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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O70157
|
TOP3A_MOUSE
|
MIFPVTLLAFQWHRRPGGRALSRAAMEVAFRGVRKVLCVAEKNDAAKGIADLLSNGRMRRKEGLSKFNKIYEFDYHLYGQNVTMIMTSVSGHLLAHDFQMQFRKWQSCNPLVLFEAEIEKYCPENFIDIKKTLERETHHCQALVIWTDCDREGENIGFEIIHVCKAVKPNLRVLRARFSEITPHAVRTACENLTEPDQRVSDAVDVRQELDLRIGAAFTRFQTLRLQRIFPEVLAEQLISYGSCQFPTLGFVVERFKAIQAFVPEVFHKIKVTHDHKDGTVEFNWKRYRLFNHTACLVLYQLCMEDPMATVVEVRSKPKSKWRPQALDTVELEKLASRKLRINAKETMRIAEKLYTQGYISYPRTETNIFPKDLNLVALVEQQTVDPHWGAFAQTILERGGPTPRNGSKSDQAHPPIHPTKYTSGLQGDDRRLYEFIVRHFLACCSQDAQGQETTVEIDIAQERFVAHGLIILARNYLDVYPYDHWSDKLLPVYEQGSHFQPSTVEMVDGETSPPQLLTEADLIALMEKHGIGTDATHAEHIETIKARMYVGLTSDKRFLPGHLGMGLVEGYDSMGYEMSKPDLRAELEADLKLICEGKKDKFQVLRQQVQKYKQVFIEAVAKAKKLDEALSQYLGERTEMAQQEEIYPAMPEPVRKCPQCNKDMVLKTKKSGGFYLSCMGFPECRSAVWFPDSVLEASRDNSVCSVCQPPPVYRLKLKFKRGSLPPAMPLEFVGCIGGCDETLKEIFGLRFPRALPRASQPSGHLQASQALNRMDSSQHNLSQPLVNRHTRPSKTVAQALLPPTTAGESNSVTCNCGREAVLLTVRKQGPNQGRHFYKCSNGDCNFFLWADSSHSTGGGTPTSASGPPGSSVGCPSSVGSHMDGFGSLGSDSDGGTPCLCGQPAVTRTVQKDGPNKGRQFHTCAKPREQQCGFFQWVDENVAPGSFAAPAWPGGRGKAQRPEAASKRPRAGSSDAGSTVKKPRKCSLCHQPGHTRTFCPQNR
|
5.6.2.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
|
chromosome separation [GO:0051304]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA topological change [GO:0006265]; double-strand break repair via homologous recombination [GO:0000724]; mitochondrial DNA metabolic process [GO:0032042]; resolution of DNA recombination intermediates [GO:0071139]
|
mitochondrial matrix [GO:0005759]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; RecQ family helicase-topoisomerase III complex [GO:0031422]
|
DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917]; single-stranded DNA binding [GO:0003697]; zinc ion binding [GO:0008270]
|
PF01131;PF01751;PF01396;PF06839;
|
3.40.50.140;3.30.65.10;1.10.460.10;2.70.20.10;1.10.290.10;
|
Type IA topoisomerase family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q13472}.
|
CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10131};
| null | null | null | null |
FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. As an essential component of the RMI complex it is involved in chromosome separation and the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Has DNA decatenation activity. It is required for mtDNA decatenation and segregation after completion of replication, in a process that does not require BLM, RMI1 and RMI2. {ECO:0000250|UniProtKB:Q13472}.
|
Mus musculus (Mouse)
|
O70161
|
PI51C_MOUSE
|
MELEVPDEAESAEAGAVTAEAAWSAESGAAAGMTQKKAGLAEAPLVTGQPGPGHGKKLGHRGVDASGETTYKKTTSSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLLLGVHNIDQQERERQAEGAQSKADEKRPVAQKALYSTAMESIQGGAARGEAIETDDTMGGIPAVNGRGERLLLHIGIIDILQSYRFIKKLEHTWKALVHDGDTVSVHRPSFYAERFFKFMSSTVFRKSSSLKSSPSKKGRGALLAVKPLGPTAAFSASQIPSEREDVQYDLRGARSYPTLEDEGRPDLLPCTPPSFEEATTASIATTLSSTSLSIPERSPSDTSEQPRYRRRTQSSGQDGRPQEEPHAEDLQKITVQVEPVCGVGVVPKEEGAGVEVPPCGASAAASVEIDAASQASEPASQASDEEDAPSTDIYFPTDERSWVYSPLHYSARPASDGESDT
|
2.7.1.68
| null |
axonogenesis [GO:0007409]; chemotaxis [GO:0006935]; exocytosis [GO:0006887]; phagocytosis [GO:0006909]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphorylation [GO:0016310]; platelet aggregation [GO:0070527]; regulation of postsynaptic neurotransmitter receptor internalization [GO:0099149]; regulation of synaptic vesicle endocytosis [GO:1900242]
|
adherens junction [GO:0005912]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; presynaptic endocytic zone membrane [GO:0098835]; ruffle membrane [GO:0032587]; uropod [GO:0001931]
|
1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; ATP binding [GO:0005524]
|
PF01504;
|
3.30.810.10;3.30.800.10;
| null |
PTM: Phosphorylation on Ser-645 negatively regulates binding to TLN2 and is strongly stimulated in mitosis. Phosphorylation on Tyr-644 is necessary for targeting to focal adhesions. Phosphorylation on Ser-645 and Tyr-644 are mutually exclusive. Phosphorylated by SYK and CSK. Tyrosine phosphorylation is enhanced by PTK2 signaling. Phosphorylated at Tyr-634 upon EGF stimulation. Some studies suggest that phosphorylation on Tyr-644 enhances binding to tailins (TLN1 and TLN2); others that phosphorylation at Tyr-644 does not directly enhance binding to tailins (TLN1 and TLN2) but may act indirectly by inhibiting phosphorylation at Ser-645. {ECO:0000269|PubMed:12422220, ECO:0000269|PubMed:14691141, ECO:0000269|PubMed:16707488, ECO:0000269|PubMed:17635937, ECO:0000269|PubMed:19153220}.; PTM: Acetylation at Lys-265 and Lys-268 seems to decrease lipid kinase activity. Deacetylation of these sites by SIRT1 positively regulates the exocytosis of TSH-containing granules from pituitary cells (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:Q5I6B8}. Endomembrane system {ECO:0000250|UniProtKB:Q5I6B8}. Cytoplasm {ECO:0000269|PubMed:19153220, ECO:0000269|PubMed:20622009}. Cell junction, focal adhesion {ECO:0000269|PubMed:12422220, ECO:0000269|PubMed:14691141}. Cell junction, adherens junction {ECO:0000250|UniProtKB:O60331}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q5I6B8}. Cell projection, phagocytic cup {ECO:0000269|PubMed:19153220}. Cell projection, uropodium {ECO:0000269|PubMed:17928408}. Note=During directional migration isoform 1 localized at the uropodium, and isoform 3 localized all along cell membrane including the uropodium and the leading edge.