRLCLSAYRTAEGRPSVHMKTCDALDKNQLWRFEK
|
2.4.1.41
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8N4A0};
|
protein O-linked glycosylation [GO:0006493]; protein O-linked glycosylation via serine [GO:0018242]; protein O-linked glycosylation via threonine [GO:0018243]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; perinuclear region of cytoplasm [GO:0048471]
|
carbohydrate binding [GO:0030246]; manganese ion binding [GO:0030145]; polypeptide N-acetylgalactosaminyltransferase activity [GO:0004653]
|
PF00535;PF00652;
|
2.80.10.50;
|
Glycosyltransferase 2 family, GalNAc-T subfamily
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41; Evidence={ECO:0000269|PubMed:9153242}; CATALYTIC ACTIVITY: Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41; Evidence={ECO:0000269|PubMed:9153242};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:9153242}.
| null | null |
FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a highest activity toward EA2 peptide substrate and a much lower activity with EPO-T, Muc2, Muc1a, Muc1b. {ECO:0000269|PubMed:9153242}.
|
Mus musculus (Mouse)
|
O08835
|
SYT11_RAT
|
MAEITNIRPSFDVSPVAAGLIGASVLVVCVSVTVFVWTCCHQQAEKKHKTPPYKFIHMLKGISIYPETLSNKKKIIKVRRDKDGSHRESGRGNLLVNAESGLLSHDRDPRGPSPASCIDQLPIKRDYGEELRSPMTSLTPGESKPTSPSSPEEDVMLGSLTFSVDYNFPKKALVVTIQEAHGLPVMDGQTQGSDPYIKMTILPDKRHRVKTRVLRKTLDPVFDETFTFYGIPYSQLQDLVLHFLVLSFDRFSRDDVIGEVMVPLAGVDPSTGKVQLTRDIIKRNIQKCISRGELQVSLSYQPVAQRMTVVVLKARHLPKMDITGLSGNPYVKVNVYYGRKRIAKKKTHVKKCTLNPIFNESFIYDIPTDLLPDISIEFLVIDFDRTTKNEVVGRLILGAHSVTTSGAEHWREVCESPRKPVAKWHSLSEY
| null |
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
|
autophagy [GO:0006914]; calcium ion regulated lysosome exocytosis [GO:1990927]; calcium ion-regulated exocytosis of neurotransmitter [GO:0048791]; cellular response to calcium ion [GO:0071277]; establishment of vesicle localization [GO:0051650]; learning [GO:0007612]; memory [GO:0007613]; negative regulation of clathrin coat assembly [GO:1905444]; negative regulation of clathrin-dependent endocytosis [GO:1900186]; negative regulation of cytokine production [GO:0001818]; negative regulation of dopamine secretion [GO:0033602]; negative regulation of endocytosis [GO:0045806]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of membrane invagination [GO:1905154]; negative regulation of microglial cell activation [GO:1903979]; negative regulation of phagocytosis [GO:0050765]; negative regulation of synaptic vesicle endocytosis [GO:1900243]; negative regulation of tumor necrosis factor production [GO:0032720]; plasma membrane repair [GO:0001778]; positive regulation of protein localization to phagocytic vesicle [GO:1905171]; regulation of calcium ion-dependent exocytosis [GO:0017158]; regulation of defense response to bacterium [GO:1900424]; regulation of dopamine secretion [GO:0014059]; regulation of synaptic vesicle endocytosis [GO:1900242]; response to wounding [GO:0009611]; vesicle fusion [GO:0006906]
|
axon [GO:0030424]; cell body [GO:0044297]; clathrin-coated vesicle membrane [GO:0030665]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; dopaminergic synapse [GO:0098691]; early phagosome [GO:0032009]; excitatory synapse [GO:0060076]; exocytic vesicle [GO:0070382]; inhibitory synapse [GO:0060077]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; neuron projection [GO:0043005]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; phagocytic cup [GO:0001891]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; presynaptic active zone membrane [GO:0048787]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]; terminal bouton [GO:0043195]; trans-Golgi network [GO:0005802]; vesicle [GO:0031982]
|
beta-tubulin binding [GO:0048487]; clathrin binding [GO:0030276]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; phosphatidylserine binding [GO:0001786]; SNARE binding [GO:0000149]; translation initiation factor binding [GO:0031369]; ubiquitin protein ligase binding [GO:0031625]
|
PF00168;
|
2.60.40.150;
|
Synaptotagmin family
|
PTM: Ubiquitinated, at least by PRKN, and targeted to the proteasome complex for degradation (PubMed:29311685). Ubiquitination is inhibited by ATP13A2 (By similarity). {ECO:0000250|UniProtKB:Q9BT88, ECO:0000269|PubMed:29311685}.
|
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9R0N3}; Single-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:Q9R0N3}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9R0N3}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9R0N3}. Recycling endosome membrane {ECO:0000269|PubMed:26589353}; Single-pass membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:Q9R0N3}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9R0N3}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q9R0N3}. Cell projection, axon {ECO:0000269|PubMed:26589353}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9R0N3}. Postsynaptic density {ECO:0000250|UniProtKB:Q9R0N3}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:26589353}; Single-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:26589353}. Note=Localized in vesicles that travels in axonal and dendritic shafts in both anterograde and retrograde directions. In macrophages and microglia, recruited in phagosomes at early stages of phagocytosis. {ECO:0000250|UniProtKB:Q9R0N3}.
| null | null | null | null | null |
FUNCTION: Synaptotagmin family member involved in vesicular and membrane trafficking which does not bind Ca(2+) (PubMed:9162066). Inhibits clathrin-mediated and bulk endocytosis in neurons, functions to ensure precision in vesicle retrieval (PubMed:26589353, PubMed:29311685). Plays an important role in dopamine transmission by regulating endocytosis and the vesicle-recycling process (PubMed:29311685). Essential component of a neuronal vesicular trafficking pathway that differs from the synaptic vesicle trafficking pathway but is crucial for development and synaptic plasticity. In macrophages and microglia, inhibits the conventional cytokine secretion, of at least IL6 and TNF, and phagocytosis. In astrocytes, regulates lysosome exocytosis, mechanism required for the repair of injured astrocyte cell membrane (By similarity). Required for the ATP13A2-mediated regulation of the autophagy-lysosome pathway (By similarity). {ECO:0000250|UniProtKB:Q9BT88, ECO:0000250|UniProtKB:Q9R0N3, ECO:0000269|PubMed:26589353, ECO:0000269|PubMed:29311685, ECO:0000269|PubMed:9162066}.
|
Rattus norvegicus (Rat)
|
O08836
|
IGBP1_RAT
|
MAASEEELLLPRLPELFETSKKLLEELEVATEPTGSRTIQDKVSKGLELLEKAAGMLSQLDLFSRNEDLEEIASIDLKYLMVPALQGALTMKQVNPSKRLDHLQRAREHFIHFLTQCHCYHVAEFQLPQTKNNSAENNTARSSMAYPNLVAMASQRQAKIERYKQKKEVEHRLSALKSAVESGQADDERVREYYLLHLRRWIGISLEEIESIDQEIKILKDKDSPREESACQSSLPEKPPMKPFILTRNKAQAKVFGTGYPSLATMTVSDWYEQHQKYGALPDRGIAKPPSADFQRAAQQQEDQEQKDEENEEKALHRMREWDDWKDTHPRGYGNRQNMG
| null | null |
B cell activation [GO:0042113]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of protein dephosphorylation [GO:0035308]; negative regulation of stress-activated MAPK cascade [GO:0032873]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of dephosphorylation [GO:0035306]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of dephosphorylation [GO:0035303]; regulation of microtubule-based movement [GO:0060632]; response to interleukin-1 [GO:0070555]; response to tumor necrosis factor [GO:0034612]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule [GO:0005874]
|
enzyme binding [GO:0019899]; mitogen-activated protein kinase kinase binding [GO:0031434]; protein domain specific binding [GO:0019904]; protein phosphatase 2A binding [GO:0051721]; protein phosphatase regulator activity [GO:0019888]; protein-containing complex binding [GO:0044877]
|
PF04177;
|
6.10.250.1140;1.25.40.540;
|
IGBP1/TAP42 family
|
PTM: Phosphorylated.; PTM: Monoubiquitination by MID1 triggers calpain-mediated cleavage and switches IGBP1 activity from protective to destructive. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Associated to surface IgM-receptor; may be involved in signal transduction. Involved in regulation of the catalytic activity of the phosphatases PP2A, PP4 and PP6 by protecting their partially folded catalytic subunits from degradative polyubiquitination until they associate with regulatory subunits (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O08837
|
CDC5L_RAT
|
MPRIMIKGGVWRNTEDEILKAAVMKYGKNQWSRIASLLHRKSAKQCKARWYEWLDPSIKKTEWSREEEEKLLHLAKLMPTQWRTIAPIIGRTAAQCLEHYEFLLDKTAQRDNEEETTDDPRKLKPGEIDPNPETKPARPDPIDMDEDELEMLSEARARLANTQGKKAKRKAREKQLEEARRLAALQKRRELRAAGIEIQKKRKKKRGVDYNAEIPFEKKPALGFYDTSEENYQALDADFRKLRQQDLDGELRSEKEGRDRKKDKQHLKRKKESDLPSAILQTSGVSEFTKKRSKLVLPAPQISDAELQEVVKVGQASEVARQTAEESGITNSASSTLLSEYNVTNNSIALRTPRTPASQDRILQEAQNLMALTNVDTPLKGGLNTPLHESDFSGVTPQRQVVQTPNTVLSTPFRTPSNGAEGLTPRSGTTPKPVTNATPGRTPLRDKLNINPEDGMADYSDPSYVKQMERESREHLRLGLLGLPAPKNDFEIVLPENAEKELEEREMDDTYIEDAADVDARKQAIRDAERVKEMKRMHKAVQKDLPRPSEVNETILRPLNVEPPLTDLQKSEELIKKEMITMLHYDLLHHPYEPSGNKKGKNVGFATNNSEHITYLEHSPYEKFSKEDLKKAQDVLVQEMEVVKQGMSHGELSSEAYNQVWEECYSQVLYLPAQSRYTRANLASKKDRIESLEKRLEINRGHMTTEAKRAAKMEKKMKILLGGYQSRAMGLLKQLNDLWDQIEQAHLELRTFEELKKHEDSAIPRRLECLKEDVQRQQEREKELQQRYADLLMEKETLQAKF
| null | null |
cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to interleukin-2 [GO:0071352]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to prolactin [GO:1990646]; cellular response to wortmannin [GO:1904568]; DNA damage checkpoint signaling [GO:0000077]; DNA repair [GO:0006281]; G2/M transition of mitotic cell cycle [GO:0000086]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]
|
catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; DNA replication factor A complex [GO:0005662]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; protein-DNA complex [GO:0032993]; Prp19 complex [GO:0000974]; spliceosomal complex [GO:0005681]; U2-type catalytic step 2 spliceosome [GO:0071007]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; leucine zipper domain binding [GO:0043522]; protein kinase binding [GO:0019901]; protein phosphatase 1 binding [GO:0008157]; RNA binding [GO:0003723]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; transcription corepressor binding [GO:0001222]; WD40-repeat domain binding [GO:0071987]
|
PF11831;PF13921;
|
1.10.10.60;
|
CEF1 family
|
PTM: Phosphorylated on serine and threonine residues. Phosphorylation on Thr-411 and Thr-438 is required for CDC5L-mediated mRNA splicing. Has no effect on subcellular location nor on homodimerization. Phosphorylated in vitro by CDK2 (By similarity). Phosphorylation enhances interaction with PPP1R8. {ECO:0000250, ECO:0000269|PubMed:10827081}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:11694351, ECO:0000269|PubMed:11884640}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00625}. Cytoplasm {ECO:0000269|PubMed:11694351}. Note=May shuttle between cytoplasm and nucleus. {ECO:0000303|PubMed:11694351}.
| null | null | null | null | null |
FUNCTION: DNA-binding protein involved in cell cycle control. May act as a transcription activator. Plays a role in pre-mRNA splicing as core component of precatalytic, catalytic and postcatalytic spliceosomal complexes. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs. {ECO:0000250|UniProtKB:Q99459}.
|
Rattus norvegicus (Rat)
|
O08838
|
AMPH_RAT
|
MADIKTGIFAKNVQKRLNRAQEKVLQKLGKADETKDEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESLHEVYEPDWYGREDVKMVGEKCDVLWEDFHQKLVDGSLLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQSSKRKDESRISKAEEEFQKAQKVFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIAVLCHKLYEVMTKLGDQHADKAFSIQGAPSDSGPLRIAKTPSPPEEASPLPSPTASPNHTLAPASPAPVRPRSPSQTRKGPPVPPLPKVTPTKELQQENIINFFEDNFVPEINVTTPSQNEVLEVKKEETLLDLDFDPFKPDVTPAGSAAATHSPMSQTLPWDLWTTSTDLVQPASGGSFNDFTQPQDTSLFTMQTDQNMAETEQALPTEPQAEEPPTTAAAPTAGLDLGLEMEEPKEEAAIPPGTDAGETVGTEGSTGEEAEAEKAALPAGEGESPEGAKIDVESTELASSESPQAAELEAGAPQEKVIPSVVIEPASNHEGEEHQETTTGTETREATEDVAPQGPAGEKQELATEPTPLDSQAATPAPAGAVDASLSAGDAAQELPPGFLYKVETLHDFEAANSDELTLQRGDVVLVVPSDSEADQDAGWLVGVKESDWLQYRDLATYKGLFPENFTRHLE
| null | null |
learning [GO:0007612]; positive regulation of endocytosis [GO:0045807]; synaptic vesicle endocytosis [GO:0048488]
|
axon terminus [GO:0043679]; cytoskeleton [GO:0005856]; extrinsic component of synaptic vesicle membrane [GO:0098850]; glutamatergic synapse [GO:0098978]; leading edge membrane [GO:0031256]; photoreceptor ribbon synapse [GO:0098684]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; presynaptic endocytic zone [GO:0098833]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
|
phosphatase binding [GO:0019902]; phospholipid binding [GO:0005543]; protein-containing complex binding [GO:0044877]
|
PF03114;
|
1.20.1270.60;2.30.30.40;
| null | null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O08839
|
BIN1_RAT
|
MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLSECLQEVYEPEWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEKAAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVSLEKQHGSNTFTVKAQPSDSAPEKGNKSPSPPPDGSPAATPEIRVNHEPEPASGASPGATIPKSPSQLRKGPPVPPPPKHTPSKEMKQEQILSLFDDAFVPEISVTTPSQFEAPGPFSEQASLLDLDFEPLPPVASPVKAPTPSGQSIPWDLWEPTESQAGVLPSGEPSSAEGSFAVAWPSQTAEPGPAQPAEASEVVGGTQEPGETAASEATSSSLPAVVVETFSATVNGAVEGSTTTGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERVQ
| null | null |
endosome to lysosome transport [GO:0008333]; lipid tube assembly [GO:0060988]; muscle cell differentiation [GO:0042692]; negative regulation of amyloid-beta formation [GO:1902430]; negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel [GO:1904878]; negative regulation of potassium ion transmembrane transport [GO:1901380]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of ventricular cardiac muscle cell action potential [GO:1903946]; nucleus localization [GO:0051647]; nucleus organization [GO:0006997]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of apoptotic process [GO:0043065]; positive regulation of astrocyte differentiation [GO:0048711]; positive regulation of endocytosis [GO:0045807]; regulation of cell cycle process [GO:0010564]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of neuron differentiation [GO:0045664]; synaptic vesicle endocytosis [GO:0048488]; T-tubule organization [GO:0033292]
|
axon [GO:0030424]; axon initial segment [GO:0043194]; axon terminus [GO:0043679]; cerebellar mossy fiber [GO:0044300]; cytosol [GO:0005829]; dendrite [GO:0030425]; endosome [GO:0005768]; extrinsic component of synaptic vesicle membrane [GO:0098850]; glutamatergic synapse [GO:0098978]; I band [GO:0031674]; lipid tube [GO:0060987]; membrane [GO:0016020]; microtubule [GO:0005874]; node of Ranvier [GO:0033268]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; RNA polymerase II transcription repressor complex [GO:0090571]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; T-tubule [GO:0030315]; varicosity [GO:0043196]; vesicle [GO:0031982]; Z disc [GO:0030018]
|
actin filament binding [GO:0051015]; aspartic-type endopeptidase inhibitor activity [GO:0019828]; GTPase binding [GO:0051020]; identical protein binding [GO:0042802]; phospholipid binding [GO:0005543]; protease binding [GO:0002020]; protein-containing complex binding [GO:0044877]; protein-folding chaperone binding [GO:0051087]; RNA polymerase binding [GO:0070063]; tau protein binding [GO:0048156]
|
PF03114;PF14604;
|
1.20.1270.60;2.30.30.40;
| null |
PTM: Phosphorylated by protein kinase C.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O08539}. Cytoplasm {ECO:0000250|UniProtKB:O08539}. Endosome {ECO:0000250|UniProtKB:O08539}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:9182667}.
| null | null | null | null | null |
FUNCTION: Is a key player in the control of plasma membrane curvature, and membrane shaping and remodeling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling (By similarity). Is a negative regulator of endocytosis (PubMed:27760323, PubMed:9736607). Is also involved in the regulation of intracellular vesicles sorting, modulation of BACE1 trafficking and the control of amyloid-beta production (By similarity). In neuronal circuits, endocytosis regulation may influence the internalization of PHF-tau aggregates (PubMed:27760323). May be involved in the regulation of MYC activity and the control cell proliferation (By similarity). {ECO:0000250|UniProtKB:O00499, ECO:0000250|UniProtKB:O08539, ECO:0000269|PubMed:27760323, ECO:0000269|PubMed:9736607}.
|
Rattus norvegicus (Rat)
|
O08841
|
QSOX1_CAVPO
|
MTGCGRRSGWLPPLRLLLLPLLLGGPGVGAAQLAALYSASDPLTLLQADTVRSTVLNSPSAWAVEFFASWCGHCIAFAPTWKALAKDIKDWRPALNLAALNCADETNNAVCRDFNIAGFPSVRFFKAFSKNSTGTTLPVAGANVQMLRERLIDALESHHDTWPSACPPLEPVKPKEIDTFFARNNQEYLVLIFEQENSYLGREVTLDLSQHHDLVVRRVLSTEANVVRKFGVADFPSCYLLFRNGSVSRVPVLVESRRFYTAYLQRLSEVTREGTPTPAVPTISDQIAPTVWKFADRSKIYMADLESALHYILRVEVGRFSVLEGQRLMALKKFVTVLTKYFPGQPLVRNFLQSTNEWLKRQHKKKMPYSFFKTAMDSRNEEAVITKEVNWVGCQGSESHFRGFPCSLWILFHFLTVQASQKNAESSQKPANGQEVLQAIRNYVRFFFGCRDCANHFEQMAAGSMHRVKSPNDAVLWLWTSHNRVNARLAGAPSEDPQFPKVQWPPPELCSACHNELSGEPVWDVDATLRFLKTHFSPSNIVLNFPPAEPASRSSVHSWGATPHLELDALGLVTRNSALALERAEISESPGSNAMPNIPAERPELFEALSHSR
|
1.8.3.2
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O00391}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O00391};
|
extracellular matrix assembly [GO:0085029]; negative regulation of macroautophagy [GO:0016242]; protein folding [GO:0006457]
|
extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; intercellular bridge [GO:0045171]
|
FAD binding [GO:0071949]; flavin-dependent sulfhydryl oxidase activity [GO:0016971]; protein disulfide isomerase activity [GO:0003756]
|
PF04777;PF18371;PF18108;PF00085;
|
1.20.120.310;3.40.30.10;1.20.120.1960;
|
Quiescin-sulfhydryl oxidase (QSOX) family
|
PTM: N-glycosylated. O-glycosylated on Thr and Ser residues. {ECO:0000250|UniProtKB:O00391}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'; Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2; Evidence={ECO:0000250|UniProtKB:O00391};
| null | null | null | null |
FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. Plays a role in disulfide bond formation in a variety of extracellular proteins. In fibroblasts, required for normal incorporation of laminin into the extracellular matrix, and thereby for normal cell-cell adhesion and cell migration. {ECO:0000250|UniProtKB:O00391}.
|
Cavia porcellus (Guinea pig)
|
O08842
|
GFRA2_MOUSE
|
MILANAFCLFFFLDETLRSLASPSSPQGSELHGWRPQVDCVRANELCAAESNCSSRYRTLRQCLAGRDRNTMLANKECQAALEVLQESPLYDCRCKRGMKKELQCLQIYWSIHLGLTEGEEFYEASPYEPVTSRLSDIFRLASIFSGTGADPVVSAKSNHCLDAAKACNLNDNCKKLRSSYISICNREISPTERCNRRKCHKALRQFFDRVPSEYTYRMLFCSCQDQACAERRRQTILPSCSYEDKEKPNCLDLRSLCRTDHLCRSRLADFHANCRASYRTITSCPADNYQACLGSYAGMIGFDMTPNYVDSNPTGIVVSPWCNCRGSGNMEEECEKFLKDFTENPCLRNAIQAFGNGTDVNMSPKGPTFSATQAPRVEKTPSLPDDLSDSTSLGTSVITTCTSIQEQGLKANNSKELSMCFTELTTNISPGSKKVIKLYSGSCRARLSTALTALPLLMVTLAQ
| null | null |
glial cell-derived neurotrophic factor receptor signaling pathway [GO:0035860]; negative regulation of protein autophosphorylation [GO:0031953]; nervous system development [GO:0007399]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
external side of plasma membrane [GO:0009897]; receptor complex [GO:0043235]
|
glial cell-derived neurotrophic factor receptor activity [GO:0016167]; heparan sulfate binding [GO:1904399]
|
PF02351;
|
1.10.220.110;
|
GDNFR family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9182803}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:9182803}.
| null | null | null | null | null |
FUNCTION: Receptor for neurturin (NRTN), a growth factor that supports the survival of sympathetic neurons (PubMed:9182803). NRTN-binding leads to autophosphorylation and activation of the RET receptor (PubMed:9182803). Also able to mediate GDNF signaling through the RET tyrosine kinase receptor (By similarity). {ECO:0000250|UniProtKB:O00451, ECO:0000269|PubMed:9182803}.; FUNCTION: [Isoform 2]: Participates in NRTN-induced 'Ser-727' phosphorylation of STAT3. {ECO:0000269|PubMed:23872421}.
|
Mus musculus (Mouse)
|
O08848
|
RO60_MOUSE
|
MEGSANQLQPLSETQVVNSEGGCVWQVTDMNRLRRFLCFGSEGGTYYIKEQKLGLENAEALIRLIEDGRGCEVIQEIKSFSQEGRTAKQEPLLFALAVCSQCADINTKQAAFKAVPEVCRIPTHLFTFIQFKKDLKESMKCGMWGRALRKAVADWYNEKGGMAVALVVTKYKQRNGWSHKDLLRLSHLKPSSEGLAIVTKYITKGWKEVHEEYKEKALSVEAEKLLKYLEAVEKVKRTKDDLEVIHLIEEHQLVREHLLTNHLKSKEVWKALLQEMPLTALLRNLGKMTANSVLEPGNSEVSLICEKLSNEKLLKKARIHPFHVLIALETYRAGHGLRGKLKWIPDKDILQALDAAFYTTFKTVEPTGKRFLLAVDVSASMNQRALGSVLNASTVAAAMCMVVTRTEKESSVVAFACDMVPFPVTTDMTLQQVLTAMNKVPAGNTDCSLPMIWAQKTDTAADVFVVFTDNETFAGQVHPAVALREYRKKMDIPAKLIVCGMTSNGFTIADPDDRGMLDMCGFDTAALDVIRNFTLDVI
| null | null |
cellular response to interferon-alpha [GO:0035457]; cilium assembly [GO:0060271]; immune system development [GO:0002520]; regulation of gene expression [GO:0010468]; response to UV [GO:0009411]; smoothened signaling pathway [GO:0007224]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]
|
metal ion binding [GO:0046872]; misfolded RNA binding [GO:0034336]; RNA binding [GO:0003723]; U2 snRNA binding [GO:0030620]
|
PF05731;
|
3.40.50.410;
|
Ro 60 kDa family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P10155}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P10155}.
| null | null | null | null | null |
FUNCTION: RNA-binding protein that binds to misfolded non-coding RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y RNAs (By similarity). May play roles in cilia formation and/or maintenance (PubMed:21289087). {ECO:0000250|UniProtKB:P10155, ECO:0000269|PubMed:21289087}.
|
Mus musculus (Mouse)
|
O08849
|
RGS2_MOUSE
|
MQSAMFLAVQHDCVPMDKSAGNGPKVEEKREKMKRTLLKDWKTRLSYFLQNSSAPGKPKTGKKSKQQTFIKPSPEEAQLWAEAFDELLASKYGLAAFRAFLKSEFCEENIEFWLACEDFKKTKSPQKLSSKARKIYTDFIEKEAPKEINIDFQTKSLIAQNIQEATSGCFTTAQKRVYSLMENNSYPRFLESEFYQDLCKKPQITTEPHAT
| null | null |
brown fat cell differentiation [GO:0050873]; cell cycle [GO:0007049]; G protein-coupled receptor signaling pathway [GO:0007186]; maternal process involved in female pregnancy [GO:0060135]; negative regulation of cardiac muscle hypertrophy [GO:0010614]; negative regulation of cell growth involved in cardiac muscle cell development [GO:0061052]; negative regulation of G protein-coupled receptor signaling pathway [GO:0045744]; negative regulation of glycine import across plasma membrane [GO:1900924]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of phospholipase activity [GO:0010519]; negative regulation of translation [GO:0017148]; positive regulation of cardiac muscle contraction [GO:0060452]; positive regulation of neuron projection development [GO:0010976]; regulation of adenylate cyclase-inhibiting adrenergic receptor signaling pathway [GO:0071877]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; relaxation of cardiac muscle [GO:0055119]; relaxation of vascular associated smooth muscle [GO:0060087]; response to amphetamine [GO:0001975]; response to ethanol [GO:0045471]; spermatogenesis [GO:0007283]
|
cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
adenylate cyclase inhibitor activity [GO:0010855]; beta-tubulin binding [GO:0048487]; G-protein alpha-subunit binding [GO:0001965]; GTPase activator activity [GO:0005096]
|
PF00615;
|
1.10.196.10;1.10.167.10;
| null |
PTM: Phosphorylated by protein kinase C. Phosphorylation by PRKG1 leads to activation of RGS2 activity. {ECO:0000250|UniProtKB:P41220}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P41220}. Cytoplasm {ECO:0000250|UniProtKB:P41220}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P41220}.
| null | null | null | null | null |
FUNCTION: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form (By similarity). It is involved in the negative regulation of the angiotensin-activated signaling pathway (By similarity). Plays a role in the regulation of blood pressure in response to signaling via G protein-coupled receptors and GNAQ. Plays a role in regulating the constriction and relaxation of vascular smooth muscle (PubMed:14608379). Binds EIF2B5 and blocks its activity, thereby inhibiting the translation of mRNA into protein (By similarity). {ECO:0000250|UniProtKB:P41220, ECO:0000269|PubMed:14608379}.
|
Mus musculus (Mouse)
|
O08852
|
PKD1_MOUSE
|
MPLGAPALLALALGLGLWLGALAGDPGRGCGPCPLPCFCGPAPDAACRVNCSGRWLQTLGPSLRIPADATALDLSHNLLQTLDIGLLVNLSALVELDLSNNRISTLEEGVFANLFNLSEINLSGNPFECNCGLAWLPRWAKEHQVHVVQSEATTCRGPIPLAGQPLLSIPLLDNACGEEYVACLPDNSSGAVAAVPFYFAHEGPLETEACSAFCFSAGEGLAALSEQNQCLCGAGQASNSSAACSSWCSSISLSLNSACGGPTLLQHTFPASPGATLVGPHGPLASGQPADFHITSSLPISSTRWNFGDGSPEVDMASPAATHFYVLPGSYHMTVVLALGAGSALLETEVQVEATPTVLELVCPSFVHSNESLELGIRHRGGSALEVTYSILALDKEPAQVVHPLCPLDTEIFPGNGHCYRLVAEKAPWLQAQEQCRTWAGAALAMVDSPAIQHFLVSKVTRSLDVWIGFSSVEGTEGLDPRGEAFSLESCQNWLPGEPHPATAEHCVRLGPAGQCNTDLCSAPHSYVCELRPGGPVWDTENFVMGMSGGGLSGPLHPLAQQETVQGPLRPVEVMVFPGLSPSREAFLTAAEFSTQKLEEPAQMRLQVYRPSGGAAAVPEGSSEPDNRTEPAPKCVPEELWCPGANVCIPFDASCNSHVCINGSVSRLGLSRASYTLWKEFFFSVPAGPPTQYLVTLHSQDVPMLPGDLIGLQHDAGPGTLLQCPLASSCPGQALYLSTNASDWMTNLPVHLEEAWAGPVCSLQLLLVTERLTPLLGLGPNPGLQHPGHYEVRATVGNSVSRQNLSCSFSVVSPIAGLRVIHPIPLDGHIYVPTNGSVLVLQVDSGANATATAQWFGGNISAPFEDACPPEVDFLKQDCTEEANGTLFSVLMLPRLKEGDHTVEIVAQNGASQANLSLRVTAEEPICGLRAVPSPEARVLQGILVRYSPMVEAGSDVAFRWTIDDKQSLTFHNTVFNVIYQSAAIFKLSLTASNHVSNITVNYNVTVERMNKMHGLWVSAVPTVLPPNATLALTGGVLVDSAVEVAFLWNFGDGEQVLRQFKPPYDESFQVPDPTVAQVLVEHNTTHIYTTPGEYNLTVLVSNTYENLTQQVTVSVRTVLPNVAIGMSSNVLVAGQPITFSPYPLPSTDGVLYTWDFGDGSPVLIQSQPVLNHTYSMTGAYRITLEVNNTVSSVTAHADIRVFQELHGLTVYLSPSVEQGAPMVVSASVESGDNITWTFDMGDGTVFTGPEATVQHVYLRAQNFTVTVEAANPAGHLSQSLHVQVFVLEVLHIEPSTCIPTQPSAQLMAHVTGDPVHYLFDWTFGDGSSNVTVHGHPSVTHNFTRSGIFPLALVLSSHVNKAHYFTSICVEPEIRNITLQPERQFVKLGDEARLVAYSWPPFPYRYTWDFGTEDTTHTQTGGSEVKFIYREPGSYLVIVTVSNNISSTNDSAFVEVQEPVLVTGIRINGSHVLELQQPYLLSAMGSGSPATYLWELGDGSQSEGPEVTHIYSSTGDFTVRVSGWNEVSRSEAQLNITVKQRVRGLTINASRTVVPLNGSVSFSTLLEVGSDVHYSWVLCDRCTPIPGGPTISYTFRSVGTFNIIVTAENEVGSAQDSIFIYVLQFIEGLQVAGGDNGCCFPTNYTLQLQAAVRDGTNISYSWTAQQEGSLITLFGSGKCFSLTSLKASTYYVHLRATNMLGSAAANRTIDFVEPVESLILSASPNPAAVNMSLTLCAELAGGSGVVYTWYLEEGLSWKTSMPSTTHTFAAPGLHLVRVTAENQLGSVNATVEVAIQVPVGGLSIRTSEPDSIFVAAGSTLPFWGQLAEGTNVTWCWTLPGGSKDSQYIAVRFSTAGSFSLQLNASNAVSWVSAMYNLTVEEPIVNLMLWASSKVVAPGQPVHFEILLAAGSALTFRLQVGGSVPEVLPSPHFSHSFFRVGDHLVNVQAENHVSHAQAQVRILVLEAVVGLQVPNCCEPGMATGTEKNFTARVQRGSRVAYAWYFSLQKVQGDSLVILSGRDVTYTPVAAGLLEIHVRAFNELGGVNLTLMVEVQDIIQYVTLQSGRCFTNRSARFEAATSPSPRRVTYHWDFGDGTPVQKTEEFWADHYYLRPGDYHVEVNATNLVSFFVAQATVTVQVLACREPEVEVALPLQVLMRRSQRNYLEAHVDLRNCVSYQTEYRWEIYRTASCQRPGRMAQMVLPGVDVSRPQLVVPRLALPVGHYCFVFVVSFGDTPLARSIQANVTVAAERLVPIIEGGSYRVWSDTQDLVLDGSKSYDPNLEDGDQTPLNFHWACVASTQSETGGCVLNFGPRGSSVVTIPLERLEAGVEYTFNLIVWKAGRKEEATNQTVLIRSGRVPIVSLECVSCKAQAVYEVSRSSYVYLEGHCHNCSRGYKQGCWAARTFSNKTLVLNETTTSTGSTGMNLVVRPGALRDGEGYIFTLTVLGHSGEEEGCASIRLSPNRPPLGGSCRLFPLDSVRGLTTKVHFECTGWRDAEDGGAPLVYALLLKRCRQSYCENFCIYKGSLSTYGAVLPPGFQPLFVVSLAVVVQDQLGAAVVALNRSLTIVLPEPSGNPADLVPWLHSLTASVLPGLLKQADPQHVIEYSLALITVLNEYEQAPDVSEPNVEQQLRAQMRKNITETLISLRVNTVDDIQQITAALAQCMVSSRELMCRSCLKKMLQKLEGMMRILQAETTEGTLTPTTIADSILNITGDLIHLASLDMQGPQPLELGVEPPSLMVASKAYNLSSALMRILMRSRVLNEEPLTLAGEEIVALGKRSDPLSLLCYGKALGPSCHFSIPEAFSGALSNLSDVVQLIFLVDSNPFPFGYISNYTVSTKVASMAFQTQTGTQIPIEQLAAERAITVKVPNNSDQAAQSSHNPVGSTIVQPQTSVSAVVTADNSNPQAGLHLRITYTVLNERYLSAEPEPYLAVYLHSVSQPNEYNCSASRRISLEVLEGADHRLYTFFIAPGTGTLDRSYYLNLTSHFHWSALEVSVGLYTSLCQYFSEEMMMWRTEGIVPLEETSPSQAVCLTRHLTAFGASLFVPPSHVQFIFPEPSASINYIVLLTCVICLVTYVVMAMILRKLDQLDVSRVRVIPFCGKGGRFKYEILVKTGWSRGSGTTAHVGIMLYGEDNRSGHRHLDGDRAFHRNSLDIFQIATPHSLGSVWKIRVWHDNKGLSPAWFLQHIIVRDLQSARSTFFLVNDWLSVETEANGGLVEKEVLAANEAALWQFQRLLVAELQRGFFDKHIWLSIWDRPPRSRFTRVQRVTCCVLLLCLFLAANAVWYGVVRDTTYSMGPVSSLISPGVDTVAIGLVSSVVVYPVYLAVLFLFRMSRSKVSGDQNPTPTGQQALDVDSYLDPSVLDSSLLTLSGLTEAFAGQVKNDLFLEDAKSLVCWPSSEGTLSWPDLLSDPSVVSSTLQRLTQGRPGCMLGSEEDGASLVSPSLPAKYLSASDEDLIHQVLADGANNLVPTQDTLLETDLLTSLSSVPGEKTETLILQTVGEERPASMGLSWEQSPVTRLSRTGLVEGFQKRLLPAWCAPLAHGLSLLLVAVAVAVSGWIGASFPPSVSVMWLLSSSSSFLASFLGWEPLKVLLEALYFSLVAKRLHPDEDDTLVESPAVTPVSERVPRVRPPHGFALFLAKEEARKVKRLHDMLKRLLVYMLFLLVTLLANYGDASCHGHAYRLQSAIKQELDSQAFLAITRSDEFWPWMSHVFLPYVHGNQSSPELGPPRLRQVRLQEAFCPDPSSSEHMCSAAGSLSTSDYGIGWQSVVQNGSETWAYSAPDLLGAWYWGYCAVYDSGGYIQELGLSLEESRARLGFLQLHNWLDSRSRAVFVELTRYSPAVGLHAAVTLRLEFPVAGHALAAFSVRPFALRRLSTGLSLPLLTSVCLLLFALYFSMAEVQTWRKDGCACTARPDTWARCLLVILTAATGLVRLAQLGIADRQWTHFVQDHPRHFTSFDQVAQLGSVARGLAASLLFLLLVKAAQQLRFVRQWSVFGKTLCRALPELMGATLGLVLLGVAYAQMAILLISSGADTLYNMARAFLVLCPGARVPTLCPSESWYLSPLLCVGLWALRVWGALRLGAILLRWRYHALRGELYRPAWEPQDYEMVELFLRRLRLWMGFSKVKEFRHKVRFEGMDPLPSRSSRGSKSSPVVLPPSSGSEASHPSTSSSQPDGPSASLSRSTLKLEPEPSRLHAVFESLLVQFDRLNQATEDVYQLEQQLQSLQGHGHNGPPSSPSPGCFPGSQPALPSRLSRASQGLDQTVGPNRVSLWPNNKVHPSST
| null | null |
blood vessel development [GO:0001568]; branching morphogenesis of an epithelial tube [GO:0048754]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; cartilage condensation [GO:0001502]; cell-cell adhesion [GO:0098609]; cell-cell signaling by wnt [GO:0198738]; detection of mechanical stimulus [GO:0050982]; digestive tract development [GO:0048565]; embryonic placenta development [GO:0001892]; establishment of epithelial cell polarity [GO:0090162]; genitalia development [GO:0048806]; heart development [GO:0007507]; in utero embryonic development [GO:0001701]; kidney development [GO:0001822]; liver development [GO:0001889]; lung epithelium development [GO:0060428]; lymph vessel morphogenesis [GO:0036303]; mesonephric duct development [GO:0072177]; metanephric ascending thin limb development [GO:0072218]; metanephric collecting duct development [GO:0072205]; metanephric distal tubule morphogenesis [GO:0072287]; metanephric proximal tubule development [GO:0072237]; mitocytosis [GO:0160040]; neural tube development [GO:0021915]; peptidyl-serine phosphorylation [GO:0018105]; placenta blood vessel development [GO:0060674]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein export from nucleus [GO:0006611]; protein heterotetramerization [GO:0051290]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of cell adhesion [GO:0030155]; regulation of cell cycle [GO:0051726]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of mitotic spindle organization [GO:0060236]; regulation of proteasomal protein catabolic process [GO:0061136]; response to fluid shear stress [GO:0034405]; skin development [GO:0043588]; spinal cord development [GO:0021510]
|
basolateral plasma membrane [GO:0016323]; calcium channel complex [GO:0034704]; cation channel complex [GO:0034703]; cell surface [GO:0009986]; cilium [GO:0005929]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; migrasome [GO:0140494]; motile cilium [GO:0031514]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; polycystin complex [GO:0002133]
|
calcium channel activity [GO:0005262]; carbohydrate binding [GO:0030246]; monoatomic cation channel activity [GO:0005261]; protein domain specific binding [GO:0019904]; protein kinase binding [GO:0019901]; transcription regulator inhibitor activity [GO:0140416]; transmembrane transporter binding [GO:0044325]; Wnt receptor activity [GO:0042813]
|
PF00059;PF13855;PF00801;PF08016;PF01477;PF20519;PF02010;PF01822;
|
2.60.40.10;3.10.100.10;2.60.60.20;3.80.10.10;
|
Polycystin family
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:P98161}.; PTM: After synthesis, undergoes autoproteolytic cleavage between Leu-3040 and Thr-3041 in the GPS region of the GAIN-B domain (PubMed:25405894). Cleavage at the GPS region occurs through a cis-autoproteolytic mechanism involving an ester-intermediate via N-O acyl rearrangement (By similarity). This process takes place in the early secretory pathway, depends on initial N-glycosylation, and requires the REJ domain (By similarity). PKD1 is ubiquitously and incompletely cleaved in wild-type mice, so that uncleaved and cleaved PKD1 molecules coexist. The differential patterns of cleavage during embryonic development, as well as in adult mice, suggest different functions of uncleaved and cleaved molecules (PubMed:18003909). {ECO:0000250|UniProtKB:P98161, ECO:0000269|PubMed:18003909, ECO:0000269|PubMed:25405894}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P98161}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P98161}. Cell projection, cilium {ECO:0000269|PubMed:12514735, ECO:0000269|PubMed:24939912, ECO:0000269|PubMed:25405894}. Endoplasmic reticulum {ECO:0000269|PubMed:25405894}. Golgi apparatus {ECO:0000269|PubMed:25405894}. Vesicle {ECO:0000250|UniProtKB:P98161}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P98161}. Note=PKD1 localization to the plasma and ciliary membranes requires PKD2, is independent of PKD2 channel activity, and involves stimulation of PKD1 autocatalytic cleavage at the GPS region of the GAIN-B domain (PubMed:12514735, PubMed:25405894). PKD1:PKD2 interaction is required to reach the Golgi apparatus from endoplasmic reticulum and then traffic to the cilia (PubMed:25405894). Ciliary localization of PKD1 requires BBS1 and ARL6/BBS3 (PubMed:24939912). Cell surface localization requires GANAB (By similarity). Detected on migrasomes and on extracellular exosomes in urine (By similarity). {ECO:0000250|UniProtKB:P98161, ECO:0000269|PubMed:12514735, ECO:0000269|PubMed:24939912, ECO:0000269|PubMed:25405894}.