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68; Evidence={ECO:0000269|PubMed:14741049, ECO:0000269|PubMed:20622009, ECO:0000269|PubMed:22942276, ECO:0000269|PubMed:9535851}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14426; Evidence={ECO:0000305|PubMed:15489334, ECO:0000305|PubMed:20622009, ECO:0000305|PubMed:22942276, ECO:0000305|PubMed:9535851}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate + ADP + H(+); Xref=Rhea:RHEA:40363, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77136, ChEBI:CHEBI:77137, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O60331}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40364; Evidence={ECO:0000250|UniProtKB:O60331}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate + ADP + H(+); Xref=Rhea:RHEA:40367, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77139, ChEBI:CHEBI:77140, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O60331}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40368; Evidence={ECO:0000250|UniProtKB:O60331}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40379, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77163, ChEBI:CHEBI:77164, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O60331}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40380; Evidence={ECO:0000250|UniProtKB:O60331}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol + ATP = 1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40383, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77158, ChEBI:CHEBI:77159, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O60331}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40384; Evidence={ECO:0000250|UniProtKB:O60331}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40375, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77160, ChEBI:CHEBI:133606, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O60331}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40376; Evidence={ECO:0000250|UniProtKB:O60331}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol + ATP = 1,2-di(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40387, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77165, ChEBI:CHEBI:77167, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O60331}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40388; Evidence={ECO:0000250|UniProtKB:O60331};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=37 uM for phosphatidylinositol-4-phosphate/PtdIns(4)P {ECO:0000269|PubMed:9535851}; KM=39 uM for ATP {ECO:0000269|PubMed:9535851}; KM=1.6 uM for 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 4-phosphate {ECO:0000269|PubMed:22942276}; KM=15 uM for 1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol 4-phosphate {ECO:0000269|PubMed:22942276};
| null | null | null |
FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility (PubMed:14741049, PubMed:20622009, PubMed:22942276, PubMed:9535851). PtdIns(4,5)P2 can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (By similarity). PIP5K1A-mediated phosphorylation of PtdIns(4)P is the predominant pathway for PtdIns(4,5)P2 synthesis (By similarity). Together with PIP5K1A, is required for phagocytosis, both enzymes regulating different types of actin remodeling at sequential steps (PubMed:19153220). Promotes particle attachment by generating the pool of PtdIns(4,5)P2 that induces controlled actin depolymerization to facilitate Fc-gamma-R clustering. Mediates RAC1-dependent reorganization of actin filaments. Required for synaptic vesicle transport (PubMed:15386003). Controls the plasma membrane pool of PtdIns(4,5)P2 implicated in synaptic vesicle endocytosis and exocytosis (By similarity). Plays a role in endocytosis mediated by clathrin and AP-2 (adaptor protein complex 2) (PubMed:16707488). Required for clathrin-coated pits assembly at the synapse (By similarity). Participates in cell junction assembly (By similarity). Modulates adherens junctions formation by facilitating CDH1/cadherin trafficking (By similarity). Required for focal adhesion dynamics (PubMed:12422220). Modulates the targeting of talins (TLN1 and TLN2) to the plasma membrane and their efficient assembly into focal adhesions (By similarity). Regulates the interaction between talins (TLN1 and TLN2) and beta-integrins (By similarity). Required for uropodium formation and retraction of the cell rear during directed migration (PubMed:17928408). Has a role in growth factor-stimulated directional cell migration and adhesion (PubMed:17635937). Required for talin assembly into nascent adhesions forming at the leading edge toward the direction of the growth factor (PubMed:17635937). Negative regulator of T-cell activation and adhesion (PubMed:20855869). Negatively regulates integrin alpha-L/beta-2 (LFA-1) polarization and adhesion induced by T-cell receptor (PubMed:20855869). Together with PIP5K1A has a role during embryogenesis and together with PIP5K1B may have a role immediately after birth (PubMed:17609388, PubMed:20622009). {ECO:0000250|UniProtKB:O60331, ECO:0000269|PubMed:12422220, ECO:0000269|PubMed:14741049, ECO:0000269|PubMed:15386003, ECO:0000269|PubMed:16707488, ECO:0000269|PubMed:17609388, ECO:0000269|PubMed:17635937, ECO:0000269|PubMed:17928408, ECO:0000269|PubMed:19153220, ECO:0000269|PubMed:20622009, ECO:0000269|PubMed:20855869, ECO:0000269|PubMed:22942276, ECO:0000269|PubMed:9535851}.
|
Mus musculus (Mouse)
|
O70165
|
FCN1_MOUSE
|
MQWPTLWAFSGLLCLCPSQALGQERGACPDVKVVGLGAQDKVVVIQSCPGFPGPPGPKGEPGSPAGRGERGFQGSPGKMGPAGSKGEPGTMGPPGVKGEKGDTGAAPSLGEKELGDTLCQRGPRSCKDLLTRGIFLTGWYTIHLPDCRPLTVLCDMDVDGGGWTVFQRRVDGSIDFFRDWDSYKRGFGNLGTEFWLGNDYLHLLTANGNQELRVDLQDFQGKGSYAKYSSFQVSEEQEKYKLTLGQFLEGTAGDSLTKHNNMSFTTHDQDNDANSMNCAALFHGAWWYHNCHQSNLNGRYLSGSHESYADGINWGTGQGHHYSYKVAEMKIRAS
| null | null |
cell surface pattern recognition receptor signaling pathway [GO:0002752]; complement activation, lectin pathway [GO:0001867]; G protein-coupled receptor signaling pathway [GO:0007186]; positive regulation of interleukin-8 production [GO:0032757]
|
collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
antigen binding [GO:0003823]; carbohydrate binding [GO:0030246]; carbohydrate derivative binding [GO:0097367]; metal ion binding [GO:0046872]; pattern recognition receptor activity [GO:0038187]; signaling receptor binding [GO:0005102]
|
PF01391;PF00147;
|
3.90.215.10;
|
Ficolin lectin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O00602}. Cell membrane {ECO:0000250|UniProtKB:O00602}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00602}; Extracellular side {ECO:0000250|UniProtKB:O00602}. Note=Found on the monocyte and granulocyte surface. {ECO:0000250|UniProtKB:O00602}.