| null | null | null | null | null |
FUNCTION: Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B. Both PKD1 and PKD2 are required for channel activity (By similarity). Involved in renal tubulogenesis (PubMed:24939912). Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (PubMed:12514735). Acts as a regulator of cilium length, together with PKD2 (PubMed:20096584). The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling. May be an ion-channel regulator. Involved in adhesive protein-protein and protein-carbohydrate interactions. Likely to be involved with polycystin-1-interacting protein 1 in the detection, sequestration and exocytosis of senescent mitochondria (By similarity). {ECO:0000250|UniProtKB:P98161, ECO:0000269|PubMed:12514735, ECO:0000269|PubMed:20096584, ECO:0000269|PubMed:24939912}.
|
Mus musculus (Mouse)
|
O08856
|
ELL_MOUSE
|
MAALKEARSYGLSCGRVSDGSRVSVFHVKLTDSALKAFESYRAHQDSVSLRPSIRFEGSQGHISIPQPDCPEEVRAFSFYLSNIGRDSPQGSFDCIQQYVSSYGDVHLDCLGSIQDKVTVCATDDSYQKARQSMAQAEEETRSRSAIVIKAGGRYMGKKVQFRKPAPGAADAVPSRKRATPINLASAIRKSSGSGASSVVQRPFRDRVLHLLALRPYRKAELLLRLQKDGLTQADKDTLDSLLQQVASVNPKDGTCTLQDCMYKSLQKDWPGYSEGDRQLLKRMLMRKLCQPQNATTDSSPPREHGRSASPSQKRPTDFIDPLASKKPRISHFTQRAQPTLNGKLGAPNGHETLLPAPGPTPSDTLSSSHLPPRLEPPRTHDPLADVSNDLGHSTQDYKHQEATPAPAPHLGLPLLTDFPQAEQPTSSSHTHSRPKKKSKKHKDKERPPEERPPAPQPDAPTAPALPPDAPGLNGACDNEPTSSSETPDYLLKYPAISSSEQRQSYKNDFNAEYSEYRSLHARIEQITRRFTQLDAQLRQLSQGSDEYETTRGQILQEYRKIKKTNTNYSCEKRRCEYLHRKLAHIKRLIAEYDQRQLQAWP
| null | null |
in utero embryonic development [GO:0001701]; positive regulation of transcription by RNA polymerase III [GO:0045945]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; snRNA transcription by RNA polymerase II [GO:0042795]; snRNA transcription by RNA polymerase III [GO:0042796]; transcription elongation by RNA polymerase II [GO:0006368]
|
Cajal body [GO:0015030]; cytosol [GO:0005829]; euchromatin [GO:0000791]; histone locus body [GO:0035363]; nuclear speck [GO:0016607]; transcription elongation factor complex [GO:0008023]
|
cis-regulatory region sequence-specific DNA binding [GO:0000987]; phosphatase binding [GO:0019902]
|
PF10390;PF07303;
|
6.10.140.340;1.10.10.2670;
|
ELL/occludin family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55199}. Nucleus speckle {ECO:0000250|UniProtKB:P55199}. Nucleus, Cajal body {ECO:0000250|UniProtKB:P55199}. Note=Colocalizes with EAF2 to nuclear speckles. Colocalizes with coilin in subnuclear cajal and histone locus bodies. Translocates in the LEC complex to cajal and histone locus bodies at snRNA genes in a ICE1-dependent manner. Associates to transcriptionally active chromatin at snRNA genes (By similarity). {ECO:0000250|UniProtKB:P55199}.
| null | null | null | null | null |
FUNCTION: Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Specifically required for stimulating the elongation step of RNA polymerase II- and III-dependent snRNA gene transcription. ELL also plays an early role before its assembly into in the SEC complex by stabilizing RNA polymerase II recruitment/initiation and entry into the pause site. Required to stabilize the pre-initiation complex and early elongation. Specifically required for stimulating the elongation step of RNA polymerase II- and III-dependent snRNA gene transcription (By similarity). Elongation factor component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968). {ECO:0000250, ECO:0000269|PubMed:22195968}.
|
Mus musculus (Mouse)
|
O08858
|
SSR5_MOUSE
|
MEPLSLTSTPSWNASAASSSSHNWSLVDPVSPMGARAVLVPVLYLLVCTVGLGGNTLVIYVVLRYAKMKTVTNVYILNLAVADVLFMLGLPFLATQNAVSYWPFGSFLCRLVMTLDGINQFTSIFCLMVMSVDRYLAVVHPLRSARWRRPRVAKLASAAVWVFSLLMSLPLLVFADVQEGWGTCNLSWPEPVGLWGAAFITYTSVLGFFGPLLVICLCYLLIVVKVKAAGMRVGSSRRRRSERKVTRMVVVVVLVFVGCWLPFFIVNIVNLAFTLPEEPTSAGLYFFVVVLSYANSCANPLLYGFLSDNFRQSFRKALCLRRGYGVEDADAIEPRPDKSGRPQTTLPTRSCEANGLMQTSRL
| null | null |
adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; cellular response to glucocorticoid stimulus [GO:0071385]; glucose homeostasis [GO:0042593]; neuropeptide signaling pathway [GO:0007218]; regulation of insulin secretion [GO:0050796]
|
neuron projection [GO:0043005]; plasma membrane [GO:0005886]
|
neuropeptide binding [GO:0042923]; somatostatin receptor activity [GO:0004994]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
|
PTM: Palmitoylated at Cys-319 by ZDHHC5, but not ZDHHC8. Palmitoylation creates an additional intracellular loop which is thought to be important for efficient coupling to G-proteins and may target the protein to lipid rafts. {ECO:0000269|PubMed:21820437}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21820437}; Multi-pass membrane protein {ECO:0000269|PubMed:21820437}.
| null | null | null | null | null |
FUNCTION: Receptor for somatostatin-28. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. Increases cell growth inhibition activity of SSTR2 following heterodimerization.
|
Mus musculus (Mouse)
|
O08859
|
TSG6_MOUSE
|
MVVLLCLCVLLWEEAHGWGFKNGIFHNSIWLEQAAGVYHREARAGRYKLTYAEAKAVCEFEGGRLATYKQLEAARKIGFHVCAAGWMAKGRVGYPIVKPGPNCGFGKTGIIDYGIRLNRSERWDAYCYNPHAKECGGVFTDPKRIFKSPGFPNEYDDNQVCYWHIRLKYGQRIHLSFLDFDLEHDPGCLADYVEIYDSYDDVHGFVGRYCGDELPEDIISTGNVMTLKFLSDASVTAGGFQIKYVTVDPASKSSQAKNTSTTGNKKFLPGRFSHL
| null | null |
cell adhesion [GO:0007155]; fibronectin fibril organization [GO:1905590]; hyaluronan metabolic process [GO:0030212]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of inflammatory response [GO:0050728]; negative regulation of neutrophil chemotaxis [GO:0090024]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of osteoclast differentiation [GO:0045671]; ovarian cumulus expansion [GO:0001550]; positive regulation of cell migration [GO:0030335]; positive regulation of receptor clustering [GO:1903911]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; carboxylesterase activity [GO:0106435]; fibronectin binding [GO:0001968]; hyaluronic acid binding [GO:0005540]
|
PF00431;PF00193;
|
3.10.100.10;2.60.120.290;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P98066}.
| null | null | null | null | null |
FUNCTION: Major regulator of extracellular matrix organization during tissue remodeling (By similarity). Catalyzes the transfer of a heavy chain (HC) from inter-alpha-inhibitor (I-alpha-I) complex to hyaluronan. Cleaves the ester bond between the C-terminus of the HC and GalNAc residue of the chondroitin sulfate chain in I-alpha-I complex followed by transesterification of the HC to hyaluronan. In the process, potentiates the antiprotease function of I-alpha-I complex through release of free bikunin (By similarity). Acts as a catalyst in the formation of hyaluronan-HC oligomers and hyaluronan-rich matrix surrounding the cumulus cell-oocyte complex, a necessary step for oocyte fertilization (PubMed:12668637). Assembles hyaluronan in pericellular matrices that serve as platforms for receptor clustering and signaling. Enables binding of hyaluronan deposited on the surface of macrophages to LYVE1 on lymphatic endothelium and facilitates macrophage extravasation. Alters hyaluronan binding to functionally latent CD44 on vascular endothelium, switching CD44 into an active state that supports leukocyte rolling (By similarity). Modulates the interaction of chemokines with extracellular matrix components and proteoglycans on endothelial cell surface, likely preventing chemokine gradient formation. In a negative feedback mechanism, may limit excessive neutrophil recruitment at inflammatory sites by antagonizing the association of CXCL8 with glycosaminoglycans on vascular endothelium (By similarity). Has a role in osteogenesis and bone remodeling. Inhibits BMP2-dependent differentiation of mesenchymal stem cell to osteoblasts. Protects against bone erosion during inflammation by inhibiting TNFSF11/RANKL-dependent osteoclast activation (By similarity) (PubMed:18586671). {ECO:0000250|UniProtKB:P98066, ECO:0000269|PubMed:12668637, ECO:0000269|PubMed:18586671}.
|
Mus musculus (Mouse)
|
O08863
|
BIRC3_MOUSE
|
MVQDSAFLAKLMKSADTFELKYDFSCELYRLSTYSAFPRGVPVSERSLARAGFYYTGANDKVKCFCCGLMLDNWKQGDSPMEKHRKLYPSCNFVQTLNPANSLEASPRPSLPSTAMSTMPLSFASSENTGYFSGSYSSFPSDPVNFRANQDCPALSTSPYHFAMNTEKARLLTYETWPLSFLSPAKLAKAGFYYIGPGDRVACFACDGKLSNWERKDDAMSEHQRHFPSCPFLKDLGQSASRYTVSNLSMQTHAARIRTFSNWPSSALVHSQELASAGFYYTGHSDDVKCFCCDGGLRCWESGDDPWVEHAKWFPRCEYLLRIKGQEFVSQVQAGYPHLLEQLLSTSDSPEDENADAAIVHFGPGESSEDVVMMSTPVVKAALEMGFSRSLVRQTVQWQILATGENYRTVSDLVIGLLDAEDEMREEQMEQAAEEEESDDLALIRKNKMVLFQHLTCVTPMLYCLLSARAITEQECNAVKQKPHTLQASTLIDTVLAKGNTAATSFRNSLREIDPALYRDIFVQQDIRSLPTDDIAALPMEEQLRKLQEERMCKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICRGTIKGTVRTFLS
|
2.3.2.27
| null |
apoptotic process [GO:0006915]; cellular response to tumor necrosis factor [GO:0071356]; necroptotic process [GO:0070266]; negative regulation of apoptotic process [GO:0043066]; negative regulation of necroptotic process [GO:0060546]; negative regulation of phosphorylation [GO:0042326]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; positive regulation of protein polyubiquitination [GO:1902916]; positive regulation of protein ubiquitination [GO:0031398]; regulation of cell cycle [GO:0051726]; regulation of non-canonical NF-kappaB signal transduction [GO:1901222]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; metal ion binding [GO:0046872]; protein-containing complex binding [GO:0044877]; ubiquitin protein ligase activity [GO:0061630]
|
PF00653;PF21290;PF00619;PF13920;
|
1.10.533.10;1.10.8.10;
|
IAP family
|
PTM: Auto-ubiquitinated and degraded by the proteasome in apoptotic cells. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:18621737};
| null | null | null | null |
FUNCTION: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, IKBKE, TRAF1, and BCL10. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. {ECO:0000269|PubMed:18621737}.
|
Mus musculus (Mouse)
|
O08873
|
MADD_RAT
|
MVQKKFCPRLLDYLVIVGARHPSSDSVAQTPELLRRYPLEDHPEFPLPPDVVFFCQPEGCLSVRQRRMSLRDDTSFVFTLTDKDTGVTRYGICVNFYRSFQKRMPKEKAEGGAGPRGKEGAHAPCASEEAATESSESGSTLQPPSADSTPDVNQSPRGKRRAKAGNRSRNSTLTSLCVLSHYPFFSTFRECLYTLKRLVDCCSERLLGKKPGIPRGVQRDTMWRIFTGSLLVEEKSSALLHDLREIEAWIYRLLRSPVPVSGQKRVDIEVLPQEVQQALTFALPDPSRFTLVDFPLHLPLELLGVDACLQVLTCILLEHKVVLQSRDYNALSMSVMAFVAMIYPLEYMFPVIPLLPTCMASAEQLLLAPTPYIIGVPASFFLYKLDFKMPDDVWLVDLDSNRVIAPTNAEVLPILPEPESLELKKHLKQALASMSLNTQPILNLEKFHEGQETPLLLGRFSNDLQSTPSTEFNPLIYGNDVDSVDVATRVAMVRFFNSANVLQGFQMHTRTLRLFPRPVVAFQAGSFLASRPRQTPFAEKLARTQAVEYFGEWILNPSNYAFQRIHNNTFDPALIGDKPKWYAHQLQPIHYRVYDSNSQLAEALSVPPERDSESDPTDDSGSDSMDYDDSSSSYSSLGDFVSEMMKCDINGDTPNVDPLTHAALGDASEVEIDELQPQKEGEEPGPDSENSQENLPLRSSSSTTASSSPSTIVHGAHSEPADSTEVGDKAATGISKPLPPVPPSICKSTVDRRQTETGEGSVCQRTYDHPYFEPQYGSPAEEDDDEQGESYTPRFSQHASGSRAQKLLRPNSLKLASDSDAESDSRASSPNSTVSNNSTEGFGGIMSFASSLYRNHSTSFSLSNLTLPTKGAREKTTPFPSLKGNRRALVDQKSSVIKHSPTVKREPPSPQGRSSNSSENQQFLKEVVHSVLDGQGVGWLNMKKVRRLLESEQLRVFVLSKLSRAVQSEDDARQDVIQDVEISRKVYKGMLDLLKCTVLSLEQSYAHAGLGGMASIFGLLEIAQTHYYSKEPDKRKRSPTENVNTPVGKDPGLAGRGDPKAMAQLRVPQLGPRAPSATGRGPKELDTRSLKEENFVASVGPEVIKPVFDLGETEEKKSQISADSGVSLASASQRTDQDSVIGVSPAVMIRSSSQDSEVSNSSGETLGADSDLSSNAGDGPGGEGSAHLASSRATLSDSEIETNSATSTIFGKAHSLKPKEKPASSPVRSSEDVSQRVYLYEGLLGRDKGSMWDQLEDAAMETFSISKERSTLWDQMQFWEDAFLDAVMLEREGMGMDQGPQEMIDRYLSLGEHDRKRLEDDEDRLLATLLHNLISYMLLMKVNKNDIRKKVRRLMGKSHVGLVYSQQINEVLDQLTNLNGRDLSIRSSGSRHMKKQTFVVHAGTDTNGDIFFMEVCDDCVVLRSNIGTVYERWWYEKLINMTYCPKTKVLCLWRRNGSETQLNKFYTKKCRELYYCVKDSMERAAARQQSIKPGPELGGEFPVQDMKTGEGGLLQVTLEGINLKFMHNQVFIELNHIKKCNTVRGVFVLEEFVPEIKEVVSHKYKTPMAHEICYSVLCLFSYVAAVRSSEEDLRTPPRPVSS
| null | null |
anterograde synaptic vesicle transport [GO:0048490]; execution phase of apoptosis [GO:0097194]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of growth hormone secretion [GO:0060125]; negative regulation of pancreatic amylase secretion [GO:1902277]; positive regulation of MAPK cascade [GO:0043410]; regulation of apoptotic process [GO:0042981]; regulation of cell cycle [GO:0051726]; regulation of extrinsic apoptotic signaling pathway [GO:2001236]; regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902041]; regulation of Rab protein signal transduction [GO:0032483]
|
axon [GO:0030424]; axon cytoplasm [GO:1904115]; cytosol [GO:0005829]; membrane [GO:0016020]; plasma membrane [GO:0005886]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]
|
guanyl-nucleotide exchange factor activity [GO:0005085]
|
PF02141;PF03456;
|
3.30.450.200;3.40.50.11500;
|
MADD family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8WXG6}. Cytoplasm {ECO:0000250|UniProtKB:Q8WXG6}. Cell projection, axon {ECO:0000250|UniProtKB:Q80U28}.
| null | null | null | null | null |
FUNCTION: Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:9020086). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (By similarity). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in synaptic vesicle exocytosis and vesicle secretion (PubMed:9020086). Plays a role in synaptic vesicle formation and in vesicle trafficking at the neuromuscular junction (By similarity). Involved in up-regulating a post-docking step of synaptic exocytosis in central synapses (By similarity). Probably by binding to the motor proteins KIF1B and KIF1A, mediates motor-dependent transport of GTP-RAB3A-positive vesicles to the presynaptic nerve terminals (By similarity). Plays a role in TNFA-mediated activation of the MAPK pathway, including ERK1/2 (By similarity). May link TNFRSF1A with MAP kinase activation (By similarity). May be involved in the regulation of TNFA-induced apoptosis (By similarity). {ECO:0000250|UniProtKB:Q80U28, ECO:0000250|UniProtKB:Q8WXG6, ECO:0000269|PubMed:9020086}.
|
Rattus norvegicus (Rat)
|
O08874
|
PKN2_RAT
|
MASNPDRGEILLTELQVDSRPLPFSENVSAVQKLDFSDTIVQQKLDDVKDRIKREIRKELKIKEGAENLRKVTTDKKNLAYVDNILKKSNKKLEELHHKLQELNAHIVVSDPEDYTDCPRTPDTPNSDSRSSTSNNRRLMALQKQLDIELKVKQGAENMIQMYSNGPSKDRKLHGTAQQLLQDNKTKIEVIRMHILQAVLTNELAFDNAKPVISPLELRNGRIIEHHFRIEFAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSLEQRLNELPKNHPKSSVVIEELSLVASPTLSPRQSMLSTQNQYSTLSKPAALTGTLEVRLWGAKISWENVPGRSKATSVALPGWSPSENRSSFMSRTSKSKSGSSRNLLKTDDLSNDVCAVLKLDNTVVGQTIWKPISNQSWDQKFTLELDRSRELEISVYWRDWRSLCAVKFLRLEDFLDNQRHGMALYLEPQGTLFAEVTFFNPVIERRPKLQRQKKIFSKQQGKTFLRAPQMNINIATWGRLVRRAIPTVNHSGTFSPQTPVPATVPVVDARTPELAPPASDSTVTKLDFDLEPEAPPAPPRASSLGEIDDSSELRVLDIPGQGSETVFDIENDRNNMRPKSKSEYELNIPDSSRSCWSVGELEDKRSQQRFQFNLQDFRCCAVLGRGHFGKVLLAEYKHTNEMFAIKALKKGDIVARDEVDSLMCEKRIFETVNSVRHPFLVNLFACFQTKEHVCFVMEYAAGGDLMMHIHTDVFSEPRAVFYAACVVLGLQYLHEHKIVYRDLKLDNLLLDTEASVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRRNPERRLGAGEKDAEDVKKHPFFRLTDWSALLDKKVKPPFVPTIRGREDVSNFDDEFTSEAPILTPPREPRILLEEEQEMFRDFDYVADWC
|
2.7.11.13
| null |
apical junction assembly [GO:0043297]; apoptotic process [GO:0006915]; cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell division [GO:0051301]; cell projection organization [GO:0030030]; epithelial cell migration [GO:0010631]; intracellular signal transduction [GO:0035556]; positive regulation of cytokinesis [GO:0032467]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of viral genome replication [GO:0045070]; protein phosphorylation [GO:0006468]; regulation of cell motility [GO:2000145]
|
apical junction complex [GO:0043296]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; lamellipodium [GO:0030027]; midbody [GO:0030496]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone deacetylase binding [GO:0042826]; kinase activity [GO:0016301]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase binding [GO:0070063]; small GTPase binding [GO:0031267]
|
PF02185;PF00069;PF00433;
|
1.10.287.160;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily
|
PTM: Phosphorylated during mitosis (By similarity). Autophosphorylated. Phosphorylated. Binding to Rho and Rac promotes autophosphorylation and phosphorylation on serine and threonine residues. Phosphorylated by CDK10 (By similarity). {ECO:0000250|UniProtKB:Q16513, ECO:0000269|PubMed:9121475}.; PTM: Proteolytically cleaved by caspase-3 during the induction of apoptotic cell death (By similarity). Activated by limited proteolysis with trypsin. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16513}. Nucleus {ECO:0000250|UniProtKB:Q16513}. Membrane {ECO:0000250|UniProtKB:Q8BWW9}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q16513}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q16513}. Cleavage furrow {ECO:0000250|UniProtKB:Q16513}. Midbody {ECO:0000250|UniProtKB:Q16513}. Cell junction {ECO:0000250|UniProtKB:Q16513}. Note=Colocalizes with PTPN13 in lamellipodia-like structures, regions of large actin turnover. Accumulates during telophase at the cleavage furrow and concentrates finally around the midbody in cytokinesis. Recruited to nascent cell-cell contacts at the apical surface of cells. {ECO:0000250|UniProtKB:Q16513}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13;
| null | null | null | null |
FUNCTION: PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Involved in the negative regulation of ciliogenesis. {ECO:0000250|UniProtKB:Q16513}.