| null | null | null | null | null |
FUNCTION: Extracellular lectin functioning as a pattern-recognition receptor in innate immunity. Binds the sugar moieties of pathogen-associated molecular patterns (PAMPs) displayed on microbes and activates the lectin pathway of the complement system. May also activate monocytes through a G protein-coupled receptor, FFAR2, inducing the secretion of interleukin-8/IL-8. Binds preferentially to 9-O-acetylated 2-6-linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O70166
|
STMN3_MOUSE
|
MASTVSAYKEKMKELSVLSLICSCFYSQPHPNTIYQYGDMEVKQLDKRASGQSFEVILKSPSDLSPESPVLSSPPKRKDASLEELQKRLEAAEERRKTQEAQVLKQLAERREHEREVLHKALEENNNFSRLAEEKLNYKMELSKEIREAHLAALRERLREKELHAAEVRRNKEQREEMSG
| null | null |
blastocyst hatching [GO:0001835]; cytoplasmic microtubule organization [GO:0031122]; microtubule depolymerization [GO:0007019]; negative regulation of Rac protein signal transduction [GO:0035021]; neuron projection development [GO:0031175]; regulation of cytoskeleton organization [GO:0051493]; regulation of GTPase activity [GO:0043087]; regulation of microtubule polymerization or depolymerization [GO:0031110]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; growth cone [GO:0030426]; neuron projection [GO:0043005]; perinuclear region of cytoplasm [GO:0048471]
|
protein domain specific binding [GO:0019904]; protein-folding chaperone binding [GO:0051087]; tubulin binding [GO:0015631]
|
PF00836;
|
6.10.280.30;
|
Stathmin family
|
PTM: N-terminal palmitoylation promotes specific anchoring to the cytosolic leaflet of Golgi membranes and subsequent vesicular trafficking along dendrites and axons. Neuronal Stathmins are substrates for palmitoyltransferases ZDHHC3, ZDHHC7 and ZDHHC15 (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Golgi apparatus. Cell projection, growth cone. Cell projection, axon. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JHU6}.
| null | null | null | null | null |
FUNCTION: Exhibits microtubule-destabilizing activity, which is antagonized by STAT3. {ECO:0000269|PubMed:16401721}.
|
Mus musculus (Mouse)
|
O70167
|
P3C2G_MOUSE
|
MAYSWQTEPNRTEPQEDGSDTQQFHHTNQHLSSRQVRLGFDQLVEEINNKTPLSESEKEEDTYFVPDAPNLGSKWPSIYETHPRYFSEFTSQSPDSSQLRFGKLSAIGFNPAVLPTHQLIHEGASWRNPSGKYHGIEYPRFDALPPSSTGQGECNPQGQSGTKHHNYCGEHEGNLPHHHSSYSIDSIPNREKRRSGDVNLVEPSLEFSKDSFLPRTSENVSVESTEPIGCPIEIVEVPQGSNKNLASFCNKVKKIRESYHASDINSNSGKIWAITTAYPSRLFADTKFRVKISIDNSAQLLLLMPHANYLVKDLIAEILLLCANEPLSPKEYLLSVCGSEEFLQMDHSLGSHKIFQKNKSVIQLHLQKNRDTPGKLSRKSEDDHSPFHLNQLLEFTHIWKISRQCLSTVMKKYNLHVEHLLKPQKDMEEKHLSSMVSGNQHTSQPHVNNVLEEVKNICSVLGCIETKQVSDAVKELNLILQRPSQNFHQNSETSKKGFIERVTAELSRSIYQLIDVYCSSFCTDFQPVHTPGGVSHVHAGLQSHLSFTVCSLHNVPETWAHSYKAFSFSCWLTYAGKKLCQVKSCRPLPVTKSFSLLVNWNEIINFPLEIKSLPRESMLVIKLFGIDSATHSTNLLAWTCLPLFPRQESVLGSRLFSVTLQSEPPIEMIAPGVWDGSQPSPLTLQIDFPDAGWEYLKPESEENRTDHEEPPRECLKHIAKLSQKKSPLLLSEEKRRYLWFYRLYCNNENSSLPLVLGSAPGWDEETVSEMHAILRRWTFSHPWEALGLLTSRFPDQDIREVAVQQLDTLLTDELLDCLPQLVQAVKFEWNLESPLVELLPRRPLQSIRVAHCLYWLLRDAQGEAYFKSWYQELLAALQFCAGEALNEELSKEQKLVKLLGDIGEKVKSASDPQRKDVLKKEIGSLEEFFKDIKTCHLPLNPALCIKGIDRDACSYFTSNASPLKITFINANPMGKNISVIFKAGDDLRQDMLALQIIQVMDNAWLQEGLDMQMITYGCLSTGRAQGFIEMVPDAVTLAKIHLHSGLIGPLKENTIKKWFSQHNHLKEDYEKALRNFFYSCAGWCVVTFILGVCDRHNDNIMLTKSGHMFHIDFGKFLGHAQTFGGIKRDRAPFIFTSEMEYFITEGGKNIQHFQDFVELCCRAYNIVRKHSQLILSLLEMMLHAGLPELRGIEDLKYVHNNLRPQDTDLEATSHFTKKIKESLECFPVKLNNLIHTLAQMPALSLAKPAPQTLLQESCILNKTRTIQRVTILGFSKTHSNLYLMEVTCSDNRRSLTKKSFEQFYRLHSQMQKQFSSLALPEFPHWWHLPFTDSDHKRIRDLSHYVEQVLRGSYEVANSDCVLSFFLSEHIQPTLEDSPFVDPGENSLDKSPKVQLLMTYEDSRLTILVKHLKNIHLPDGSVPSAHVEIYLLPHPSEVRRKKTKCVPKCTDPTYNEIVVYDEVLGLQGHVLMLIVKSKTVFVGAVNIQLCSVPLNEEKWYPLGNSII
|
2.7.1.137; 2.7.1.154
| null |
cell migration [GO:0016477]; chemotaxis [GO:0006935]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; phosphatidylinositol 3-kinase complex [GO:0005942]; plasma membrane [GO:0005886]
|
1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; phosphatidylinositol binding [GO:0035091]
|
PF00168;PF00454;PF00792;PF00613;PF00787;
|
2.60.40.150;1.10.1070.11;1.25.40.70;3.30.1520.10;
|
PI3/PI4-kinase family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9514948}; Peripheral membrane protein {ECO:0000269|PubMed:9514948}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154; Evidence={ECO:0000269|PubMed:9514948}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374; Evidence={ECO:0000305|PubMed:9514948}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137; Evidence={ECO:0000269|PubMed:9514948}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710; Evidence={ECO:0000305|PubMed:9514948};
| null | null | null | null |
FUNCTION: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers (PubMed:9514948). May play a role in SDF1A-stimulated chemotaxis. {ECO:0000269|PubMed:20536348, ECO:0000269|PubMed:9514948}.