|
Rattus norvegicus (Rat)
|
O08875
|
DCLK1_RAT
|
MLELIEVNGTPGSQLSTPRSGKSPSPSPTSPGSLRKQRISQHGGSSTSLSSTKVCSSMDENDGPGEEESDEGFQIPATITERYKVGRTIGDGNFAVVKECIERSTAREYALKIIKKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDVPTELYLVMELVKGGDLFDAITSTSKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKSLKLGDFGLATIVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLFDQILMGQVDFPSPYWDNVSDSAKELINMMLLVNVDQRFSAVQVLEHPWVNDDGLPENEHQLSVAGKIKKHFNTGPKPSSTAAGVSVIATTALDKERQVFRRRRNQDVRGRYKAQPAPPELNSESEDYSPSSSETVRSPNSPF
|
2.7.11.1
| null |
axon extension [GO:0048675]; axonogenesis [GO:0007409]; brain development [GO:0007420]; central nervous system projection neuron axonogenesis [GO:0021952]; dendrite morphogenesis [GO:0048813]; forebrain development [GO:0030900]; negative regulation of protein localization to nucleus [GO:1900181]; neuron migration [GO:0001764]; neuron projection morphogenesis [GO:0048812]; phosphorylation [GO:0016310]; protein localization to nucleus [GO:0034504]; response to virus [GO:0009615]
|
axon [GO:0030424]; growth cone [GO:0030426]; postsynaptic density [GO:0014069]
|
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O08876
|
KLF10_RAT
|
MLNFGASLQQASEGKMELISEKSKEGAHPWDKAEQSDFEAVEALMSMSCDWKSHFKKYLENRPVTPVSDTSEEDSLLPGTPDLQTVPAFCLTPPYSPSDFEPSQGSNLTAPAPPTGHFRSLSDAAKPPSIAPFKEEEKSPLAAPPLPKAQATSVIRHTADAQLCNHQSCPVKAASILNYQDNSFRRRTHINVEATRKNIPCAAVSPNRPKPEPSTAANGAEKAGTAPYDFAVPSSETVICRSSQPAPTSPVQKSVLMSSPTVSTGGVPPLPVICQMVPLPANNSLVTTVVPSSPPSQPPAVCSPVLFMGTQVPKGTVMFVVPQPVVQSPKPPVVSPNGTRLSPIAPAPGFSPSAARVTPQIDSSRVRSHICSHPGCGKTYFKSSHLKAHVRTHTGEKPFSCSWKGCERRFARSDELSRHRRTHTGEKKFACPMCDRRFMRSDHLTKHARRHLSAKKLPNWQMEVSKLNDIALPPATASAQ
| null | null |
bone mineralization [GO:0030282]; cellular response to peptide [GO:1901653]; cellular response to starvation [GO:0009267]; circadian rhythm [GO:0007623]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of circadian rhythm [GO:0042752]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; somatic stem cell population maintenance [GO:0035019]
|
nucleus [GO:0005634]
|
core promoter sequence-specific DNA binding [GO:0001046]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00096;
|
3.30.160.60;
|
Sp1 C2H2-type zinc-finger protein family
|
PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation. {ECO:0000250|UniProtKB:Q13118}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20070857}.
| null | null | null | null | null |
FUNCTION: Transcriptional repressor which binds to the consensus sequence 5'-GGTGTG-3'. Regulates the circadian expression of genes involved in lipogenesis, gluconeogenesis, and glycolysis in the liver. Represses the expression of PCK2, a rate-limiting step enzyme of gluconeogenesis. May play a role in the cell cycle regulation (By similarity). Plays a role in the regulation of the circadian clock; binds to the GC box sequence in the promoter of the core clock component ARTNL/BMAL1 and represses its transcriptional activity. {ECO:0000250|UniProtKB:O89091, ECO:0000250|UniProtKB:Q13118, ECO:0000269|PubMed:20070857}.
|
Rattus norvegicus (Rat)
|
O08878
|
GPER1_RAT
|
MAATTPAQDVGVEIYLGPVWPAPSNSTPLALNLSLALREDAPGNLTGDLSEHQQYVIALFLSCLYTIFLFPIGFVGNILILVVNISFREKMTIPDLYFINLAAADLILVADSLIEVFNLDEQYYDIAVLCTFMSLFLQINMYSSVFFLTWMSFDRYLALAKAMRCGLFRTKHHARLSCGLIWMASVSATLVPFTAVHLRHTEEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRALIRAHRHRGLRPRRQKALRMIFAVVLVFFICWLPENVFISVHLLQWAQPGDTPCKQSFRHAYPLTGHIVNLAAFSNSCLSPLIYSFLGETFRDKLRLYVAQKTSLPALNRFCHATLKAVIPDSTEQSDVKFSSAV
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; apoptotic chromosome condensation [GO:0030263]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to estradiol stimulus [GO:0071392]; cellular response to glucose stimulus [GO:0071333]; cellular response to mineralocorticoid stimulus [GO:0071389]; cellular response to peptide hormone stimulus [GO:0071375]; cellular response to tumor necrosis factor [GO:0071356]; G protein-coupled receptor signaling pathway [GO:0007186]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; intracellular estrogen receptor signaling pathway [GO:0030520]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of cell cycle process [GO:0010948]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of gene expression [GO:0010629]; negative regulation of inflammatory response [GO:0050728]; negative regulation of leukocyte activation [GO:0002695]; negative regulation of lipid biosynthetic process [GO:0051055]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of vascular associated smooth muscle cell proliferation [GO:1904706]; nervous system development [GO:0007399]; neuronal action potential [GO:0019228]; nuclear fragmentation involved in apoptotic nuclear change [GO:0030264]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cardiac vascular smooth muscle cell differentiation [GO:2000724]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of endothelial cell apoptotic process [GO:2000353]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of G protein-coupled receptor signaling pathway [GO:0045745]; positive regulation of gene expression [GO:0010628]; positive regulation of inositol trisphosphate biosynthetic process [GO:0032962]; positive regulation of insulin secretion [GO:0032024]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of neurogenesis [GO:0050769]; positive regulation of neurotransmitter secretion [GO:0001956]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of uterine smooth muscle contraction [GO:0070474]; regulation of cell cycle [GO:0051726]; regulation of cytosolic calcium ion concentration [GO:0051480]; serotonin receptor signaling pathway [GO:0007210]; steroid hormone mediated signaling pathway [GO:0043401]; vasodilation [GO:0042311]
|
axon [GO:0030424]; axon terminus [GO:0043679]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; dendritic spine head [GO:0044327]; dendritic spine membrane [GO:0032591]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; keratin filament [GO:0045095]; mitochondrial membrane [GO:0031966]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; presynaptic active zone [GO:0048786]; presynaptic membrane [GO:0042734]; recycling endosome [GO:0055037]; trans-Golgi network [GO:0005802]
|
chromatin binding [GO:0003682]; estradiol binding [GO:1903924]; G protein-coupled estrogen receptor activity [GO:0038054]; nuclear estrogen receptor activity [GO:0030284]; steroid binding [GO:0005496]; steroid hormone binding [GO:1990239]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
|
PTM: Ubiquitinated; ubiquitination occurs at the plasma membrane and leads to proteasome-mediated degradation. {ECO:0000250}.; PTM: Glycosylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:22919059}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22919059}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21242460}; Multi-pass membrane protein {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Golgi apparatus membrane {ECO:0000269|PubMed:21242460, ECO:0000269|PubMed:22919059}; Multi-pass membrane protein. Cell projection, dendrite. Cell projection, dendritic spine membrane {ECO:0000269|PubMed:22919059, ECO:0000269|PubMed:23300088}; Multi-pass membrane protein. Cell projection, axon {ECO:0000269|PubMed:22919059}. Postsynaptic density {ECO:0000269|PubMed:22919059, ECO:0000269|PubMed:23300088}. Mitochondrion membrane {ECO:0000269|PubMed:22919059}; Multi-pass membrane protein. Note=Endocytosed in an agonist- and arrestin-independent manner. Colocalized with RAMP3 and clathrin-coated pits at the plasma membrane. Colocalized with transferrin receptor at the plasma membrane and perinuclear region. Accumulated and colocalized with RAB11 proteins in recycling endosomes and trans-Golgi network (TGN), but does neither recycle back to the cell surface nor traffics to late endosome or lysosome. Colocalized with calnexin in the endoplasmic reticulum. Traffics to intracellular sites via cytokeratin intermediate filaments like KRT7 and KRT8 after constitutive endocytosis in epithelial cells. Colocalized with EGFR in the nucleus of agonist-induced cancer-associated fibroblasts (CAF) (By similarity). Colocalized with BSN to the active zone of presynaptic density. Colocalized with DLG4/PSD95 and neurabin-2 PPP1R9B in neuronal synaptosomes. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: G-protein coupled estrogen receptor that binds to 17-beta-estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Stimulates cAMP production, calcium mobilization and tyrosine kinase Src inducing the release of heparin-bound epidermal growth factor (HB-EGF) and subsequent transactivation of the epidermal growth factor receptor (EGFR), activating downstream signaling pathways such as PI3K/Akt and ERK/MAPK. Mediates pleiotropic functions among others in the cardiovascular, endocrine, reproductive, immune and central nervous systems. Has a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a RAMP3-dependent manner. Regulates arterial blood pressure by stimulating vasodilation and reducing vascular smooth muscle and microvascular endothelial cell proliferation. Plays a role in blood glucose homeostasis contributing to the insulin secretion response by pancreatic beta cells. Triggers mitochondrial apoptosis during pachytene spermatocyte differentiation. Stimulates uterine epithelial cell proliferation. Enhances uterine contractility in response to oxytocin. Contributes to thymic atrophy by inducing apoptosis. Attenuates TNF-mediated endothelial expression of leukocyte adhesion molecules. Promotes neuritogenesis in developing hippocampal neurons. Plays a role in acute neuroprotection against NMDA-induced excitotoxic neuronal death. Increases firing activity and intracellular calcium oscillations in luteinizing hormone-releasing hormone (LHRH) neurons. Inhibits early osteoblast proliferation at growth plate during skeletal development. Inhibits mature adipocyte differentiation and lipid accumulation. Involved in the recruitment of beta-arrestin 2 ARRB2 at the plasma membrane in epithelial cells. Functions also as a receptor for aldosterone mediating rapid regulation of vascular contractibility through the PI3K/ERK signaling pathway. Involved in cancer progression regulation. Stimulates cancer-associated fibroblast (CAF) proliferation by a rapid genomic response through the EGFR/ERK transduction pathway. Associated with EGFR, may act as a transcription factor activating growth regulatory genes (c-fos, cyclin D1). Promotes integrin alpha-5/beta-1 and fibronectin (FN) matrix assembly in breast cancer cells. {ECO:0000269|PubMed:19179659, ECO:0000269|PubMed:20132863}.
|
Rattus norvegicus (Rat)
|
O08888
|
PTSS2_CRIGR
|
MRRAERRVAGGSGSGSPLLEGRRSTESEVYDDGTNTFFWRAHTLTVLFILTCSLGYVTLLEETPQDTAYNTKRGIVASILVFLCFGVTQAKDGPFSRPHPAYWRFWLCVSVVYELFLIFILFQTVQDGRQFLKYVDPRLGVPLPERDYGGNCLIYDADNKTDPFHNIWDKLDGFVPAHFIGWYLKTLMIRDWWMCMIISVMFEFLEYSLEHQLPNFSECWWDHWIMDVLICNGLGIYCGMKTLEWLSLKTYKWQGLWNIPTYKGKMKRIAFQFTPYSWVRFEWKPASSLHRWLAVCGIILVFLLAELNTFYLKFVLWMPPEHYLVLLRLVFFVNVGGVAMREIYDFMDELKPHRKLGQQAWLVAAITVTELLIVVKYDPHTLTLSLPFYISQCWTLGSILVLTWTVWRFFLRDITMRYKETRRQKQQSHQGRAINNGDGHPGPDDDLLGTGTAEEEGSTNDSVPAEKEGASAAS
|
2.7.8.29
| null |
phosphatidylserine biosynthetic process [GO:0006659]
|
endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
|
L-serine-phosphatidylethanolamine phosphatidyltransferase activity [GO:0106245]
|
PF03034;
| null |
Phosphatidyl serine synthase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z1X2}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:12912985}. Note=Highly enriched in the mitochondria-associated membrane (MAM). {ECO:0000250|UniProtKB:Q9Z1X2}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine; Xref=Rhea:RHEA:27606, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262, ChEBI:CHEBI:57603, ChEBI:CHEBI:64612; EC=2.7.8.29; Evidence={ECO:0000269|PubMed:12912985, ECO:0000269|PubMed:3084470, ECO:0000269|PubMed:9235902}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27607; Evidence={ECO:0000305|PubMed:9235902}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + L-serine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + ethanolamine; Xref=Rhea:RHEA:41484, ChEBI:CHEBI:33384, ChEBI:CHEBI:57603, ChEBI:CHEBI:73007, ChEBI:CHEBI:75029; Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41485; Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphoethanolamine + L-serine = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphoserine + ethanolamine; Xref=Rhea:RHEA:41488, ChEBI:CHEBI:33384, ChEBI:CHEBI:57603, ChEBI:CHEBI:78261, ChEBI:CHEBI:78262; Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41489; Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + L-serine = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoserine + ethanolamine; Xref=Rhea:RHEA:41500, ChEBI:CHEBI:33384, ChEBI:CHEBI:57603, ChEBI:CHEBI:78268, ChEBI:CHEBI:78269; Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41501; Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphoethanolamine + L-serine = 1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphoserine + ethanolamine; Xref=Rhea:RHEA:41492, ChEBI:CHEBI:33384, ChEBI:CHEBI:57603, ChEBI:CHEBI:78265, ChEBI:CHEBI:78266; Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41493; Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CATALYTIC ACTIVITY: Reaction=1-(1Z-octadecenyl)-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphoethanolamine + L-serine = 1-(1Z-octadecenyl)-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phospho-L-serine + ethanolamine; Xref=Rhea:RHEA:41496, ChEBI:CHEBI:33384, ChEBI:CHEBI:57603, ChEBI:CHEBI:78263, ChEBI:CHEBI:78264; Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41497; Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + L-serine = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + ethanolamine; Xref=Rhea:RHEA:40795, ChEBI:CHEBI:33384, ChEBI:CHEBI:57603, ChEBI:CHEBI:75038, ChEBI:CHEBI:78260; Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40796; Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CATALYTIC ACTIVITY: Reaction=1-(1Z-octadecenyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + L-serine = 1-(1Z-octadecenyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + ethanolamine; Xref=Rhea:RHEA:41600, ChEBI:CHEBI:33384, ChEBI:CHEBI:57603, ChEBI:CHEBI:78340, ChEBI:CHEBI:78341; Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41601; Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; CATALYTIC ACTIVITY: Reaction=1-(1Z-octadecenyl)-2-(5Z,8Z,11Z,14Z- eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + L-serine = 1-(1Z-octadecenyl)-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-L-serine + ethanolamine; Xref=Rhea:RHEA:41604, ChEBI:CHEBI:33384, ChEBI:CHEBI:57603, ChEBI:CHEBI:78342, ChEBI:CHEBI:78343; Evidence={ECO:0000250|UniProtKB:Q9Z1X2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41605; Evidence={ECO:0000250|UniProtKB:Q9Z1X2};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=89 uM for L-serine {ECO:0000269|PubMed:12912985}; Vmax=0.29 nmol/h/ng enzyme for L-serine {ECO:0000269|PubMed:12912985};
|
PATHWAY: Phospholipid metabolism; phosphatidylserine biosynthesis.
| null | null |
FUNCTION: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine (PubMed:12912985, PubMed:9235902). Catalyzes the conversion of phosphatatidylethanolamine and does not act on phosphatidylcholine (PubMed:12912985, PubMed:9235902). Shows a substrate specificity for phosphatatidylethanolamine and does not act on phosphatidylcholine (By similarity). Can utilize both phosphatidylethanolamine (PE) plasmalogen and diacyl PE as substrate and the latter is six times better utilized, indicating the importance of an ester linkage at the sn-1 position (By similarity). Although it shows no sn-1 fatty acyl preference, exhibits significant preference towards docosahexaenoic acid (22:6n-3) compared with 18:1 or 20:4 at the sn-2 position (By similarity). {ECO:0000250|UniProtKB:Q9Z1X2, ECO:0000269|PubMed:12912985, ECO:0000269|PubMed:9235902}.
|
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
|
O08892
|
5HT1B_CAVPO
|
MGNPEASCTPPAVLGSQTGLPHANVSAPPNNCSAPSHIYQDSIALPWKVLLVVLLALITLATTLSNAFVIATVYRTRKLHTPANYLIASLAFTDLLVSILVMPISTMYTVTGRWTLGQALCDFWLSSDITCCTASIMHLCVIALDRYWAITDAVGYSAKRTPRRAAGMIALVWVFSICISLPPFFWRQAKAEEEVLDCLVNTDHVLYTVYSTGGAFYLPTLLLIALYGRIYVEARSRILKQTPNKTGKRLTRAQLITDSPGSTSSVTSINSRAPEVPCDSGSPVYVNQVKVRVSDALLEKKKLMAARERKATKTLGVILGAFIVCWLPFFIISLVMPICKDACWFHMAIFDFFTWLGYLNSLINPIIYTMSNEDFKQAFHKLIRFKCTT
| null | null |
adenylate cyclase-inhibiting serotonin receptor signaling pathway [GO:0007198]; behavior [GO:0007610]; bone remodeling [GO:0046849]; cellular response to alkaloid [GO:0071312]; cellular response to temperature stimulus [GO:0071502]; cellular response to xenobiotic stimulus [GO:0071466]; chemical synaptic transmission [GO:0007268]; G protein-coupled receptor internalization [GO:0002031]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger [GO:0007187]; negative regulation of serotonin secretion [GO:0014063]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; regulation of behavior [GO:0050795]; vasoconstriction [GO:0042310]
|
dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; G protein-coupled serotonin receptor complex [GO:0098666]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; serotonergic synapse [GO:0099154]
|
G protein-coupled serotonin receptor activity [GO:0004993]; neurotransmitter receptor activity [GO:0030594]; serotonin binding [GO:0051378]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
|
PTM: Phosphorylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9225276}; Multi-pass membrane protein {ECO:0000269|PubMed:9225276}.
| null | null | null | null | null |
FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries (By similarity). {ECO:0000250, ECO:0000269|PubMed:9225276}.
|
Cavia porcellus (Guinea pig)
|
O08900
|
IKZF3_MOUSE
|
MEDIQPTVELKSTEEQPLPTESPDALNDYSLPKPHEIENVDSREAPANEDEDAGEDSMKVKDEYSDRDENIMKPEPMGDAEESEMPYSYAREYSDYESIKLERHVPYDNSRPTGGKMNCDVCGLSCISFNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHTGEKPFKCHLCNYACQRRDALTGHLRTHSVEKPYKCEFCGRSYKQRSSLEEHKERCRAFLQNPDLGDAASVEARHIKAEMGSERALVLDRLASNVAKRKSSMPQKFIGEKRHCFDANYNPGYMYEKENEMMQTRMMDQAINNAISYLGAEALRPLVQTPPAPTSEMVPVISSVYPIALTRADMPNGAPQEMEKKRILLPEKILPSERGLSPNNSAQDSTDTDSNHEDRQHLYQQSHVVLPQARNGMPLLKEVPRSFELLKPPPICLRDSIKVINKEGEVMDVFRCDHCHVLFLDYVMFTIHMGCHGFRDPFECNMCGYRSHDRYEFSSHIARGEHRAMLK
| null | null |
B cell differentiation [GO:0030183]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of apoptotic process [GO:0042981]; regulation of B cell differentiation [GO:0045577]; regulation of B cell proliferation [GO:0030888]; regulation of lymphocyte differentiation [GO:0045619]; regulation of transcription by RNA polymerase II [GO:0006357]; response to bacterium [GO:0009617]; T cell differentiation [GO:0030217]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; histone deacetylase binding [GO:0042826]; metal ion binding [GO:0046872]; promoter-specific chromatin binding [GO:1990841]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]
|
PF00096;
|
3.30.160.60;
|
Ikaros C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9155026}. Cytoplasm {ECO:0000269|PubMed:9155026}.
| null | null | null | null | null |
FUNCTION: Transcription factor that plays an important role in the regulation of lymphocyte differentiation. Binds to GGGAA. Plays an essential role in regulation of B-cell differentiation, proliferation and maturation to an effector state. Involved in regulating BCL2 expression and controlling apoptosis in T-cells in an IL2-dependent manner. {ECO:0000269|PubMed:34155405, ECO:0000269|PubMed:9155026, ECO:0000269|PubMed:9806640}.