|
Mus musculus (Mouse)
|
O70172
|
PI42A_MOUSE
|
MATPGNLGSSVLASKTKTKKKHFVAQKVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQYIVECHGVTLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVECEENDGEEEGESDSTHPIGTPPDSPGNTLNSSPPLAPGEFDPNIDVYAIKCHENAPRKEVYFMAIIDILTHYDAKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFLDFIGHIL
|
2.7.1.149
| null |
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate biosynthetic process [GO:1902635]; autophagosome-lysosome fusion [GO:0061909]; megakaryocyte development [GO:0035855]; negative regulation of insulin receptor signaling pathway [GO:0046627]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphorylation [GO:0016310]; positive regulation of autophagosome assembly [GO:2000786]; regulation of autophagy [GO:0010506]; vesicle-mediated cholesterol transport [GO:0090119]
|
autophagosome [GO:0005776]; cytosol [GO:0005829]; lysosome [GO:0005764]; nucleus [GO:0005634]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]
|
1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; 1-phosphatidylinositol-5-phosphate 4-kinase activity [GO:0016309]; ATP binding [GO:0005524]; protein homodimerization activity [GO:0042803]
|
PF01504;
|
3.30.810.10;3.30.800.10;
| null |
PTM: Phosphorylated in tyrosines. Phosphorylation is induced by light and increases kinase activity. {ECO:0000250|UniProtKB:Q9R0I8}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20204506}. Nucleus {ECO:0000250|UniProtKB:P48426}. Lysosome {ECO:0000269|PubMed:29727621}. Cytoplasm {ECO:0000269|PubMed:20204506}. Photoreceptor inner segment {ECO:0000305|PubMed:20204506}. Cell projection, cilium, photoreceptor outer segment {ECO:0000305|PubMed:20204506}. Note=May translocate from the cytosol to the cell membrane upon activation of tyrosine phosphorylation. May translocate from the inner to the outer segments of the rod photoreceptor cells in response to light (PubMed:20204506). Localization to the nucleus is modulated by the interaction with PIP4K2B (By similarity). {ECO:0000250|UniProtKB:P48426, ECO:0000269|PubMed:20204506}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:12280, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57795, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.149; Evidence={ECO:0000250|UniProtKB:P48426}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12281; Evidence={ECO:0000250|UniProtKB:P48426}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + ATP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:55992, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:83423, ChEBI:CHEBI:84968, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P48426}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55993; Evidence={ECO:0000250|UniProtKB:P48426}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + GTP = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + GDP + H(+); Xref=Rhea:RHEA:55964, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:83423, ChEBI:CHEBI:84968; Evidence={ECO:0000250|UniProtKB:P48426}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55965; Evidence={ECO:0000250|UniProtKB:P48426};
| null | null | null | null |
FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Has both ATP- and GTP-dependent kinase activities. May exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2 (By similarity). May regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation (By similarity). Required for lysosome-peroxisome membrane contacts and intracellular cholesterol transport through modulating peroxisomal PtdIns(4,5)P2 level (By similarity). In collaboration with PIP4K2B, has a role in mediating autophagy in times of nutrient stress (PubMed:29727621). Required for autophagosome-lysosome fusion and the regulation of cellular lipid metabolism (PubMed:29727621). Negatively regulates insulin signaling through a catalytic-independent mechanism. PIP4Ks interact with PIP5Ks and suppress PIP5K-mediated PtdIns(4,5)P2 synthesis and insulin-dependent conversion to PtdIns(3,4,5)P3 (By similarity). May be involved in thrombopoiesis, and the terminal maturation of megakaryocytes and regulation of their size (PubMed:16434494). {ECO:0000250|UniProtKB:P48426, ECO:0000250|UniProtKB:Q9R0I8, ECO:0000269|PubMed:16434494, ECO:0000269|PubMed:29727621}.
|
Mus musculus (Mouse)
|
O70173
|
P3C2G_RAT
|
MAYNWQTEPNRAEPQEGGHDHQQCHHADQHLSSRQVRLGFDQLVEELSNKTPLPEDEKEGTCFVPDTPNLDSKWQSIYGPHPRHFNEFTSQSPHFSQLPFGKASAIGFNPAVLPAHQFIHEGASWRNPTRKYHGGEDPRFSALTPSSTGLDKCHQQGQSGTEHCNYYVEPENNVPHHYSPYSMDSIPDSEEKGSGDADLVEPSLVFSKDSFLPRASENMSVESTEPIGCPLEIVEAPQGSNKSLASFCNNVTKIRGLYHASDTNSNSGKIWAITTAYPSRLFADTQFRVKISTDNSAQLLLLKPPANYLVKDLIAEILLLCANEQLSPKEYLLSICGSEEFLQTDHCLGSHKIFQKSKSVIQLHLQRSRDTPGKLSRKRDDDRSRVHLNQLLEFTHIWKISRQCLSTVMKSYNLHVEHLLKTQEDVEEKPLSSMFSCGRHPPQPHGNDIIEDVRNICSVLGCIETKQVSDAVKELTLILQRPSQNFHQNSETSKKGFIENVTSELSRSLHQLVDVYCSSFCTDFRPARAPGGVSRDHAGLHSHLSFTVCSLHNVPETWAHSYKAFSFSCWLTYAGKKLCQVKSCRSLPVTKSFSFSVNWNEIINFPLEIKSLPRESMLVIKLFGIDSATHSANLLAWTCLPLFPKEKSPLGSRLLSMTLQSEPPIEMMAPGVWDGSQPTPLTLQIDFPAATWEYVKPETEENRTDHQEPPRECLKHIARLSQKQPPLLLSVEKRRYLWFYRFYCNNENSSLPLVLGSAPGWDEGTVSEMHAVLRRWTFSHPLEALGLLTSRFPDQDIREVAVQQLDNFLTDELLDCLPQLVQAVKFEWSLESPLVELLLHRSLQSIRVAHRLFWLLRDAQGEDYFKSWYQELLAALQFCAGEALIEELSKEQKLVKLLGDIGEKVKSAGDAQRKDVLKKEIGSLEEFFKDIKTCHLPLNPALCVKGIDRDACSYFTSNALPLKITFINANPMGKNISVIFKAGDDLRQDMLVLQIIQVMDNVWLQEGLDMQMIIYGCLATGKAQGFIEMVPDAVTLAKIHLHSGLIGPLKENTIKKWFSQHNHLKEDYEKALRNFFYSCAGWCVVTFILGVCDRHNDNIMLTKSGHMFHIDFGKFLGHAQTFGGIKRDRAPFIFTSEMEYFITEGGKNTQHFQDFVELCCRAYNIVRKHSQLLLSLLEMMLHAGLPELRGIEDLKYVHDNLRPQDTDLEATSHFTTKIKQSLECFPVKLNNLIHTLAQMPAFSLARPAPQTPPQECCVLNKTRTIQRVTILGFSKTHSNLYLIEVTRSDNRKNLAKKSFEQFYRLHSQIQKQFPLLTLPEFPHWWHLPFTDSHHERIRDLSHYVEQVLHGSYEVANSDCVLSFFLSEHIQQTLEDSPFVDPGDHSPDKSPQVQLLMTYEDTKLTILVKHLKNIHLPDGSAPSAHVEIYLLPHPSEVRRKKTKCVPKCTDPTYNEIVVYDDVSGLQGHVLMLIVKSKTVFVGAVNIQLCSVPLNEEKWYPLGNSII
|
2.7.1.137; 2.7.1.154
| null |
cell migration [GO:0016477]; chemotaxis [GO:0006935]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; phosphatidylinositol 3-kinase complex [GO:0005942]; plasma membrane [GO:0005886]
|
1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; phosphatidylinositol binding [GO:0035091]
|
PF00168;PF00454;PF00792;PF00794;PF00613;PF00787;
|
2.60.40.150;1.10.1070.11;1.25.40.70;3.30.1520.10;
|
PI3/PI4-kinase family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9516481}; Peripheral membrane protein {ECO:0000269|PubMed:9516481}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137; Evidence={ECO:0000269|PubMed:9516481}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710; Evidence={ECO:0000305|PubMed:9516481}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154; Evidence={ECO:0000269|PubMed:9516481}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374; Evidence={ECO:0000305|PubMed:9516481};
| null | null | null | null |
FUNCTION: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers (PubMed:9516481). May play a role in SDF1A-stimulated chemotaxis (By similarity). {ECO:0000250|UniProtKB:O70167, ECO:0000269|PubMed:9516481}.
|
Rattus norvegicus (Rat)
|
O70174
|
ACHA4_MOUSE
|
MEIGGSGAPPPLLLLPLLLLLGTGLLPASSHIETRAHAEERLLKRLFSGYNKWSRPVANISDVVLVRFGLSIAQLIDVDEKNQMMTTNVWVKQEWHDYKLRWDPGDYENVTSIRIPSELIWRPDIVLYNNADGDFAVTHLTKAHLFYDGRVQWTPPAIYKSSCSIDVTFFPFDQQNCTMKFGSWTYDKAKIDLVSMHSRVDQLDFWESGEWVIVDAVGTYNTRKYECCAEIYPDITYAFIIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKVTLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPRTHTMPAWVRRVFLDIVPRLLFMKRPSVVKDNCRRLIESMHKMANAPRFWPEPESEPGILGDICNQGLSPAPTFCNRMDTAVETQPTCRSPSHKVPDLKTSEVEKASPCPSPGSCHPPNSSGAPVLIKARSLSVQHVPSSQEAAEGSIRCRSRSIQYCVSQDGAASLTESKPTGSPASLKTRPSQLPVSDQTSPCKCTCKEPSPVSPITVLKAGGTKAPPQHLPLSPALTRAVEGVQYIADHLKAEDTDFSVKEDWKYVAMVIDRIFLWMFIIVCLLGTVGLFLPPWLAGMI
| null | null |
acetylcholine receptor signaling pathway [GO:0095500]; B cell activation [GO:0042113]; behavioral response to nicotine [GO:0035095]; calcium ion transport [GO:0006816]; exploration behavior [GO:0035640]; inhibitory postsynaptic potential [GO:0060080]; locomotory behavior [GO:0007626]; membrane depolarization [GO:0051899]; nervous system process [GO:0050877]; neuronal action potential [GO:0019228]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; regulation of dopamine secretion [GO:0014059]; regulation of membrane potential [GO:0042391]; respiratory gaseous exchange by respiratory system [GO:0007585]; response to acetylcholine [GO:1905144]; response to nicotine [GO:0035094]; sensory perception of pain [GO:0019233]; synaptic transmission, cholinergic [GO:0007271]
|
acetylcholine-gated channel complex [GO:0005892]; cholinergic synapse [GO:0098981]; dendrite [GO:0030425]; dopaminergic synapse [GO:0098691]; external side of plasma membrane [GO:0009897]; membrane [GO:0016020]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynaptic specialization membrane [GO:0099634]; presynaptic membrane [GO:0042734]; protein-containing complex [GO:0032991]; synapse [GO:0045202]
|
acetylcholine binding [GO:0042166]; acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; heterocyclic compound binding [GO:1901363]; monoatomic ion channel activity [GO:0005216]; protein-containing complex binding [GO:0044877]; quaternary ammonium group binding [GO:0050997]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Alpha-4/CHRNA4 sub-subfamily
| null |
SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane permeable to sodium ions.
|
Mus musculus (Mouse)
|
O70176
|
PACA_MOUSE
|
MTMCSGARLALLVYGIIMHSSVSCSPAAGLSFPGIRPEDEAYDQDGNPLQDFYDWDPPGVGSPASALRDAYALYYPADRRDVAHEILNEAYRKVLDQLSARKYLQSVVARGAGENLGGSAVDDPAPLTKRHSDGIFTDSYSRYRKQMAVKKYLAAVLGKRYKQRVKNKGRRIAYL
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; behavioral fear response [GO:0001662]; cAMP-mediated signaling [GO:0019933]; cellular response to glucocorticoid stimulus [GO:0071385]; histamine secretion [GO:0001821]; insulin secretion [GO:0030073]; negative regulation of acute inflammatory response to antigenic stimulus [GO:0002865]; negative regulation of acute inflammatory response to non-antigenic stimulus [GO:0002878]; negative regulation of cell cycle [GO:0045786]; negative regulation of glial cell proliferation [GO:0060253]; negative regulation of muscle cell apoptotic process [GO:0010656]; negative regulation of potassium ion transport [GO:0043267]; neuron projection development [GO:0031175]; neuropeptide signaling pathway [GO:0007218]; ovarian follicle development [GO:0001541]; pituitary gland development [GO:0021983]; positive regulation of cAMP-mediated signaling [GO:0043950]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of chemokine (C-C motif) ligand 5 production [GO:0071651]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of growth hormone secretion [GO:0060124]; positive regulation of GTPase activity [GO:0043547]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of somatostatin secretion [GO:0090274]; positive regulation of synaptic transmission, glutamatergic [GO:0051968]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; regulation of oligodendrocyte progenitor proliferation [GO:0070445]; regulation of postsynaptic membrane potential [GO:0060078]; regulation of protein localization [GO:0032880]; regulation of protein phosphorylation [GO:0001932]; response to ethanol [GO:0045471]; response to starvation [GO:0042594]; vasodilation [GO:0042311]
|
extracellular space [GO:0005615]; neuron projection [GO:0043005]; perikaryon [GO:0043204]; terminal bouton [GO:0043195]
|
neuropeptide hormone activity [GO:0005184]; peptide hormone receptor binding [GO:0051428]; pituitary adenylate cyclase activating polypeptide activity [GO:0016521]; pituitary adenylate cyclase-activating polypeptide receptor binding [GO:0031858]
|
PF00123;
|
6.10.250.590;
|
Glucagon family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Binding to its receptor activates G proteins and stimulates adenylate cyclase in pituitary cells (By similarity). Promotes neuron projection development through the RAPGEF2/Rap1/B-Raf/ERK pathway (By similarity). In chromaffin cells, induces long-lasting increase of intracellular calcium concentrations and neuroendocrine secretion (By similarity). Involved in the control of glucose homeostasis, induces insulin secretion by pancreatic beta cells (PubMed:23913443). {ECO:0000250|UniProtKB:P13589, ECO:0000250|UniProtKB:P18509, ECO:0000250|UniProtKB:Q29W19, ECO:0000269|PubMed:23913443}.