|
Mus musculus (Mouse)
|
O08901
|
BUB1_MOUSE
|
MDNLENVFRMFEAHMQSYTGNDPLGEWESFIKWVEENFPDNKEYLMTLLEHLMKEFLHKKNYHNDSRFINYCLKFAEYNSDRHQFFEFLYNQGIGTKSSYIYMSWAGHLEAQGELQHASAIFQTGIHNEAEPKELLQQQYRLFQARLTGIHLPAQATTSEPLHSAQILNQVMMTNSSPEKNSACVPKSQGSECSGVASSTCDEKSNMEQRVIMISKSECSVSSSVAPKPEAQQVMYCKEKLIRGDSEFSFEELRAQKYNQRKKHEQWVSEDRNYMKRKEANAFEEQLLKQKMDELHKKLHQVVELSHKDLPASENRPDVSLVCVGQNTCSQQELRGPSLSSISHQTSESSGEKPQEEPSVPLMVNAVNSTLLFPAANLPALPVPVSGQSLTDSRCVNQSVHEFMPQCGPETKEVCETNKVASINDFHTTPNTSLGMVQGTPCKVQPSPTVHTKEALGFIMDMFQAPTLPDISDDKDEWPSLDQNEDAFEAQFQKNAVSSGDWGVKKIMTLSSAFPIFEDGNKENYGLPQPKNKPLGARTFGERSLSKYSSRSNEMPHTDEFMDDSTVCGIRCNKTLAPSPKSIGDFTSAAQLSSTPFHKFPADLVQIPEDKENVVATQYTHMALDSCKENIVDLSKGRKLGPIQEKISASLPCPSQPATGGLFTQEAVFGLEAFKCTGIDHATVEDLSDANAGLQVECVQTLGNVNAPSFTVENPWDDELILKLLSGLSKPVTSYSNTFEWQSKLPAIKTKTEYQLGSLLVYVNHLLGEGAFAQVFEAIHGDVRNAKSEQKCILKVQRPANSWEFYIGMQLMERLKPEVHHMFIKFYSAHLFKNGSILVGELYSYGTLLNVINLYKNTSEKVMPQALVLTFAIRMLYMVEQVHSCEIIHGDIKPDNFILGHRFLEQADEDLATGLALIDLGQSIDMKLFPKGTVFTGKCETSGFQCPEMLSNKPWNYQIDYFGVAATIYCMLFGSYMKVKNEGGVWKPEGLFRRLPHLDMWEEFFHIMLNIPDCHNLPSLDFLRQNMKKLLEQQYSNKIKTLRNRLIVMLSEYKRSRK
|
2.7.11.1
| null |
cell division [GO:0051301]; chromosome segregation [GO:0007059]; intrinsic apoptotic signaling pathway [GO:0097193]; meiotic sister chromatid cohesion, centromeric [GO:0051754]; mitotic spindle assembly checkpoint signaling [GO:0007094]; phosphorylation [GO:0016310]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; regulation of sister chromatid cohesion [GO:0007063]
|
chromosome, centromeric region [GO:0000775]; condensed chromosome, centromeric region [GO:0000779]; kinetochore [GO:0000776]; nucleus [GO:0005634]; outer kinetochore [GO:0000940]
|
ATP binding [GO:0005524]; histone H2A kinase activity [GO:0140995]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF08311;PF00069;
|
1.25.40.430;6.10.130.20;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, BUB1 subfamily
|
PTM: Upon spindle-assembly checkpoint activation it is hyperphosphorylated and its kinase activity toward CDC20 is stimulated. Phosphorylation at Thr-595 is required for interaction with PLK1, phosphorylation at this site probably creates a binding site for the POLO-box domain of PLK1, thus enhancing the PLK1-BUB1 interaction (By similarity). {ECO:0000250}.; PTM: Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Note=Nuclear in interphase cells. Accumulates gradually during G1 and S phase of the cell cycle, peaks at G2/M, and drops dramatically after mitosis. Localizes to the outer kinetochore. Kinetochore localization is required for normal mitotic timing and checkpoint response to spindle damage and occurs very early in prophase. AURKB, KNL1 and INCENP are required for kinetochore localization (By similarity). {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase that performs 2 crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Has a key role in the assembly of checkpoint proteins at the kinetochore, being required for the subsequent localization of CENPF, BUB1B, CENPE and MAD2L1. Required for the kinetochore localization of PLK1. Required for centromeric enrichment of AUKRB in prometaphase. Plays an important role in defining SGO1 localization and thereby affects sister chromatid cohesion. Promotes the centromeric localization of TOP2A (By similarity). Acts as a substrate for anaphase-promoting complex or cyclosome (APC/C) in complex with its activator CDH1 (APC/C-Cdh1). Necessary for ensuring proper chromosome segregation and binding to BUB3 is essential for this function. Can regulate chromosome segregation in a kinetochore-independent manner. Can phosphorylate BUB3. The BUB1-BUB3 complex plays a role in the inhibition of APC/C when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1. Kinase activity is essential for inhibition of APC/CCDC20 and for chromosome alignment but does not play a major role in the spindle-assembly checkpoint activity. Mediates cell death in response to chromosome missegregation and acts to suppress spontaneous tumorigenesis. Essential during early and later stages of embryonic development. Necessary for postimplantation embryogenesis and proliferation of primary embryonic fibroblasts and plays an important role in spermatogenesis and fertility. {ECO:0000250|UniProtKB:O43683, ECO:0000269|PubMed:17925231, ECO:0000269|PubMed:17938250, ECO:0000269|PubMed:19772675}.
|
Mus musculus (Mouse)
|
O08908
|
P85B_MOUSE
|
MAGAEGFQYRAVYPFRRERPEDLELLPGDLLVVSRVALQALGVADGGERCPHNVGWMPGFNERTRQRGDFPGTYVEFLGPVALARPGPRPRGPRPLPARPLDGSSESGHILPDLAEQFSPPDPAPPILVKLVEAIEQAELDSECYSKPELPATRTDWSLSDLEQWDRTALYDAVKGFLLALPAAVVTPEAAAEAYRALREVAGPVGLVLEPPTLPLHQALTLRFLLQHLGRVARRAPSPDTAVHALASAFGPLLLRIPPSGGEGDGSEPVPDFPVLLLERLVQEHVEEQDAAPPALPPKPSKAKPAPTALANGGSPPSLQDAEWYWGDISREEVNERLRDTPDGTFLVRDASSKIQGEYTLTLRKGGNNKLIKVFHRDGHYGFSEPLTFCSVVELISHYRHESLAQYNAKLDTRLLYPVSKYQQDQVVKEDSIEAVGAQLKVYHQQYQDKSREYDQLYEEYTRTSQELQMKRTAIEAFNETIKIFEEQGQTQEKCSKEYLERFRREGNEKEMQRILLNSERLKSRIAEIHESRTKLEQDLRAQASDNREIDKRMNSLKPDLMQLRKIRDQYLVWLTQKGARQRKINEWLGIKNETEDQYSLMEDEDALPHHEERTWYVGKINRTQAEEMLSGKRDGTFLIRESSQRGCYACSVVVDGDTKHCVIYRTATGFGFAEPYNLYGSLKELVLHYQHASLVQHNDALTVTLAHPVRAPGPGPPSAAR
| null | null |
cellular response to insulin stimulus [GO:0032869]; insulin receptor signaling pathway [GO:0008286]; intracellular glucose homeostasis [GO:0001678]; negative regulation of cell migration involved in sprouting angiogenesis [GO:0090051]; negative regulation of MAPK cascade [GO:0043409]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; positive regulation of cell adhesion [GO:0045785]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein transport [GO:0015031]; regulation of actin filament polymerization [GO:0030833]; regulation of autophagy [GO:0010506]; regulation of protein localization to plasma membrane [GO:1903076]; regulation of stress fiber assembly [GO:0051492]; response to endoplasmic reticulum stress [GO:0034976]
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focal adhesion [GO:0005925]; nucleus [GO:0005634]; phosphatidylinositol 3-kinase complex [GO:0005942]; phosphatidylinositol 3-kinase complex, class IA [GO:0005943]
|
1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; phosphatidylinositol 3-kinase regulatory subunit binding [GO:0036312]; phosphotyrosine residue binding [GO:0001784]; protein heterodimerization activity [GO:0046982]; protein phosphatase binding [GO:0019903]; receptor tyrosine kinase binding [GO:0030971]
|
PF16454;PF00620;PF00017;
|
1.10.287.1490;1.10.555.10;3.30.505.10;2.30.30.40;
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PI3K p85 subunit family
|
PTM: Phosphorylated in response to signaling from activated receptor-type protein kinases. Dephosphorylated by PTPRJ. Dephosphorylated at Tyr-649 by PTPN13. Phosphorylation of Tyr-649 impairs while its dephosphorylation promotes interaction with FBXL2 and SCF(FBXL2)-mediated polyubiquitination. {ECO:0000250|UniProtKB:O00459}.; PTM: Ubiquitinated. Polyubiquitination by the SCF(FBXL2) complex probably promotes proteasomal degradation of PIK3R2. {ECO:0000250|UniProtKB:O00459}.
| null | null | null | null | null | null |
FUNCTION: Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Indirectly regulates autophagy (By similarity). Promotes nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (PubMed:20348926). {ECO:0000250|UniProtKB:O00459, ECO:0000269|PubMed:20348926}.
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Mus musculus (Mouse)
|
O08911
|
MK12_MOUSE
|
MSSPPPARKGFYRQEVTKTAWEVRAVYQDLQPVGSGAYGAVCSAVDSRTGNKVAIKKLYRPFQSELFAKRAYRELRLLKHMRHENVIGLLDVFTPDESLDDFTDFYLVMPFMGTDLGKLMKHETLSEDRIQFLVYQMLKGLKYIHAAGVIHRDLKPGNLAVNEDCELKILDFGLARQADSEMTGYVVTRWYRAPEVILNWMRYTQTVDIWSVGCIMAEMITGKILFKGNDHLDQLKEIMKITGTPPPEFVQKLQSAEAKNYMEGLPELEKKDFASVLTNASPQAVNLLERMLVLDAEQRVTAAEALTHPYFESLRDTEDEPKAQKYDDSFDDVDRTLEEWKRVTYKEVLSFKPPRQLGARVPKETAL
|
2.7.11.24
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 2 magnesium ions.;
|
cell cycle [GO:0007049]; intracellular signal transduction [GO:0035556]; myoblast differentiation [GO:0045445]; negative regulation of cell cycle [GO:0045786]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
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ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily
|
PTM: Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K3/MKK3 and MAP2K6/MKK6, which activates the enzyme. {ECO:0000269|PubMed:20004242}.; PTM: Ubiquitinated. Ubiquitination leads to degradation by the proteasome pathway (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Mitochondrial when associated with SH3BP5. In skeletal muscle colocalizes with SNTA1 at the neuromuscular junction and throughout the sarcolemma. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24;
| null | null | null | null |
FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK12 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in myoblast differentiation and also in the down-regulation of cyclin D1 in response to hypoxia in adrenal cells suggesting MAPK12 may inhibit cell proliferation while promoting differentiation. Phosphorylates DLG1. Following osmotic shock, MAPK12 in the cell nucleus increases its association with nuclear DLG1, thereby causing dissociation of DLG1-SFPQ complexes. This function is independent of its catalytic activity and could affect mRNA processing and/or gene transcription to aid cell adaptation to osmolarity changes in the environment. Regulates UV-induced checkpoint signaling and repair of UV-induced DNA damage and G2 arrest after gamma-radiation exposure. MAPK12 is involved in the regulation of SLC2A1 expression and basal glucose uptake in L6 myotubes; and negatively regulates SLC2A4 expression and contraction-mediated glucose uptake in adult skeletal muscle. C-Jun (JUN) phosphorylation is stimulated by MAPK14 and inhibited by MAPK12, leading to a distinct AP-1 regulation. MAPK12 is required for the normal kinetochore localization of PLK1, prevents chromosomal instability and supports mitotic cell viability. MAPK12-signaling is also positively regulating the expansion of transient amplifying myogenic precursor cells during muscle growth and regeneration. {ECO:0000269|PubMed:20026657, ECO:0000269|PubMed:21170151, ECO:0000269|PubMed:21558321}.
|
Mus musculus (Mouse)
|
O08912
|
GALT1_MOUSE
|
MRKFAYCKVVLATSLVWVLLDMFLLLYFSECNKCEEKQERGLPAGDVLELVQKPHEGPGEMGKPVVIPKEDQEKMKEMFKINQFNLMASEMIALNRSLPDVRLEGCKTKVYPDNLPTTSVVIVFHNEAWSTLLRTVHSVINRSPRHMIEEIVLVDDASERDFLKRPLESYVKKLKVPVHVIRMEQRSGLIRARLKGAAVSRGQVITFLDAHCECTAGWLEPLLARIKHDRRTVVCPIIDVISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREMDRRKGDRTLPVRTPTMAGGLFSIDRDYFQEIGTYDAGMDIWGGENLEISFRIWQCGGTLEIVTCSHVGHVFRKATPYTFPGGTGQIINKNNRRLAEVWMDEFKNFFYIISPGVTKVDYGDISSRLGLRRKLQCKPFSWYLENIYPDSQIPRHYFSLGEIRNVETNQCLDNMARKENEKVGIFNCHGMGGNQVFSYTANKEIRTDDLCLDVSKLNGPVTMLKCHHLKGNQLWEYDPVKLTLQHVNSNQCLDKATEEDSQVPSIRDCTGSRSQQWLLRNVTLPEIF
|
2.4.1.41
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:9153242};
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protein O-linked glycosylation [GO:0006493]; protein O-linked glycosylation via serine [GO:0018242]; protein O-linked glycosylation via threonine [GO:0018243]
|
extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; perinuclear region of cytoplasm [GO:0048471]
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carbohydrate binding [GO:0030246]; manganese ion binding [GO:0030145]; polypeptide N-acetylgalactosaminyltransferase activity [GO:0004653]
|
PF00535;PF00652;
|
2.80.10.50;
|
Glycosyltransferase 2 family, GalNAc-T subfamily
| null |
SUBCELLULAR LOCATION: [Polypeptide N-acetylgalactosaminyltransferase 1]: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Polypeptide N-acetylgalactosaminyltransferase 1 soluble form]: Secreted {ECO:0000250}.
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CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41; Evidence={ECO:0000269|PubMed:10037781, ECO:0000269|PubMed:9153242}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23957; Evidence={ECO:0000305|PubMed:10037781, ECO:0000305|PubMed:9153242}; CATALYTIC ACTIVITY: Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41; Evidence={ECO:0000269|PubMed:10037781, ECO:0000269|PubMed:9153242}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52425; Evidence={ECO:0000305|PubMed:10037781, ECO:0000305|PubMed:9153242};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:10037781, ECO:0000269|PubMed:9153242}.
| null | null |
FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor (PubMed:10037781, PubMed:9153242). Has a broad spectrum of substrates such as apomucin-, MUC5AC-, MUC1- and MUC2-derived peptides (By similarity). {ECO:0000250|UniProtKB:Q10472, ECO:0000269|PubMed:10037781, ECO:0000269|PubMed:9153242}.
|
Mus musculus (Mouse)
|
O08914
|
FAAH1_MOUSE
|
MVLSEVWTALSGLSGVCLACSLLSAAVVLRWTRSQTARGAVTRARQKQRAGLETMDKAVQRFRLQNPDLDSEALLALPLLQLVQKLQSGELSPEAVLFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPRQGLLYGVPVSLKECFSYKGHASTLGLSLNEGVTSESDCVVVQVLKLQGAVPFVHTNVPQSMLSYDCSNPLFGQTMNPWKPSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKSCVYGQTAVQLSVGPMARDVDSLALCMKALLCEDLFRLDSTIPPLPFREEIYRSSRPLRVGYYETDNYTMPTPAMRRAVMETKQSLEAAGHTLVPFLPNNIPYALEVLSAGGLFSDGGCSFLQNFKGDFVDPCLGDLVLVLKLPRWFKKLLSFLLKPLFPRLAAFLNSMCPRSAEKLWELQHEIEMYRQSVIAQWKAMNLDVVLTPMLGPALDLNTPGRATGAISYTVLYNCLDFPAGVVPVTTVTAEDDAQMEHYKGYFGDMWDNILKKGMKKGIGLPVAVQCVALPWQEELCLRFMREVERLMTPEKRPS
|
3.1.1.-; 3.5.1.99
| null |
fatty acid catabolic process [GO:0009062]; fatty acid metabolic process [GO:0006631]; monoacylglycerol catabolic process [GO:0052651]; positive regulation of vasoconstriction [GO:0045907]
|
endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; organelle membrane [GO:0031090]
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acylglycerol lipase activity [GO:0047372]; amidase activity [GO:0004040]; fatty acid amide hydrolase activity [GO:0017064]; hydrolase activity, acting on ester bonds [GO:0016788]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; phospholipid binding [GO:0005543]
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PF01425;
|
3.90.1300.10;
|
Amidase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:32271712}; Single-pass membrane protein {ECO:0000250|UniProtKB:P97612}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P97612}; Single-pass membrane protein {ECO:0000250|UniProtKB:P97612}. Note=Seems to be associated with the endoplasmic reticulum and/or Golgi apparatus. {ECO:0000250|UniProtKB:P97612}.
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CATALYTIC ACTIVITY: Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + ethanolamine; Xref=Rhea:RHEA:26136, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:57603; EC=3.5.1.99; Evidence={ECO:0000269|PubMed:15533037, ECO:0000269|PubMed:32271712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26137; Evidence={ECO:0000269|PubMed:15533037, ECO:0000269|PubMed:32271712}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenamide + H2O = (9Z)-octadecenoate + NH4(+); Xref=Rhea:RHEA:26506, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:30823, ChEBI:CHEBI:116314; EC=3.5.1.99; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26507; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-hexadecenoyl) ethanolamine = (9Z)-hexadecenoate + ethanolamine; Xref=Rhea:RHEA:35563, ChEBI:CHEBI:15377, ChEBI:CHEBI:32372, ChEBI:CHEBI:57603, ChEBI:CHEBI:71465; Evidence={ECO:0000269|PubMed:15533037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35564; Evidence={ECO:0000269|PubMed:15533037}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl) ethanolamine = (9Z)-octadecenoate + ethanolamine; Xref=Rhea:RHEA:45060, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:57603, ChEBI:CHEBI:71466; Evidence={ECO:0000269|PubMed:15533037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45061; Evidence={ECO:0000269|PubMed:15533037}; CATALYTIC ACTIVITY: Reaction=H2O + N-octadecanoyl ethanolamine = ethanolamine + octadecanoate; Xref=Rhea:RHEA:63124, ChEBI:CHEBI:15377, ChEBI:CHEBI:25629, ChEBI:CHEBI:57603, ChEBI:CHEBI:85299; Evidence={ECO:0000269|PubMed:15533037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63125; Evidence={ECO:0000269|PubMed:15533037}; CATALYTIC ACTIVITY: Reaction=H2O + N-docosanoyl-ethanolamine = docosanoate + ethanolamine; Xref=Rhea:RHEA:63128, ChEBI:CHEBI:15377, ChEBI:CHEBI:23858, ChEBI:CHEBI:57603, ChEBI:CHEBI:146186; Evidence={ECO:0000269|PubMed:15533037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63129; Evidence={ECO:0000269|PubMed:15533037}; CATALYTIC ACTIVITY: Reaction=H2O + N-tetracosanoyl-taurine = taurine + tetracosanoate; Xref=Rhea:RHEA:63140, ChEBI:CHEBI:15377, ChEBI:CHEBI:31014, ChEBI:CHEBI:132049, ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:15533037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63141; Evidence={ECO:0000269|PubMed:15533037}; CATALYTIC ACTIVITY: Reaction=H2O + N-(15Z-tetracosenoyl)-ethanolamine = (15Z)-tetracosenoate + ethanolamine; Xref=Rhea:RHEA:63144, ChEBI:CHEBI:15377, ChEBI:CHEBI:32392, ChEBI:CHEBI:57603, ChEBI:CHEBI:146187; Evidence={ECO:0000305|PubMed:15533037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63145; Evidence={ECO:0000305|PubMed:15533037}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-taurine = (9Z)-octadecenoate + taurine; Xref=Rhea:RHEA:63148, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:146191, ChEBI:CHEBI:507393; Evidence={ECO:0000305|PubMed:15533037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63149; Evidence={ECO:0000305|PubMed:15533037}; CATALYTIC ACTIVITY: Reaction=H2O + N-docosanoyl-taurine = docosanoate + taurine; Xref=Rhea:RHEA:63156, ChEBI:CHEBI:15377, ChEBI:CHEBI:23858, ChEBI:CHEBI:146196, ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:15533037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63157; Evidence={ECO:0000269|PubMed:15533037}; CATALYTIC ACTIVITY: Reaction=H2O + N-(15Z-tetracosenoyl)-taurine = (15Z)-tetracosenoate + taurine; Xref=Rhea:RHEA:63160, ChEBI:CHEBI:15377, ChEBI:CHEBI:32392, ChEBI:CHEBI:146198, ChEBI:CHEBI:507393; Evidence={ECO:0000305|PubMed:15533037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63161; Evidence={ECO:0000305|PubMed:15533037}; CATALYTIC ACTIVITY: Reaction=H2O + N-tricosanoyl-taurine = taurine + tricosanoate; Xref=Rhea:RHEA:63164, ChEBI:CHEBI:15377, ChEBI:CHEBI:79007, ChEBI:CHEBI:146197, ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:15533037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63165; Evidence={ECO:0000269|PubMed:15533037}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienamide + H2O = (9Z,12Z,15Z)-octadecatrienoate + NH4(+); Xref=Rhea:RHEA:62976, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:32387, ChEBI:CHEBI:142684; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62977; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenamide + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + NH4(+); Xref=Rhea:RHEA:63016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:32395, ChEBI:CHEBI:137830; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63017; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=(6Z)-octadecenamide + H2O = (6Z)-octadecenoate + NH4(+); Xref=Rhea:RHEA:63008, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:32375, ChEBI:CHEBI:146168; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63009; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=(15Z)-tetracosenamide + H2O = (15Z)-tetracosenoate + NH4(+); Xref=Rhea:RHEA:63028, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:32392, ChEBI:CHEBI:146166; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63029; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienamide + H2O = (8Z,11Z,14Z)-eicosatrienoate + NH4(+); Xref=Rhea:RHEA:62996, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:71589, ChEBI:CHEBI:146163; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62997; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=(11Z,14Z,17Z)-eicosatrienamide + H2O = (11Z,14Z,17Z)-eicosatrienoate + NH4(+); Xref=Rhea:RHEA:63000, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:77223, ChEBI:CHEBI:146164; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63001; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=(11Z,14Z)-eicosadienamide + H2O = (11Z,14Z)-eicosadienoate + NH4(+); Xref=Rhea:RHEA:63004, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:77220, ChEBI:CHEBI:146165; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63005; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienamide + H2O = (9Z,12Z)-octadecadienoate + NH4(+); Xref=Rhea:RHEA:63020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:30245, ChEBI:CHEBI:82984; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63021; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecamide = NH4(+) + tetradecanoate; Xref=Rhea:RHEA:62992, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:30807, ChEBI:CHEBI:137125; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62993; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + methanol; Xref=Rhea:RHEA:63052, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:32395, ChEBI:CHEBI:78033; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63053; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=(11Z)-eicosenamide + H2O = (11Z)-eicosenoate + NH4(+); Xref=Rhea:RHEA:63120, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:32426, ChEBI:CHEBI:146167; Evidence={ECO:0000250|UniProtKB:P97612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63121; Evidence={ECO:0000250|UniProtKB:P97612}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + glycine = H2O + N-(9Z-octadecenoyl)glycine; Xref=Rhea:RHEA:51316, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:57305, ChEBI:CHEBI:133992; Evidence={ECO:0000269|PubMed:32271712}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51318; Evidence={ECO:0000269|PubMed:32271712}; CATALYTIC ACTIVITY: Reaction=H2O + N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycine; Xref=Rhea:RHEA:64108, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:57305, ChEBI:CHEBI:59002; Evidence={ECO:0000269|PubMed:32271712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64109; Evidence={ECO:0000269|PubMed:32271712}; CATALYTIC ACTIVITY: Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-serine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + L-serine; Xref=Rhea:RHEA:64116, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:33384, ChEBI:CHEBI:149697; Evidence={ECO:0000269|PubMed:32271712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64117; Evidence={ECO:0000269|PubMed:32271712};
| null | null | null | null |
FUNCTION: Catalyzes the hydrolysis of endogenous amidated lipids like the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides such as the taurine-conjugated fatty acids (a structural class of central nervous system (CNS) metabolites), to their corresponding fatty acids, thereby regulating the signaling functions of these molecules (PubMed:15533037, PubMed:32271712). FAAH cooperates with PM20D1 in the hydrolysis of amino acid-conjugated fatty acids such as N-fatty acyl glycine and N-fatty acyl-L-serine, thereby acting as a physiological regulator of specific subsets of intracellular, but not of extracellular, N-fatty acyl amino acids (PubMed:32271712). It can also catalyze the hydrolysis of the endocannabinoid 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol) (By similarity). {ECO:0000250|UniProtKB:P97612, ECO:0000269|PubMed:15533037, ECO:0000269|PubMed:32271712}.
|
Mus musculus (Mouse)
|
O08915
|
AIP_MOUSE
|
MADLIARLREDGIQKRVIQEGRGELPDFQDGTKATFHFRTLHSDNEGSVIDDSRTRGKPMELIVGKKFKLPVWETIVCTMREGEIAQFLCDIKHVVLYPLVAKSLRNIAEGKDPLEGQRHCCGIAQMHEHSSLGHADLDALQQNPQPLIFHIEMLKVESPGTYQQDPWAMTDEEKAKAVPVIHQEGNRLYREGQVKEAAAKYYDAIACLKNLQMKEQPGSPDWIQLDLQITPLLLNYCQCKLVAQEYYEVLDHCSSILNKYDDNVKAYFKRGKAHAAVWNAQEAQADFAKVLELDPALAPVVSRELRALETRIRQKDEEDKARFRGIFSH
| null | null |
protein maturation by protein folding [GO:0022417]; protein targeting to mitochondrion [GO:0006626]; regulation of protein kinase A signaling [GO:0010738]; xenobiotic metabolic process [GO:0006805]
|
aryl hydrocarbon receptor complex [GO:0034751]; cytosol [GO:0005829]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
aryl hydrocarbon receptor binding [GO:0017162]; GAF domain binding [GO:0036004]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; transcription coregulator activity [GO:0003712]; unfolded protein binding [GO:0051082]
|
PF00254;
|
3.10.50.40;1.25.40.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: May play a positive role in AHR-mediated (aromatic hydrocarbon receptor) signaling, possibly by influencing its receptivity for ligand and/or its nuclear targeting.
|
Mus musculus (Mouse)
|
O08917
|
FLOT1_MOUSE
|
MFFTCGPNEAMVVSGFCRSPPVMVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKATYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEAEAFAIGARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVTGEVLDILSRLPESVERLTGVSISQVNHNKPLRTA
| null | null |
axon guidance [GO:0007411]; axonogenesis [GO:0007409]; cellular response to exogenous dsRNA [GO:0071360]; dsRNA transport [GO:0033227]; endocytosis [GO:0006897]; extracellular matrix disassembly [GO:0022617]; plasma membrane raft assembly [GO:0044854]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell junction assembly [GO:1901890]; positive regulation of cell-cell adhesion mediated by cadherin [GO:2000049]; positive regulation of endocytosis [GO:0045807]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of myoblast fusion [GO:1901741]; positive regulation of protein binding [GO:0032092]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of skeletal muscle tissue development [GO:0048643]; positive regulation of synaptic transmission, dopaminergic [GO:0032226]; positive regulation of toll-like receptor 3 signaling pathway [GO:0034141]; protein kinase C signaling [GO:0070528]; protein localization to plasma membrane [GO:0072659]; protein stabilization [GO:0050821]; regulation of neurotransmitter uptake [GO:0051580]; regulation of receptor internalization [GO:0002090]; regulation of Rho protein signal transduction [GO:0035023]; response to endoplasmic reticulum stress [GO:0034976]
|
adherens junction [GO:0005912]; basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; cell-cell contact zone [GO:0044291]; centriolar satellite [GO:0034451]; COP9 signalosome [GO:0008180]; cortical actin cytoskeleton [GO:0030864]; cytoplasmic vesicle [GO:0031410]; dopaminergic synapse [GO:0098691]; early endosome [GO:0005769]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; flotillin complex [GO:0016600]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; lamellipodium [GO:0030027]; melanosome [GO:0042470]; membrane [GO:0016020]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853]; presynapse [GO:0098793]; presynaptic active zone [GO:0048786]; sarcolemma [GO:0042383]; synapse [GO:0045202]; uropod [GO:0001931]
|
ionotropic glutamate receptor binding [GO:0035255]; protease binding [GO:0002020]
|
PF01145;PF15975;
|
3.30.479.30;
|
Band 7/mec-2 family, Flotillin subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75955}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75955}. Endosome {ECO:0000250|UniProtKB:O75955}. Membrane, caveola {ECO:0000269|PubMed:9153235}; Peripheral membrane protein {ECO:0000269|PubMed:9153235}. Melanosome {ECO:0000250|UniProtKB:O75955}. Membrane raft {ECO:0000250|UniProtKB:O75955}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). Membrane-associated protein of caveola (PubMed:9153235). {ECO:0000250|UniProtKB:O75955, ECO:0000269|PubMed:9153235}.
| null | null | null | null | null |
FUNCTION: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.
|
Mus musculus (Mouse)
|
O08919
|
NUMBL_MOUSE
|
MSRSAAASGGPRRPDQHLSPAPCGASGPPETFRTESDGAGTMNKLRQSLRRRKPAYVPEASRPHQWQADEDAVRKGTCSFPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRNLDKAFSYICRDGTTRRWICHCFLALKDSGERLSHAVGCAFAACLERKQRREKECGVTAAFDASRTSFAREGSFRLSGGGRPAEREAGDKKKAEAAAAPAVAPGPAQPGHVSPTPATTSPGEKGEAGTPVAAGTTAAAIPRRHAPLEQLVRQGSFRGFPALSQKNSPFKRQLSLRLNELPSTLQRRTDFQVKGTVPEMEPPGTGDSDGINALCTQISSSFASAGAPASGPPPATTGTSAWGEPSVPAAAAFQPGHKRTPSEAERWLEEVSQVAKAQQQQQQQQQQQQQQQATSVPPMPTMAPTLQPFSAPVGPFDTAAAQVAVFLPPTHMQPPFVPAYPGLGYPPMPRVPVVGITPSQMVANAFCSAAQLQPQPATLLGKAGAFPPPAAPSAPGGQARPRPNGAPWPPEPAPAPAPELDPFEAQWAALEGKPAVEKPSNPFSGDLQKTFEIEL
| null | null |
adherens junction organization [GO:0034332]; axonogenesis [GO:0007409]; cytokine-mediated signaling pathway [GO:0019221]; forebrain development [GO:0030900]; lateral ventricle development [GO:0021670]; nervous system development [GO:0007399]; neuroblast division in subventricular zone [GO:0021849]; neuroblast proliferation [GO:0007405]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of neurogenesis [GO:0050769]; protein metabolic process [GO:0019538]; regulation of postsynapse assembly [GO:0150052]
|
cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]
| null |
PF06311;PF00640;
|
2.30.29.30;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9169836}. Note=Symmetrically distributed throughout the cytoplasm in non dividing neuroblasts of the CNS.
| null | null | null | null | null |
FUNCTION: Plays a role in the process of neurogenesis. Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate. Not required for the proliferation of neural progenitor cells before the onset of embryonic neurogenesis. Also required postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity. Negative regulator of NF-kappa-B signaling pathway. The inhibition of NF-kappa-B activation is mediated at least in part, by preventing MAP3K7IP2 to interact with polyubiquitin chains of TRAF6 and RIPK1 and by stimulating the 'Lys-48'-linked polyubiquitination and degradation of TRAF6 in cortical neurons. {ECO:0000269|PubMed:12410312, ECO:0000269|PubMed:15273690, ECO:0000269|PubMed:17174898, ECO:0000269|PubMed:9169836}.
|
Mus musculus (Mouse)
|
O08934
|
UNC4_MOUSE
|
MMDGRLLEHPHAQFGGSLGGVVGFPYPLGHHHVYELAGHQLQSAAAAAAAASVPFSIDGLLSGSCAAAAASVVNPTPLLPAACGVAGESQPFKLADSGDPDKESPGCKRRRTRTNFTGWQLEELEKAFNESHYPDVFMREALALRLDLVESRVQVWFQNRRAKWRKKENTKKGPGRPAHNSHPTTCSGEPMDPEEIARKELEKMEKKKRKHEKKLLKSQSRHLHSPGGLSLHSAPSSDSDSGGGGLSPEPPEPPPPTAAAKGPGAHGSGIAGSAPVPPGEPPAPGTCDPAFYPSQRSGAGSQPRLGRPADKDTVPCGPGAAATAGLPKASPFSVESLLSDSPPRRKATPANAAATAGLDFTPGLPCAPRTLIGKGHFLLYPITQPLGFLVPQAALKGGAGPELVPKDAPPAPPAPPAPPAQASFGTFPGPGGAADPAFARRSPEVVASPGPPAPASFRDLTAAAAESGAGDCADVGTVCPAASPPPPLETSPGPGPRAPSPPGEPATCGAAEPGAATGPSPPEGEEVDMD
| null | null |
cartilage condensation [GO:0001502]; common myeloid progenitor cell proliferation [GO:0035726]; dorsal spinal cord development [GO:0021516]; olfactory bulb interneuron differentiation [GO:0021889]; pattern specification process [GO:0007389]; regulation of cell differentiation [GO:0045595]; regulation of gene expression [GO:0010468]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00046;
|
1.10.10.60;
|
Paired homeobox family, Unc-4 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
| null | null | null | null | null |
FUNCTION: Transcription factor involved in somitogenesis and neurogenesis. Required for the maintenance and differentiation of particular elements of the axial skeleton. May act upstream of PAX9. Plays a role in controlling the development of connections of hypothalamic neurons to pituitary elements, allowing central neurons to reach the peripheral blood circulation and to deliver hormones for control of peripheral functions. {ECO:0000269|PubMed:10804168, ECO:0000269|PubMed:10804169, ECO:0000269|PubMed:16461927}.
|
Mus musculus (Mouse)
|
O08949
|
TF2AA_RAT
|
MANSANTNTVPKLYRSVIEDVINDVRDIFLDDGVDEQVLMELKTLWENKLMQSRAVDGFHSEEQQLLLQVQQQHQPQQQQHHHHHHHQQAQPQQTVPQQAQTQQVLIPASQQATAPQVIVPDSKLIQHMNASSITSAAATAATLALPAGVTPVQQILTNSGQLLQVVRAANGAQYIFQPQQSVVLQQQVIPQMQPGGVQAPVIQQVLAPLPGGISPQTGVIIQPQQILFTGNKTQVIPTTVAAPTPAQAQIPAAGQQQPQAQPAQQQAPLVLQVDGTGDTSSEEDEDEEEDYDDDEEEDKEKDGAEDGQVEEEPLNSEDDVSDEEGQELFDTENVVVCQYDKIHRSKNKWKFHLKDGIMNLNGRDYIFSKAIGDAEW
| null | null |
positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; transcription by RNA polymerase II [GO:0006366]; transcription initiation at RNA polymerase II promoter [GO:0006367]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; transcription factor TFIIA complex [GO:0005672]; transcription factor TFIID complex [GO:0005669]; transcription preinitiation complex [GO:0097550]
|
DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II general transcription initiation factor activity [GO:0016251]; RNA polymerase II general transcription initiation factor binding [GO:0001091]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; TBP-class protein binding [GO:0017025]
|
PF03153;
|
1.10.287.100;2.30.18.10;
|
TFIIA subunit 1 family
|
PTM: The alpha and beta subunits are postranslationally produced from the precursor formby TASP1. The cleavage promotes proteasomal degradation (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O08954
|
SNAI2_RAT
|
MPRSFLVKKHFNASKKPNYSELDTHTVIISPYLCESYPMPVIPKPEILTSGAYSPITVWTSAVPFHSPLPSGLSPLTGYSSSLGRVSPLPSSDTSSKDHSGSESPISDEEERLQPKLSDPHAIEAEKFQCNLCNKTYSTFSGLAKHKQLHCDAQARKSFSCKYCDKEYVSLGALKMHIRTHTLPCVCKICGKAFSRPWLLQGHIRTHTGEKPFSCPHCNRAFADRSNLRAHLQTHSDVKKYQCKNCSKTFSRMSLLHKHEESGCCVAH
| null | null |
cartilage morphogenesis [GO:0060536]; cell migration involved in endocardial cushion formation [GO:0003273]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to ionizing radiation [GO:0071479]; chromatin organization [GO:0006325]; desmosome disassembly [GO:0035921]; endothelial cell migration [GO:0043542]; epithelial cell migration [GO:0010631]; epithelial to mesenchymal transition [GO:0001837]; epithelial to mesenchymal transition involved in endocardial cushion formation [GO:0003198]; epithelium development [GO:0060429]; hematopoietic stem cell proliferation [GO:0071425]; myeloid cell apoptotic process [GO:0033028]; negative regulation of anoikis [GO:2000811]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell adhesion involved in substrate-bound cell migration [GO:0006933]; negative regulation of cell adhesion mediated by integrin [GO:0033629]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of hematopoietic stem cell proliferation [GO:1902034]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [GO:1902230]; negative regulation of keratinocyte proliferation [GO:0010839]; negative regulation of myeloid cell apoptotic process [GO:0033033]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of vitamin D biosynthetic process [GO:0010957]; negative regulation of vitamin D receptor signaling pathway [GO:0070563]; neural crest cell development [GO:0014032]; Notch signaling pathway [GO:0007219]; osteoblast differentiation [GO:0001649]; pigmentation [GO:0043473]; positive regulation of cell migration [GO:0030335]; positive regulation of fat cell differentiation [GO:0045600]; regulation of bicellular tight junction assembly [GO:2000810]; regulation of branching involved in salivary gland morphogenesis [GO:0060693]; regulation of chemokine production [GO:0032642]; regulation of DNA-templated transcription [GO:0006355]; regulation of osteoblast differentiation [GO:0045667]; response to radiation [GO:0009314]; roof of mouth development [GO:0060021]; sensory perception of sound [GO:0007605]; substrate-dependent cell migration [GO:0006929]; white fat cell differentiation [GO:0050872]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00096;
|
3.30.160.60;
|
Snail C2H2-type zinc-finger protein family
|
PTM: GSK3B-mediated phosphorylation results in cytoplasmic localization and degradation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43623}. Cytoplasm {ECO:0000250}. Note=Observed in discrete foci in interphase nuclei. These nuclear foci do not overlap with the nucleoli, the SP100 and the HP1 heterochromatin or the coiled body, suggesting SNAI2 is associated with active transcription or active splicing regions (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Transcriptional repressor that modulates both activator-dependent and basal transcription. Involved in the generation and migration of neural crest cells. Plays a role in mediating RAF1-induced transcriptional repression of the TJ protein, occludin (OCLN) and subsequent oncogenic transformation of epithelial cells. Represses BRCA2 expression by binding to its E2-box-containing silencer and recruiting CTBP1 and HDAC1 in breast cells. In epidermal keratinocytes, binds to the E-box in ITGA3 promoter and represses its transcription. Involved in the regulation of ITGB1 and ITGB4 expression and cell adhesion and proliferation in epidermal keratinocytes. Binds to E-box2 domain of BSG and activates its expression during TGFB1-induced epithelial-mesenchymal transition (EMT) in hepatocytes. Represses E-Cadherin/CDH1 transcription via E-box elements. Involved in osteoblast maturation. Binds to RUNX2 and SOC9 promoters and may act as a positive and negative transcription regulator, respectively, in osteoblasts. Binds to CXCL12 promoter via E-box regions in mesenchymal stem cells and osteoblasts. Plays an essential role in TWIST1-induced EMT and its ability to promote invasion and metastasis (By similarity). {ECO:0000250, ECO:0000269|PubMed:16924233}.