|
Mus musculus (Mouse)
|
O70183
|
BDNF_CAVPO
|
MTILFLTMVISYFGCMKAAPMKEASVRGPGSLAYPGVRTHGALESATGPKVGARGLTSSSSSSSSSLADTFEHVIEELLVEDQKARPHEESAKDADLYTSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSVSEWVTAADKKTAVDMSGGTVTVLEKVPVSKGQLKQYFYETKCNPMGYTKEGCRGIDKRHWNSQCRTTQSYVRALTMDSKKRIGWRFIRIDTSCVCTLTIKRGR
| null | null |
memory [GO:0007613]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of neuron apoptotic process [GO:0043524]; nerve development [GO:0021675]; nerve growth factor signaling pathway [GO:0038180]; neuron projection morphogenesis [GO:0048812]; peripheral nervous system development [GO:0007422]; positive regulation of collateral sprouting [GO:0048672]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; regulation of neuron differentiation [GO:0045664]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
axon [GO:0030424]; dendrite [GO:0030425]; extracellular space [GO:0005615]; synaptic vesicle [GO:0008021]
|
growth factor activity [GO:0008083]; nerve growth factor receptor binding [GO:0005163]
|
PF00243;
|
2.10.90.10;
|
NGF-beta family
|
PTM: [BDNF precursor form]: N-glycosylated and glycosulfated, contrary to mature BDNF. {ECO:0000250|UniProtKB:P23560}.; PTM: Mature BDNF is produced by proteolytic removal of the propeptide, catalyzed by a FURIN family member. In addition, the precursor form is proteolytically cleaved within the propeptide, but this is not an obligatory intermediate for the production of mature BDNF. Can be converted into mature BDNF by plasmin (PLG). {ECO:0000250|UniProtKB:P23560}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P23560}.; SUBCELLULAR LOCATION: [BDNF precursor form]: Secreted {ECO:0000250|UniProtKB:P23560}. Note=A proportion of BDNF is secreted as immature precursor (proBDNF). {ECO:0000250|UniProtKB:P23560}.
| null | null | null | null | null |
FUNCTION: Important signaling molecule that activates signaling cascades downstream of NTRK2 (By similarity). During development, promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. Participates in axonal growth, pathfinding and in the modulation of dendritic growth and morphology. Major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability (By similarity). {ECO:0000250|UniProtKB:P21237, ECO:0000250|UniProtKB:P23560}.; FUNCTION: [BDNF precursor form]: Important signaling molecule that activates signaling cascades downstream of NTRK2. Activates signaling cascades via the heterodimeric receptor formed by NGFR and SORCS2. Signaling via NGFR and SORCS2 plays a role in synaptic plasticity and long-term depression (LTD). Binding to NGFR and SORCS2 promotes neuronal apoptosis. Promotes neuronal growth cone collapse. {ECO:0000250|UniProtKB:P21237}.
|
Cavia porcellus (Guinea pig)
|
O70191
|
ATF5_MOUSE
|
MSLLATLGLELDRALLPASGLGWLVDYGKLPLAPAPLGPYEVLGGALEGGLPGGGEPLAGDGFSDWMTERVDFTALLPLEAPLPPGTLPPPSPAPPDLEAMASLLKKELEQMEDFFLDAPLLPPPSPPPPPPPAAAPSLPLPLPLPTFDLPQPPTLDTLDLLAVYCRSEAGPGDSGLSTLPVPQQPPPLAPLPSPARPAPYPSPASTRGDRKQKKRDQNKSAALRYRQRKRAEGEALEGECQGLEARNRELRERAESVEREIQYVKDLLIEVYKARSQRTRST
| null | null |
cerebellar granule cell precursor proliferation [GO:0021930]; circadian rhythm [GO:0007623]; fat cell differentiation [GO:0045444]; multicellular organism growth [GO:0035264]; negative regulation of apoptotic process [GO:0043066]; negative regulation of astrocyte differentiation [GO:0048712]; negative regulation of cell cycle G2/M phase transition [GO:1902750]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of neurogenesis [GO:0050768]; olfactory bulb interneuron development [GO:0021891]; olfactory bulb interneuron differentiation [GO:0021889]; olfactory lobe development [GO:0021988]; positive regulation of DNA-templated transcription [GO:0045893]; post-embryonic development [GO:0009791]; regulation of centrosome cycle [GO:0046605]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]
|
centrosome [GO:0005813]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667]
|
chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; heat shock protein binding [GO:0031072]; kinase binding [GO:0019900]; 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]; tubulin binding [GO:0015631]
|
PF00170;
|
1.20.5.170;
|
BZIP family
|
PTM: Acetylated at Lys-29 by EP300, the acetylation enhances the interaction with CEBPB, DNA-binding and transactivation activity. {ECO:0000269|PubMed:24216764}.; PTM: Ubiquitinated by CDC34 and UBE2B in order to be degraded by the proteasome. Cisplatin inhibits ubiquitination and proteasome-mediated degradation by inhibiting the interaction with CDC34. Ubiquitination and degradation by the proteasome are inhibited by NLK in a kinase-independent manner. {ECO:0000250|UniProtKB:Q9Y2D1}.; PTM: Phosphorylated by NLK, probably at Ser-92 and Ser-126. {ECO:0000250|UniProtKB:Q9Y2D1}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2D1}. Nucleus {ECO:0000269|PubMed:22095825}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y2D1}. Note=Actively transported to the centrosome and accumulated in the pericentriolar material (PCM) during G1 to M phase via a microtubule-dependent mechanism. During late telophase and cytokinesis, translocates from the centrosome to the midbody. {ECO:0000250|UniProtKB:Q9Y2D1}.