|
Rattus norvegicus (Rat)
|
O08961
|
ZN423_RAT
|
MSRRKQAKPRSVKVEEGEASDFSLAWDSSVAAAGGLEGESECDRKSSRALEDRNSVTSQEERNEDDEDVEDESIYTCDHCQQDFESLADLTDHRAHRCPGDGDDDPQLSWVASSPSSKDVASPTQMIGDGCDLGLGEEEGGTGLPYPCQFCDKSFIRLSYLKRHEQIHSDKLPFKCTFCSRLFKHKRSRDRHIKLHTGDKKYHCHECEAAFSRRDHLKIHLKTHSSSKPFKCSVCKRGFSSTSSLQSHMQAHKKNKEHLAKSEKEAKKDDFMCDYCEDTFSQTEELEKHVLTLHPQLSEKADLQCIHCPEVFVDESTLLAHIHQAHANQKHKCPMCPEQFSSVEGVYCHLDSHRQPDSSNHSVSPDPVLGSVASMSSATPDSTPDPVLGSVASMSSATPDSSASVERGSTPDSTLKPLRGQKKMRDDGQSWSKVVYSCPYCSKRDFTSLAVLEIHLKTIHADKPQQSHTCQICLDSMPTLYNLNEHVRKLHKSHAYPVMQFGNISAFHCNYCPEMFADINSLQEHIRVSHCGPNANPPDGNNAFFCNQCSMGFLTESSLTEHIQQAHCSVGSTKLESPVIQPTQSFMEVYSCPYCTNSPIFGSILKLTKHIKENHKNIPLAHSKKSKAEQSPVSSDVEVSSPKRQRLSGSANSISNGEYPCNQCDLKFSNFESFQTHLKLHLELLLRKQACPQCKEDFDSQESLLQHLTVHYMTTSTHYVCESCDKQFSSVDDLQKHLLDMHTFVLYHCTLCQEVFDSKVSIQVHLAVKHSNEKKMYRCTACNWDFRKEADLQVHVKHSHLGNPAKAHKCIFCGETFSTEVELQCHITTHSKKYNCRFCSKAFHAVLLLEKHLREKHCVFDPAAENGTANGVPPTSTKKAEPADLQGMLLKNPEAPNSHEASEDDVDASEPMYGCDICGAAYTMEVLLQNHRLRDHNIRPGEDDGSRKKAEFIKGSHKCNVCSRTFFSENGLREHLQTHRGPAKHYMCPICGERFPSLLTLTEHKVTHSKSLDTGTCRICKMPLQSEEEFIEHCQMHPDLRNSLTGFRCVVCMQTVTSTLELKIHGTFHMQKLAGSSAASSPNGQGLQKLYKCALCLKEFRSKQDLVRLDVNGLPYGLCAGCMARSANGQVGGLAPPEPADRPCAGLRCPECNVKFESAEDLESHMQVDHRDLTPETSGPRKGAQTSPVPRKKTYQCIKCQMTFENEREIQIHVANHMIEEGINHECKLCNQMFDSPAKLLCHLIEHSFEGMGGTFKCPVCFTVFVQANKLQQHIFAVHGQEDKIYDCSQCPQKFFFQTELQNHTMSQHAQ
| null | null |
brown fat cell differentiation [GO:0050873]; cerebellar granule cell precursor proliferation [GO:0021930]; cilium assembly [GO:0060271]; negative regulation of cold-induced thermogenesis [GO:0120163]; negative regulation of DNA-templated transcription [GO:0045892]; Notch signaling pathway [GO:0007219]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of DNA-templated transcription [GO:0045893]; protein localization to cilium [GO:0061512]; regulation of transcription by RNA polymerase II [GO:0006357]; smoothened signaling pathway [GO:0007224]; white fat cell differentiation [GO:0050872]
|
chromosome [GO:0005694]; nucleus [GO:0005634]
|
chromatin insulator sequence binding [GO:0043035]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein-containing complex binding [GO:0044877]; sequence-specific DNA binding [GO:0043565]
|
PF00096;PF13912;
|
3.30.160.60;
|
Krueppel C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Transcription factor that can both act as an activator or a repressor depending on the context. Plays a central role in BMP signaling and olfactory neurogenesis. Associates with SMADs in response to BMP2 leading to activate transcription of BMP target genes. Acts as a transcriptional repressor via its interaction with EBF1, a transcription factor involved in terminal olfactory receptor neurons differentiation; this interaction preventing EBF1 to bind DNA and activate olfactory-specific genes. Involved in olfactory neurogenesis by participating in a developmental switch that regulates the transition from differentiation to maturation in olfactory receptor neurons. Controls proliferation and differentiation of neural precursors in cerebellar vermis formation. {ECO:0000269|PubMed:9151733}.
|
Rattus norvegicus (Rat)
|
O08962
|
KCNH2_RAT
|
MPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARVENCAVIYCNDGFCELCGYSRAEVMQRPCTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDGAVIMFILNFEVVMEKDMVGSPAHDTNHRGPSTSWLASGRAKTFRLKLPALLALTARESPMRTGSTGSPGAPGAVVVDVDLTPAAPSSESLALDEVSAMDNHVAGLGPAEERRALVGPASASPVASIPGPHPSPRAQSLNPDASGSSCSLARTRSRESCASVRRASSADDIEAMRAGALPLPPRHASTGAMHPLRSGLLNSTSDSDLVRYRTISKIPQITLNFVDLKGDPFLASPTSDREIIAPKIKERTHNVTEKVTQVLSLGADVLPEYKLQAPRIHRWTILHYSPFKAVWDWLILLLVIYTAVFTPYSAAFLLKETEDGSQAPDCGYACQPLAVVDLLVDIMFIVDILINFRTTYVNANEEVVSHPGRIAVHYFKGWFLIDMVAAIPFDLLIFGSGSEELIGLLKTARLLRLVRVARKLDRYSEYGAAVLFLLMCTFALIAHWLACIWYAIGNMEQPHMDSHIGWLHNLGDQIGKPYNSSGLGGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVREFIRFHQIPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGFPECLQADICLHLNRSLLQHCKPFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALYFISRGSIEILRGDVVVAILGKNDIFGEPLNLYARPGKSNGDVRALTYCDLHKIHRDDLLEVLDMYPEFSDHFWSSLEITFNLRDTNMIPGSPSSAELESGFNRQRKRKLSFRRRTDKDTEQPGEVSALGQGPARVGPGPSCRGQPGGPWGESPSSGPSSPESSEDEGPGRSSSPLRLVPFSSPRPPGDSPGGEPLTEDGEKSSDTCNPLSGAFSGVSNIFSFWGDSRGRQYQELPRCPAPAPSLLNIPLSSPGRRSRGDVESRLDALQRQLNRLETRLSADMATVLQLLQRQMTLVPPAYSAVTTPGPGPTSTSPLLPVGPVPTLTLDSLSQVSQFVAFEELPAGAPELPQDGPTRRLSLPGQLGALTSQPLHRHGSDPGS
| null | null |
cardiac muscle contraction [GO:0060048]; cellular response to xenobiotic stimulus [GO:0071466]; membrane depolarization during action potential [GO:0086010]; membrane repolarization [GO:0086009]; membrane repolarization during action potential [GO:0086011]; membrane repolarization during cardiac muscle cell action potential [GO:0086013]; membrane repolarization during ventricular cardiac muscle cell action potential [GO:0098915]; negative regulation of potassium ion export across plasma membrane [GO:1903765]; negative regulation of potassium ion transmembrane transport [GO:1901380]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of potassium ion transmembrane transport [GO:1901381]; potassium ion export across plasma membrane [GO:0097623]; potassium ion homeostasis [GO:0055075]; potassium ion import across plasma membrane [GO:1990573]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of membrane potential [GO:0042391]; regulation of membrane repolarization [GO:0060306]; regulation of potassium ion transmembrane transport [GO:1901379]; regulation of ventricular cardiac muscle cell membrane repolarization [GO:0060307]; spinal cord development [GO:0021510]; ventricular cardiac muscle cell action potential [GO:0086005]
|
cell surface [GO:0009986]; cytoplasm [GO:0005737]; inward rectifier potassium channel complex [GO:1902937]; nuclear envelope [GO:0005635]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076]
|
C3HC4-type RING finger domain binding [GO:0055131]; delayed rectifier potassium channel activity [GO:0005251]; identical protein binding [GO:0042802]; inward rectifier potassium channel activity [GO:0005242]; monoatomic ion channel activity [GO:0005216]; potassium channel activity [GO:0005267]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; scaffold protein binding [GO:0097110]; transcription cis-regulatory region binding [GO:0000976]; ubiquitin protein ligase binding [GO:0031625]; voltage-gated potassium channel activity [GO:0005249]; voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization [GO:1902282]
|
PF00027;PF00520;PF13426;
|
1.10.1200.260;1.10.287.70;2.60.120.10;3.30.450.20;
|
Potassium channel family, H (Eag) (TC 1.A.1.20) subfamily, Kv11.1/KCNH2 sub-subfamily
|
PTM: Phosphorylated on serine and threonine residues. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12809}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr) (By similarity). {ECO:0000250|UniProtKB:Q12809}.
|
Rattus norvegicus (Rat)
|
O08966
|
S22A1_MOUSE
|
MPTVDDVLEHVGEFGWFQKQAFLLLCLISASLAPIYVGIVFLGFTPDHHCRSPGVAELSQRCGWSPAEELNYTVPGLGSAGEASFLSQCMKYEVDWNQSTLDCVDPLSSLAANRSHLPLSPCEHGWVYDTPGSSIVTEFNLVCGDAWKVDLFQSCVNLGFFLGSLVVGYIADRFGRKLCLLVTTLVTSLSGVLTAVAPDYTSMLLFRLLQGMVSKGSWVSGYTLITEFVGSGYRRTTAILYQVAFTVGLVGLAGVAYAIPDWRWLQLAVSLPTFLFLLYYWFVPESPRWLLSQKRTTQAVRIMEQIAQKNRKVPPADLKMMCLEEDASERRSPSFADLFRTPSLRKHTLILMYLWFSCAVLYQGLIMHVGATGANLYLDFFYSSLVEFPAAFIILVTIDRIGRIYPIAASNLVAGAACLLMIFIPHELHWLNVTLACLGRMGATIVLQMVCLVNAELYPTFIRNLGMMVCSALCDLGGIFTPFMVFRLMEVWQALPLILFGVLGLSAGAVTLLLPETKGVALPETIEEAENLGRRKSKAKENTIYLQVQTGKSPHT
| null | null |
(R)-carnitine transmembrane transport [GO:1902270]; acetylcholine transport [GO:0015870]; acyl carnitine transmembrane transport [GO:1902616]; cellular detoxification [GO:1990748]; dopamine transport [GO:0015872]; epinephrine transport [GO:0048241]; establishment or maintenance of transmembrane electrochemical gradient [GO:0010248]; metanephric proximal tubule development [GO:0072237]; monoamine transport [GO:0015844]; monoatomic cation transmembrane transport [GO:0098655]; monoatomic cation transport [GO:0006812]; norepinephrine transport [GO:0015874]; organic cation transport [GO:0015695]; prostaglandin transport [GO:0015732]; putrescine transport [GO:0015847]; quaternary ammonium group transport [GO:0015697]; serotonin transport [GO:0006837]; serotonin uptake [GO:0051610]; spermidine transport [GO:0015848]; thiamine transmembrane transport [GO:0071934]; toxin transport [GO:1901998]; xenobiotic transport [GO:0042908]; xenobiotic transport across blood-brain barrier [GO:1990962]
|
apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; lateral plasma membrane [GO:0016328]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
|
(R)-carnitine transmembrane transporter activity [GO:1901235]; acetylcholine transmembrane transporter activity [GO:0005277]; dopamine:sodium symporter activity [GO:0005330]; identical protein binding [GO:0042802]; monoamine transmembrane transporter activity [GO:0008504]; neurotransmitter transmembrane transporter activity [GO:0005326]; norepinephrine:sodium symporter activity [GO:0005334]; organic anion transmembrane transporter activity [GO:0008514]; organic cation transmembrane transporter activity [GO:0015101]; prostaglandin transmembrane transporter activity [GO:0015132]; putrescine transmembrane transporter activity [GO:0015489]; pyrimidine nucleoside transmembrane transporter activity [GO:0015214]; quaternary ammonium group transmembrane transporter activity [GO:0015651]; secondary active organic cation transmembrane transporter activity [GO:0008513]; spermidine transmembrane transporter activity [GO:0015606]; thiamine transmembrane transporter activity [GO:0015234]; toxin transmembrane transporter activity [GO:0019534]; xenobiotic transmembrane transporter activity [GO:0042910]
|
PF00083;
|
1.20.1250.20;
|
Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family
|
PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q63089}.
|
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:28942964}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:23680637}; Multi-pass membrane protein {ECO:0000305}. Lateral cell membrane {ECO:0000250|UniProtKB:O15245}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000250|UniProtKB:O15245}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the sinusoidal/basolateral membrane of hepatocytes (PubMed:28942964). Mainly localized to the basolateral membrane of renal proximal tubular cells (By similarity). However, also identified at the apical side of proximal tubular cells (By similarity). Mainly expressed at the lateral membrane of enterocytes (By similarity). Also observed at the apical side of enterocytes (PubMed:23680637). Localized to the basal membrane of Sertoli cells (By similarity). {ECO:0000250|UniProtKB:O15245, ECO:0000250|UniProtKB:Q63089, ECO:0000269|PubMed:23680637, ECO:0000269|PubMed:28942964}.
|
CATALYTIC ACTIVITY: Reaction=1-methylnicotinamide(out) = 1-methylnicotinamide(in); Xref=Rhea:RHEA:73859, ChEBI:CHEBI:16797; Evidence={ECO:0000250|UniProtKB:Q63089}; CATALYTIC ACTIVITY: Reaction=dopamine(out) = dopamine(in); Xref=Rhea:RHEA:73863, ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:35469921}; CATALYTIC ACTIVITY: Reaction=serotonin(out) = serotonin(in); Xref=Rhea:RHEA:73867, ChEBI:CHEBI:350546; Evidence={ECO:0000269|PubMed:24961373, ECO:0000269|PubMed:35469921}; CATALYTIC ACTIVITY: Reaction=(R)-adrenaline(out) = (R)-adrenaline(in); Xref=Rhea:RHEA:73875, ChEBI:CHEBI:71406; Evidence={ECO:0000269|PubMed:35469921}; CATALYTIC ACTIVITY: Reaction=(R)-noradrenaline(out) = (R)-noradrenaline(in); Xref=Rhea:RHEA:73871, ChEBI:CHEBI:72587; Evidence={ECO:0000269|PubMed:35469921}; CATALYTIC ACTIVITY: Reaction=histamine(out) = histamine(in); Xref=Rhea:RHEA:73879, ChEBI:CHEBI:58432; Evidence={ECO:0000269|PubMed:35469921}; CATALYTIC ACTIVITY: Reaction=guanidine(out) = guanidine(in); Xref=Rhea:RHEA:73883, ChEBI:CHEBI:30087; Evidence={ECO:0000250|UniProtKB:Q63089}; CATALYTIC ACTIVITY: Reaction=choline(out) = choline(in); Xref=Rhea:RHEA:32751, ChEBI:CHEBI:15354; Evidence={ECO:0000269|PubMed:35469921}; CATALYTIC ACTIVITY: Reaction=acetylcholine(in) = acetylcholine(out); Xref=Rhea:RHEA:74663, ChEBI:CHEBI:15355; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=thiamine(in) = thiamine(out); Xref=Rhea:RHEA:34919, ChEBI:CHEBI:18385; Evidence={ECO:0000269|PubMed:24961373, ECO:0000269|PubMed:35469921}; CATALYTIC ACTIVITY: Reaction=spermidine(in) = spermidine(out); Xref=Rhea:RHEA:35039, ChEBI:CHEBI:57834; Evidence={ECO:0000269|PubMed:23458604}; CATALYTIC ACTIVITY: Reaction=agmatine(out) = agmatine(in); Xref=Rhea:RHEA:72131, ChEBI:CHEBI:58145; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=putrescine(out) = putrescine(in); Xref=Rhea:RHEA:72135, ChEBI:CHEBI:326268; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine(in) = (R)-carnitine(out); Xref=Rhea:RHEA:34959, ChEBI:CHEBI:16347; Evidence={ECO:0000269|PubMed:28942964, ECO:0000269|PubMed:34040533}; CATALYTIC ACTIVITY: Reaction=O-isobutanoyl-(R)-carnitine(in) = O-isobutanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74315, ChEBI:CHEBI:84838; Evidence={ECO:0000269|PubMed:28942964, ECO:0000269|PubMed:34040533, ECO:0000269|PubMed:35469921}; CATALYTIC ACTIVITY: Reaction=O-acetyl-(R)-carnitine(in) = O-acetyl-(R)-carnitine(out); Xref=Rhea:RHEA:74319, ChEBI:CHEBI:57589; Evidence={ECO:0000269|PubMed:34040533}; CATALYTIC ACTIVITY: Reaction=O-3-hydroxybutanoyl-(R)-carnitine(in) = O-3-hydroxybutanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74323, ChEBI:CHEBI:84842; Evidence={ECO:0000269|PubMed:34040533}; CATALYTIC ACTIVITY: Reaction=O-propanoyl-(R)-carnitine(in) = O-propanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74327, ChEBI:CHEBI:53210; Evidence={ECO:0000269|PubMed:34040533}; CATALYTIC ACTIVITY: Reaction=O-butanoyl-(R)-carnitine(in) = O-butanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74331, ChEBI:CHEBI:21949; Evidence={ECO:0000269|PubMed:34040533}; CATALYTIC ACTIVITY: Reaction=O-2-methylbutanoyl-(R)-carnitine(in) = O-2-methylbutanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74335, ChEBI:CHEBI:84840; Evidence={ECO:0000269|PubMed:34040533}; CATALYTIC ACTIVITY: Reaction=O-3-methylbutanoyl-(R)-carnitine(in) = O-3-methylbutanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74339, ChEBI:CHEBI:70819; Evidence={ECO:0000269|PubMed:34040533}; CATALYTIC ACTIVITY: Reaction=O-hexanoyl-(R)-carnitine(in) = O-hexanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:74343, ChEBI:CHEBI:84834; Evidence={ECO:0000269|PubMed:34040533}; CATALYTIC ACTIVITY: Reaction=L-histidyl-L-proline diketopiperazine(in) = L-histidyl-L-proline diketopiperazine(out); Xref=Rhea:RHEA:74787, ChEBI:CHEBI:90039; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=(R)-salsolinol(in) = (R)-salsolinol(out); Xref=Rhea:RHEA:74791, ChEBI:CHEBI:194082; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=prostaglandin F2alpha(out) = prostaglandin F2alpha(in); Xref=Rhea:RHEA:50988, ChEBI:CHEBI:57404; Evidence={ECO:0000250|UniProtKB:O15245}; CATALYTIC ACTIVITY: Reaction=prostaglandin E2(out) = prostaglandin E2(in); Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:O15245};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=242 uM for adrenaline {ECO:0000269|PubMed:35469921}; KM=1286 uM for choline {ECO:0000269|PubMed:35469921}; KM=285 uM for dopamine {ECO:0000269|PubMed:35469921}; KM=497 uM for histamine {ECO:0000269|PubMed:35469921}; KM=1470 uM for O-isobutanoyl-(R)-carnitine {ECO:0000269|PubMed:34040533}; KM=1377 uM for O-isobutanoyl-(R)-carnitine {ECO:0000269|PubMed:35469921}; KM=409 uM for noradrenaline {ECO:0000269|PubMed:35469921}; KM=257 uM for serotonin {ECO:0000269|PubMed:35469921}; KM=143 uM for thiamine {ECO:0000269|PubMed:35469921}; KM=490 uM for thiamine {ECO:0000269|PubMed:24961373}; Vmax=7.547 nmol/min/mg enzyme with adrenaline as substrate {ECO:0000269|PubMed:35469921}; Vmax=16.564 nmol/min/mg enzyme with choline as substrate {ECO:0000269|PubMed:35469921}; Vmax=1.714 nmol/min/mg enzyme with dopamine as substrate {ECO:0000269|PubMed:35469921}; Vmax=5.961 nmol/min/mg enzyme with histamine as substrate {ECO:0000269|PubMed:35469921}; Vmax=8.5 nmol/min/mg enzyme with O-isobutanoyl-(R)-carnitine as substrate {ECO:0000269|PubMed:34040533}; Vmax=8.366 nmol/min/mg enzyme with O-isobutanoyl-(R)-carnitine as substrate {ECO:0000269|PubMed:35469921}; Vmax=6.068 nmol/min/mg enzyme with noradrenaline as substrate {ECO:0000269|PubMed:35469921}; Vmax=16.162 nmol/min/mg enzyme with serotonin as substrate {ECO:0000269|PubMed:35469921}; Vmax=3.715 nmol/min/mg enzyme with thiamine as substrate {ECO:0000269|PubMed:35469921}; Vmax=5.8 nmol/min/mg enzyme with thiamine as substrate {ECO:0000269|PubMed:24961373};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 for TEA transport (PubMed:10216142). Optimum pH is 8.4 for MPP(+) transport (PubMed:12176030). {ECO:0000269|PubMed:10216142, ECO:0000269|PubMed:12176030};
| null |
FUNCTION: Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (PubMed:10216142, PubMed:11463829, PubMed:12176030, PubMed:23458604, PubMed:24961373). Functions as a pH- and Na(+)-independent, bidirectional transporter (By similarity). Cation cellular uptake or release is driven by the electrochemical potential (i.e. membrane potential and concentration gradient) and substrate selectivity (By similarity). Hydrophobicity is a major requirement for recognition in polyvalent substrates and inhibitors (PubMed:23458604). Primarily expressed in the basolateral membrane of hepatocytes and proximal tubules and involved in the uptake and disposition of cationic compounds from the blood by hepatic and renal clearance (By similarity). Most likely functions as an uptake carrier in enterocytes contributing to the intestinal elimination of organic cations from the systemic circulation (PubMed:11463829, PubMed:24961373). Transports endogenous monoamines such as N-1-methylnicotinamide (NMN), guanidine, neurotransmitters dopamine, serotonin, noradrenaline, adrenaline and histamine, and quaternary ammonium compound such as choline (PubMed:24961373, PubMed:35469921). Also transports natural polyamines such as spermidine, agmatine and putrescine at low affinity, but relatively high turnover (PubMed:23458604). Involved in the hepatic and intestinal uptake of the vitamin B1/thiamine, hence regulating hepatic lipid and energy metabolism (PubMed:24961373). Contributes to the influx and efflux of fatty acid carriers carnitines and acylcarnitines across the basolateral membrane of hepatocytes, from the liver to the systemic circulation and inversely and may be involved in regulating the systemic availability of hepatic acylcarnitines (PubMed:28942964, PubMed:34040533). Also capable of transporting non-amine endogenous compounds such as prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) (By similarity). May contribute to the transport of cationic compounds in testes across the blood-testis-barrier (By similarity). Also mediates the uptake of xenobiotics tributylmethylammonium (TBuMA), quinidine, N-methyl-quinine (NMQ), N-methyl-quinidine (NMQD) N-(4,4-azo-n-pentyl)-quinuclidine (APQ), azidoprocainamide methoiodide (AMP), N-(4,4-azo-n-pentyl)-21-deoxyajmalinium (APDA) and 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP) (PubMed:11463829). {ECO:0000250|UniProtKB:O15245, ECO:0000250|UniProtKB:Q63089, ECO:0000269|PubMed:10216142, ECO:0000269|PubMed:11463829, ECO:0000269|PubMed:12176030, ECO:0000269|PubMed:23458604, ECO:0000269|PubMed:24961373, ECO:0000269|PubMed:28942964, ECO:0000269|PubMed:34040533, ECO:0000269|PubMed:35469921}.
|
Mus musculus (Mouse)
|
O08967
|
CYH3_MOUSE
|
MDEGGGGEGGSVPEDLSLEEREELLDIRRRKKELIDDIERLKYEIAEVMTEIDNLTSVEESKTTQRNKQIAMGRKKFNMDPKKGIQFLIENDLLQSSPEDVAQFLYKGEGLNKTVIGDYLGERDDFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAFASRYCLCNPGVFQSTDTCYVLSFAIIMLNTSLHNHNVRDKPTAERFITMNRGINEGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDPRKPNCFELYNPSHKGQVIKACKTEADGRVVEGNHVVYRISAPSPEEKEEWMKSIKASISRDPFYDMLATRKRRIANKK
| null | null |
establishment of epithelial cell polarity [GO:0090162]; Golgi vesicle transport [GO:0048193]; positive regulation of cell adhesion [GO:0045785]; regulation of ARF protein signal transduction [GO:0032012]
|
adherens junction [GO:0005912]; bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; ruffle [GO:0001726]
|
guanyl-nucleotide exchange factor activity [GO:0005085]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]
|
PF00169;PF01369;
|
1.10.220.20;1.10.1000.11;2.30.29.30;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:18042453}; Peripheral membrane protein {ECO:0000269|PubMed:18042453}. Cell junction, adherens junction {ECO:0000269|PubMed:20080746}. Cell junction, tight junction {ECO:0000269|PubMed:20080746}. Note=Translocates from the cytosol to membranes enriched in phosphatidylinositol 3,4,5-trisphosphate.
| null | null | null | null | null |
FUNCTION: Promotes guanine-nucleotide exchange on ARF1. Promotes the activation of ARF factors through replacement of GDP with GTP (PubMed:18042453). Plays a role in the epithelial polarization (PubMed:20080746). {ECO:0000269|PubMed:18042453, ECO:0000269|PubMed:20080746}.
|
Mus musculus (Mouse)
|
O08969
|
PHLA2_MOUSE
|
MASKIVMSSKTVKTSDEILCEGELEKRSDSLFQVWKKKRCVLTADRLRLFSGKTSPAKELFFHSILKVDCVEHTSKYVYFTIVTNYYKEIDFRCTVESCWNAAITMALIDFQNRRALQDFPRYRYQRSESEMPSEPGEQSALGP
| null | null |
animal organ morphogenesis [GO:0009887]; placenta development [GO:0001890]; positive regulation of apoptotic process [GO:0043065]; regulation of cell migration [GO:0030334]; regulation of embryonic development [GO:0045995]; regulation of gene expression [GO:0010468]; regulation of glycogen metabolic process [GO:0070873]; regulation of spongiotrophoblast cell proliferation [GO:0060721]
|
cytoplasm [GO:0005737]; membrane [GO:0016020]
|
phosphatidylinositol phosphate binding [GO:1901981]
| null |
2.30.29.30;
|
PHLDA2 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12374806}. Membrane {ECO:0000269|PubMed:12374806}; Peripheral membrane protein {ECO:0000269|PubMed:12374806}.
| null | null | null | null | null |
FUNCTION: Plays a role in regulating placenta growth. May act via its PH domain that competes with other PH domain-containing proteins, thereby preventing their binding to membrane lipids. {ECO:0000269|PubMed:12032310}.
|
Mus musculus (Mouse)
|
O08983
|
HPS1_MOUSE
|
MKCVLVATEGAEVLFYWTDEEFAESLRLKLQQSEDEEEELPVLEDQLSTLLAPVIISSMTMLEKLSDTYTCFSTENDNHLYVLHLFGEYLFVAINGDHSESEGDLRRKLCVLKYLFEVHFGLVTVDGQLIRKELRPPDLEERARVWKHFQRLLGTYSYLRDREQSFAVEAVERLIHPQLCEQSIETLERHVVQAINASPERGGEEVLHAFLLVHCKLLAFYSGHGASTLRPADLLALILLVQDLQPSPGTTEEEEEEEDSDSPQRRPKSSQNIPVQQARSQSTSVPTRSSRETDTDSISLPEEYFTPAPSPGDQSSGSLVWLDGGTPPSDALQMAEDTPEGLASHSPELPSPRRIFLDANIKENYCPLVPHTMYCLPLWPGINMVLLTKSPSTPLALILYQLLDGFSLLEKKLKEGQEAGSALRSQPFVADLRQKMDKFIKNRVGQEIQNTWLEFKSKAFSRSEPGSSWELLQVCGKLKRQLCVIYRLSFLVTAPSRGGPHLPQHLQDRAQKLMKERLLDWKDFLLVKSRRNVTMVSYLEDFPGLVHFIYVDRTTGQMVAPSLSPNEKMSSELGKGPLAAFVKAKVWALVRLARRYLQKGCTTLLFQEGDFRCSYFLWFENDMGYKLQMIEVPVLSDDSVPIGVLGGDYYRKLLRYYSKSHPSEPVRCYELLTLHLSVIPTDLLVQQASQLARRLGEASRVTLP
| null | null |
blood coagulation [GO:0007596]; cell morphogenesis [GO:0000902]; eye pigmentation [GO:0048069]; gene expression [GO:0010467]; inflammatory response [GO:0006954]; intracellular transport [GO:0046907]; intracellular zinc ion homeostasis [GO:0006882]; lipid homeostasis [GO:0055088]; lipid metabolic process [GO:0006629]; lung development [GO:0030324]; lung morphogenesis [GO:0060425]; lysosome organization [GO:0007040]; melanocyte differentiation [GO:0030318]; melanosome assembly [GO:1903232]; organelle organization [GO:0006996]; pigmentation [GO:0043473]; platelet dense granule organization [GO:0060155]; positive regulation of natural killer cell activation [GO:0032816]; protein secretion [GO:0009306]; respiratory system process [GO:0003016]; retina development in camera-type eye [GO:0060041]; secretion of lysosomal enzymes [GO:0033299]; single fertilization [GO:0007338]; spermatogenesis [GO:0007283]; vesicle-mediated transport [GO:0016192]
|
BLOC-3 complex [GO:0031085]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]
|
guanyl-nucleotide exchange factor activity [GO:0005085]
|
PF19036;PF19037;PF19038;
| null | null | null | null | null | null | null | null | null |
FUNCTION: Component of the BLOC-3 complex, a complex that acts as a guanine exchange factor (GEF) for RAB32 and RAB38, promotes the exchange of GDP to GTP, converting them from an inactive GDP-bound form into an active GTP-bound form. The BLOC-3 complex plays an important role in the control of melanin production and melanosome biogenesis and promotes the membrane localization of RAB32 and RAB38. {ECO:0000250|UniProtKB:Q92902}.
|
Mus musculus (Mouse)
|
O08984
|
LBR_RAT
|
MPGRKFADGEVVRGRWPGSSLYYEVEILSHDSTSQLYTVKYKDGTELELKESDIKPLKSFKQRKSGSTSSSPSRRRSSRSRSRSRSRSPGRAPKGSRRSVSASYQADAKEKEMRREILQVKLTPLVLKPFANSVSVYNGEPEHMEKSATPPKNKQERVILSTEDSYIATQYSLRPRREEVKPKHRVRGTNLVTRGPVPLGTFQVTTPQRRDLEFGGVPGALLIMLGLPACVFLLLLQCAQKDPGLLQFPPPLPALRELWEARVCGVYLLWFFLQALFSLLPVGKVVEGTPLVDGRRLKYRLNGLYAFILTSAAVGTAVFWDIELYYLYTHFLQFALAAIVFSVVLSVYLYARSLKVPRDELSPASSGNAVYDFFIGRELNPRIGAFDLKFFCELRPGLIGWVVINLVMLLAEMKVQERSAPSLAMTLVNSFQLLYVVDALWFEEALLTTMDIIHDGFGFMLAFGDLVWVPFTYSLQAFYLVNHPQDLSWPLTSVIIALKLCGYVIFRCANSQKNAFRKNPTDPKLAHLKTIPTSTWKSLLVSGWWGFVRHPNYLGDLIMALAWSLPCGFNHILPYFYVIYFTALLIHREARDEHQCRRKYGLAWEKYCQRVPYRIFPYIY
|
1.3.1.70
| null |
cholesterol biosynthetic process [GO:0006695]; ergosterol biosynthetic process [GO:0006696]; neutrophil differentiation [GO:0030223]
|
cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleus [GO:0005634]
|
chromo shadow domain binding [GO:0070087]; delta14-sterol reductase activity [GO:0050613]; DNA binding [GO:0003677]; NADPH binding [GO:0070402]; nuclear localization sequence binding [GO:0008139]; protein-folding chaperone binding [GO:0051087]
|
PF01222;PF09465;
|
1.20.120.1630;2.30.30.140;
|
ERG4/ERG24 family
|
PTM: Phosphorylated by CDK1 in mitosis when the inner nuclear membrane breaks down into vesicles that dissociate from the lamina and the chromatin (By similarity). It is phosphorylated by different protein kinases in interphase when the membrane is associated with these structures (By similarity). Phosphorylation of LBR and HP1 proteins may be responsible for some of the alterations in chromatin organization and nuclear structure which occur at various times during the cell cycle (By similarity). Phosphorylated by SRPK1 (By similarity). In late anaphase LBR is dephosphorylated, probably by PP1 and/or PP2A, allowing reassociation with chromatin (By similarity). {ECO:0000250|UniProtKB:Q14739}.
|
SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250|UniProtKB:Q14739}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q14739}. Cytoplasm {ECO:0000250|UniProtKB:Q14739}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14739}. Note=Nucleus; nuclear rim. {ECO:0000250|UniProtKB:Q14739}.
|
CATALYTIC ACTIVITY: Reaction=5alpha-cholest-8,14-dien-3beta-ol + H(+) + NADPH = 5alpha-cholest-8-en-3beta-ol + NADP(+); Xref=Rhea:RHEA:46456, ChEBI:CHEBI:15378, ChEBI:CHEBI:16608, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:86131; Evidence={ECO:0000250|UniProtKB:Q14739}; CATALYTIC ACTIVITY: Reaction=4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + H(+) + NADPH; Xref=Rhea:RHEA:18561, ChEBI:CHEBI:15378, ChEBI:CHEBI:17813, ChEBI:CHEBI:18364, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.70; Evidence={ECO:0000250|UniProtKB:Q14739}; CATALYTIC ACTIVITY: Reaction=4,4-dimethyl-8,14-cholestadien-3beta-ol + H(+) + NADPH = 4,4-dimethyl-5alpha-cholest-8-en-3beta-ol + NADP(+); Xref=Rhea:RHEA:46812, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78904, ChEBI:CHEBI:87044; Evidence={ECO:0000250|UniProtKB:Q14739};
| null |
PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
| null | null |
FUNCTION: Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (By similarity). Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (By similarity). Anchors the lamina and the heterochromatin to the inner nuclear membrane (By similarity). {ECO:0000250|UniProtKB:Q14739, ECO:0000250|UniProtKB:Q3U9G9}.
|
Rattus norvegicus (Rat)
|
O08992
|
SDCB1_MOUSE
|
MSLYPSLEDLKVDKVIQAQTAYSANPASQAFVLVDASAALPPDGNLYPKLYPELSQYMGLSLNEAEICESMPMVSGAPAQGQLVARPSSVNYMVAPVTGNDAGIRRAEIKQGIREVILCKDQDGKIGLRLKSIDNGIFVQLVQANSPASLVGLRFGDQVLQINGENCAGWSSDKAHKVLKQAFGEKITMTIRDRPFERTVTMHKDSSGHVGFIFKSGKITSIVKDSSAARNGLLTDHHICEINGQNVIGLKDAQIADILSTAGTVVTITIMPTFIFEHIIKRMAPSIMKSLMDHTIPEV
| null | null |
negative regulation of receptor internalization [GO:0002091]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of cell growth [GO:0030307]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of extracellular exosome assembly [GO:1903553]; positive regulation of phosphorylation [GO:0042327]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; presynapse assembly [GO:0099054]; Ras protein signal transduction [GO:0007265]; regulation of mitotic cell cycle [GO:0007346]
|
adherens junction [GO:0005912]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; interleukin-5 receptor complex [GO:0005895]; melanosome [GO:0042470]; membrane raft [GO:0045121]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
|
cell adhesion molecule binding [GO:0050839]; ephrin receptor binding [GO:0046875]; frizzled binding [GO:0005109]; growth factor binding [GO:0019838]; identical protein binding [GO:0042802]; interleukin-5 receptor binding [GO:0005137]; ionotropic glutamate receptor binding [GO:0035255]; neurexin family protein binding [GO:0042043]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; protein heterodimerization activity [GO:0046982]; protein sequestering activity [GO:0140311]; protein-containing complex binding [GO:0044877]; syndecan binding [GO:0045545]
|
PF00595;
|
2.30.42.10;
| null |
PTM: Phosphorylated on tyrosine residues. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250|UniProtKB:O00560}. Cell junction, adherens junction {ECO:0000250|UniProtKB:O00560}. Cell membrane {ECO:0000250|UniProtKB:O00560}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00560}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00560}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00560}. Nucleus {ECO:0000250|UniProtKB:O00560}. Melanosome {ECO:0000250|UniProtKB:O00560}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O00560}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O00560}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:O00560}. Membrane raft {ECO:0000250|UniProtKB:O00560}. Note=Mainly membrane-associated. Localized to adherens junctions, focal adhesions and endoplasmic reticulum. Colocalized with actin stress fibers. Also found in the nucleus. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Associated to the plasma membrane in the presence of FZD7 and phosphatidylinositol 4,5-bisphosphate (PIP2) (By similarity). {ECO:0000250|UniProtKB:O00560}.
| null | null | null | null | null |
FUNCTION: Multifunctional adapter protein involved in diverse array of functions including trafficking of transmembrane proteins, neuro and immunomodulation, exosome biogenesis, and tumorigenesis. Positively regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types. May increase TGFB1 signaling by enhancing cell-surface expression of TGFR1 by preventing the interaction between TGFR1 and CAV1 and subsequent CAV1-dependent internalization and degradation of TGFR1. In concert with SDC1/4 and PDCD6IP, regulates exosome biogenesis (By similarity). Regulates migration, growth, proliferation, and cell cycle progression in a variety of cancer types (PubMed:26539120). In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA). May also play a role in vesicular trafficking. Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway (By similarity). {ECO:0000250|UniProtKB:O00560, ECO:0000269|PubMed:26539120}.
|
Mus musculus (Mouse)
|
O08999
|
LTBP2_MOUSE
|
MRAPTTARCSGCIQRVRWRGFLPLVLAVLMGTSHAQRDSIGRYEPASRDANRLWHPVGSHPAAAAAKVYSLFREPDAPVPGLSPSEWNQPAQGNPGWLAEAEARRPPRTQQLRRVQPPVQTRRSHPRGQQQIAARAAPSVARLETPQRPAAARRGRLTGRNVCGGQCCPGWTTSNSTNHCIKPVCQPPCQNRGSCSRPQVCICRSGFRGARCEEVIPEEEFDPQNARPVPRRSVERAPGPHRSSEARGSLVTRIQPLVPPPSPPPSRRLSQPWPLQQHSGPSRTVRRYPATGANGQLMSNALPSGLELRDSSPQAAHVNHLSPPWGLNLTEKIKKIKVVFTPTICKQTCARGRCANSCEKGDTTTLYSQGGHGHDPKSGFRIYFCQIPCLNGGRCIGRDECWCPANSTGKFCHLPVPQPDREPAGRGSRHRTLLEGPLKQSTFTLPLSNQLASVNPSLVKVQIHHPPEASVQIHQVARVRGELDPVLEDNSVETRASHRPHGNLGHSPWASNSIPARAGEAPRPPPVLSRHYGLLGQCYLSTVNGQCANPLGSLTSQEDCCGSVGTFWGVTSCAPCPPRQEGPAFPVIENGQLECPQGYKRLNLSHCQDINECLTLGLCKDSECVNTRGSYLCTCRPGLMLDPSRSRCVSDKAVSMQQGLCYRSLGSGTCTLPLVHRITKQICCCSRVGKAWGSTCEQCPLPGTEAFREICPAGHGYTYSSSDIRLSMRKAEEEELASPLREQTEQSTAPPPGQAERQPLRAATATWIEAETLPDKGDSRAVQITTSAPHLPARVPGDATGRPAPSLPGQGIPESPAEEQVIPSSDVLVTHSPPDFDPCFAGASNICGPGTCVSLPNGYRCVCSPGYQLHPSQDYCTDDNECMRNPCEGRGRCVNSVGSYSCLCYPGYTLVTLGDTQECQDIDECEQPGVCSGGRCSNTEGSYHCECDRGYIMVRKGHCQDINECRHPGTCPDGRCVNSPGSYTCLACEEGYVGQSGSCVDVNECLTPGICTHGRCINMEGSFRCSCEPGYEVTPDKKGCRDVDECASRASCPTGLCLNTEGSFTCSACQSGYWVNEDGTACEDLDECAFPGVCPTGVCTNTVGSFSCKDCDQGYRPNPLGNRCEDVDECEGPQSSCRGGECKNTEGSYQCLCHQGFQLVNGTMCEDVNECVGEEHCAPHGECLNSLGSFFCLCAPGFASAEGGTRCQDVDECAATDPCPGGHCVNTEGSFSCLCETASFQPSPDSGECLDIDECEDREDPVCGAWRCENSPGSYRCILDCQPGFYVAPNGDCIDIDECANDTVCGNHGFCDNTDGSFRCLCDQGFETSPSGWECVDVNECELMMAVCGDALCENVEGSFLCLCASDLEEYDAEEGHCRPRVAGAQRIPEVRTEDQAPSLIRMECYSEHNGGPPCSQILGQNSTQAECCCTQGARWGKACAPCPSEDSVEFSQLCPSGQGYIPVEGAWTFGQTMYTDADECVLFGPALCQNGRCSNIVPGYICLCNPGYHYDASSRKCQDHNECQDLACENGECVNQEGSFHCLCNPPLTLDLSGQRCVNTTSSTEDFPDHDIHMDICWKKVTNDVCSQPLRGHHTTYTECCCQDGEAWSQQCALCPPRSSEVYAQLCNVARIEAERGAGIHFRPGYEYGPGLDDLPENLYGPDGAPFYNYLGPEDTAPEPPFSNPASQPGDNTPVLEPPLQPSELQPHYLASHSEPPASFEGLQAEECGILNGCENGRCVRVREGYTCDCFEGFQLDAPTLACVDVNECEDLNGPARLCAHGHCENTEGSYRCHCSPGYVAEPGPPHCAAKE
| null | null |
Golgi to vacuole transport [GO:0006896]; protein targeting to vacuole [GO:0006623]; supramolecular fiber organization [GO:0097435]
|
collagen-containing extracellular matrix [GO:0062023]; endosome [GO:0005768]; extracellular region [GO:0005576]; Golgi transport complex [GO:0017119]; membrane [GO:0016020]; trans-Golgi network [GO:0005802]
|
calcium ion binding [GO:0005509]; growth factor binding [GO:0019838]; heparin binding [GO:0008201]; microfibril binding [GO:0050436]
|
PF00008;PF07645;PF12661;PF00683;
|
2.10.25.10;3.90.290.10;
|
LTBP family
|
PTM: N-Glycosylated. {ECO:0000250|UniProtKB:Q14767}.; PTM: Contains hydroxylated asparagine residues. {ECO:0000250|UniProtKB:Q14766}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q14767}.
| null | null | null | null | null |
FUNCTION: May play an integral structural role in elastic-fiber architectural organization and/or assembly. {ECO:0000250|UniProtKB:Q14767}.
|
Mus musculus (Mouse)
|
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