| null | null | null | null | null |
FUNCTION: Transcription factor that either stimulates or represses gene transcription through binding of different DNA regulatory elements such as cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), ATF5-specific response element (ARE) (consensus: 5'-C[CT]TCT[CT]CCTT[AT]-3') but also the amino acid response element (AARE), present in many viral and cellular promoters. Critically involved, often in a cell type-dependent manner, in cell survival, proliferation, and differentiation. Its transcriptional activity is enhanced by CCND3 and slightly inhibited by CDK4 (By similarity). Important regulator of the cerebral cortex formation, functions in cerebral cortical neuroprogenitor cells to maintain proliferation and to block differentiation into neurons. Must be down-regulated in order for such cells to exit the cycle and differentiate. Participates in the pathways by which SHH promotes cerebellar granule neuron progenitor cells proliferation (PubMed:22095825). Critical for survival of mature olfactory sensory neurons (OSN), directs expression of OSN-specific genes (PubMed:23090999). May be involved in osteogenic differentiation. Promotes cell proliferation and survival by inducing the expression of EGR1 sinergistically with ELK1. Once acetylated by EP300, binds to ARE sequences on target genes promoters, such as BCL2 and EGR1 (By similarity). Plays an anti-apoptotic role through the transcriptional regulation of BCL2, this function seems to be cell type-dependent (By similarity) (PubMed:12130540). Cooperates with NR1I3/CAR in the transcriptional activation of CYP2B6 in liver. In hepatic cells, represses CRE-dependent transcription and inhibits proliferation by blocking at G2/M phase. May act as a negative regulator of IL1B transduction pathway in liver. Upon IL1B stimulus, cooperates with NLK to activate the transactivation activity of C/EBP subfamily members. Besides its function of transcription factor, acts as a cofactor of CEBPB to activate CEBPA and promote adipocyte differentiation. Regulates centrosome dynamics in a cell-cycle- and centriole-age-dependent manner. Forms 9-foci symmetrical ring scaffold around the mother centriole to control centrosome function and the interaction between centrioles and pericentriolar material (By similarity). {ECO:0000250|UniProtKB:Q6P788, ECO:0000250|UniProtKB:Q9Y2D1, ECO:0000269|PubMed:12130540, ECO:0000269|PubMed:22095825, ECO:0000269|PubMed:23090999}.
|
Mus musculus (Mouse)
|
O70194
|
EIF3D_MOUSE
|
MAKFMTPVIQDNPSGWGPCAVPEQFRDMPYQPFSKGDRLGKVADWTGATYQDKRYTNKYSSQFGGGSQYAYFHEEDETSFQLVDTARTQKTAYQRNRMRFAQRNLRRDKDRRNMVQFNLQTLPKSAKQKERERIRLQKKFQKQFGVRQKWDQKSQKPRDSSVEVRSDWEVKEEMDFPQLMKMRYLEVSEPQDIECCGALEYYDKAFDRITTRSEKPLRSIKRIFHTVTTTDDPVIRKLAKTQGNVFATDAILATLMSCTRSVYSWDIVVQRVGSKLFFDKRDNSDFDLLTVSETANEPPQDEGNSFNSPRNLAMEATYINHNFSQQCLRMGRERYNFPNPNPFVEDDMDKNEIASVAYRYRRWKLGDDIDLIVRCEHDGVMTGANGEVSFINIKTLNEWDSRHCNGVDWRQKLDSQRGAVIATELKNNSYKLARWTCCALLAGSEYLKLGYVSRYHVKDSSRHVILGTQQFKPNEFASQINLSVENAWGILRCVIDICMKLEEGKYLILKDPNKQVIRVYSLPDGTFSSEEDEEDEEEEEEEEEEEET
| null | null |
cap-dependent translational initiation [GO:0002191]; formation of cytoplasmic translation initiation complex [GO:0001732]; IRES-dependent viral translational initiation [GO:0075522]; positive regulation of translation [GO:0045727]; translational initiation [GO:0006413]; viral translational termination-reinitiation [GO:0075525]
|
eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; eukaryotic translation initiation factor 3 complex, eIF3m [GO:0071541]; synapse [GO:0045202]
|
mRNA cap binding [GO:0098808]; translation initiation factor activity [GO:0003743]
|
PF05091;
| null |
EIF-3 subunit D family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003}.
| null | null | null | null | null |
FUNCTION: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. In the eIF-3 complex, EIF3D specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs. {ECO:0000255|HAMAP-Rule:MF_03003}.
|
Mus musculus (Mouse)
|
O70196
|
PPCE_RAT
|
MLSFQYPDVYRDETSVQDYHGHKICDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIRGLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNTLSDDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFTCMAWTHDGKGMFYNSYPQQDGKSDGTETSTNLHQKLCYHVLGTDQSEDVLCAEFPDEPKWMGGAELSDDGRYVLLSIWEGCDPVNRLWYCDLQQGSNGINGILKWVKLIDNFEGEYDYITNEGTVFTFKTNRNSPNYRLINIDFTDPDESKWKVLVPEHEKDVLEWVACVRSNFLVLCYLRNVKNILQLHDLTTGALLKTFPLDVGSVVGYSGRKKDSEIFYQFTSFLSPGVIYHCDLTREELEPRVFREVTVKGIDASDYQTIQVFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISITPNYSVSRLIFVRHMGGVLAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKEGYTTSKRLTINGGSNGGLLVAACANQRPDLFGCVIAQVGVMDMLKFHKFTIGHAWTTDYGCSDSKQHFEWLLKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIVGRSRKQSNPLLIHVDTKAGHGPGKPTAKVIEEVSDMFAFIARCLNIEWIQ
|
3.4.21.26
| null |
protein catabolic process [GO:0030163]; proteolysis [GO:0006508]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
endopeptidase activity [GO:0004175]; oligopeptidase activity [GO:0070012]; peptide binding [GO:0042277]; serine-type endopeptidase activity [GO:0004252]
|
PF00326;PF02897;
|
3.40.50.1820;2.130.10.120;
|
Peptidase S9A family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23687}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.; EC=3.4.21.26; Evidence={ECO:0000269|PubMed:10766975};
| null | null | null | null |
FUNCTION: Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Has high activity on the succinyl- (suc-) peptide-4-methylcoumaryl-7-amide (MCA) substrates suc-Gly-Pro-Leu-Gly-Pro-MCA, suc-Gly-Pro-MCA and suc-Ala-Ala-Ala-MCA. {ECO:0000269|PubMed:10766975}.
|
Rattus norvegicus (Rat)
|
O70200
|
AIF1_MOUSE
|
MSQSRDLQGGKAFGLLKAQQEERLEGINKQFLDDPKYSNDEDLPSKLEAFKVKYMEFDLNGNGDIDIMSLKRMLEKLGVPKTHLELKRLIREVSSGSEETFSYSDFLRMMLGKRSAILRMILMYEEKNKEHKRPTGPPAKKAISELP
| null | null |
actin crosslink formation [GO:0051764]; actin filament bundle assembly [GO:0051017]; actin filament polymerization [GO:0030041]; cellular response to oxidative stress [GO:0034599]; cellular response to type II interferon [GO:0071346]; inflammatory response [GO:0006954]; microglial cell activation [GO:0001774]; negative regulation of apoptotic process [GO:0043066]; negative regulation of gene expression [GO:0010629]; negative regulation of smooth muscle cell chemotaxis [GO:0071672]; negative regulation of smooth muscle cell proliferation [GO:0048662]; parallel actin filament bundle assembly [GO:0030046]; phagocytosis, engulfment [GO:0006911]; positive regulation of cell migration [GO:0030335]; positive regulation of chemokine production [GO:0032722]; positive regulation of fibroblast growth factor production [GO:0090271]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of monocyte chemotaxis [GO:0090026]; positive regulation of muscle hyperplasia [GO:0014739]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of smooth muscle cell chemotaxis [GO:0071673]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of T cell migration [GO:2000406]; positive regulation of T cell proliferation [GO:0042102]; Rac protein signal transduction [GO:0016601]; ruffle assembly [GO:0097178]
|
actin filament [GO:0005884]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; glial cell projection [GO:0097386]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; phagocytic cup [GO:0001891]; ruffle [GO:0001726]; ruffle membrane [GO:0032587]
|
actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]
|
PF21008;
|
1.10.238.10;
| null |
PTM: Phosphorylated on serine residues. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10934045}. Cell projection, ruffle membrane {ECO:0000269|PubMed:10934045, ECO:0000269|PubMed:14756805}; Peripheral membrane protein; Cytoplasmic side. Cell projection, phagocytic cup {ECO:0000269|PubMed:10934045, ECO:0000269|PubMed:14756805}. Note=Associated with the actin cytoskeleton at membrane ruffles and at sites of phagocytosis. {ECO:0000269|PubMed:10934045}.
| null | null | null | null | null |
FUNCTION: Actin-binding protein that enhances membrane ruffling and RAC activation. Enhances the actin-bundling activity of LCP1. Binds calcium. Plays a role in RAC signaling and in phagocytosis. May play a role in macrophage activation and function. Promotes the proliferation of vascular smooth muscle cells and of T-lymphocytes. Enhances lymphocyte migration. Plays a role in vascular inflammation. {ECO:0000269|PubMed:10934045, ECO:0000269|PubMed:11500035, ECO:0000269|PubMed:11722645, ECO:0000269|PubMed:11916959, ECO:0000269|PubMed:14756805}.
|
Mus musculus (Mouse)
|
O70201
|
BIRC5_MOUSE
|
MGAPALPQIWQLYLKNYRIATFKNWPFLEDCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDNPIEEHRKHSPGCAFLTVKKQMEELTVSEFLKLDRQRAKNKIAKETNNKQKEFEETAKTTRQSIEQLAA
| null | null |
apoptotic process [GO:0006915]; cell division [GO:0051301]; establishment of chromosome localization [GO:0051303]; G2/M transition of mitotic cell cycle [GO:0000086]; meiosis I [GO:0007127]; microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; mitotic cytokinesis [GO:0000281]; mitotic spindle assembly checkpoint signaling [GO:0007094]; mitotic spindle midzone assembly [GO:0051256]; mitotic spindle organization [GO:0007052]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of neuron apoptotic process [GO:0043524]; positive regulation of attachment of mitotic spindle microtubules to kinetochore [GO:1902425]; positive regulation of cell cycle [GO:0045787]; positive regulation of exit from mitosis [GO:0031536]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090267]; positive regulation of mitotic cytokinesis [GO:1903490]; positive regulation of mitotic sister chromatid separation [GO:1901970]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein ubiquitination [GO:0031398]; protein phosphorylation [GO:0006468]; protein-containing complex localization [GO:0031503]; regulation of cell cycle [GO:0051726]; regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061178]; regulation of mitotic cell cycle [GO:0007346]; regulation of type B pancreatic cell proliferation [GO:0061469]
|
apical plasma membrane [GO:0016324]; centriole [GO:0005814]; chromosome passenger complex [GO:0032133]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; interphase microtubule organizing center [GO:0031021]; kinetochore [GO:0000776]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; nucleus [GO:0005634]; spindle microtubule [GO:0005876]; survivin complex [GO:1990713]
|
cysteine-type endopeptidase inhibitor activity [GO:0004869]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; microtubule binding [GO:0008017]; protein homodimerization activity [GO:0042803]; tubulin binding [GO:0015631]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
|
PF00653;
| null |
IAP family
|
PTM: Ubiquitinated by the Cul9-RING ubiquitin-protein ligase complex, leading to its degradation. Ubiquitination is required for centrosomal targeting. Deubiquitinated by USP35 or USP38; leading to stabilization. {ECO:0000250|UniProtKB:O15392}.; PTM: Acetylation at Lys-129 results in its homodimerization, while deacetylation promotes the formation of monomers which heterodimerize with XPO1/CRM1 which facilitates its nuclear export. The acetylated form represses STAT3 transactivation. The dynamic equilibrium between its acetylation and deacetylation at Lys-129 determines its interaction with XPO1/CRM1, its subsequent subcellular localization, and its ability to inhibit STAT3 transactivation. {ECO:0000250|UniProtKB:O15392}.; PTM: In vitro phosphorylation at Thr-117 by AURKB prevents interaction with INCENP and localization to mitotic chromosomes. Phosphorylation at Thr-48 by CK2 is critical for its mitotic and anti-apoptotic activities. Phosphorylation at Thr-34 by CDK15 is critical for its anti-apoptotic activity. {ECO:0000250|UniProtKB:O15392}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15392}. Nucleus {ECO:0000250|UniProtKB:O15392}. Chromosome {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere {ECO:0000250|UniProtKB:O15392}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O15392}. Midbody {ECO:0000250|UniProtKB:O15392}. Note=Localizes at the centromeres from prophase to metaphase, at the spindle midzone during anaphase and a the midbody during telophase and cytokinesis. Accumulates in the nucleus upon treatment with leptomycin B (LMB), a XPO1/CRM1 nuclear export inhibitor (By similarity). Localizes on chromosome arms and inner centromeres from prophase through metaphase. Localizes to kinetochores in metaphase, distributes to the midzone microtubules in anaphase and at telophase, localizes exclusively to the midbody. Colocalizes with AURKB at mitotic chromosomes. Acetylation at Lys-129 directs its localization to the nucleus by enhancing homodimerization and thereby inhibiting XPO1/CRM1-mediated nuclear export (By similarity). {ECO:0000250|UniProtKB:E3SCZ8, ECO:0000250|UniProtKB:O15392}.
| null | null | null | null | null |
FUNCTION: Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis (PubMed:25778398). Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis (By similarity). Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules (By similarity). Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis (By similarity). The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules (By similarity). May counteract a default induction of apoptosis in G2/M phase (By similarity). The acetylated form represses STAT3 transactivation of target gene promoters (By similarity). May play a role in neoplasia. Inhibitor of CASP3 and CASP7 (By similarity). Essential for the maintenance of mitochondrial integrity and function (PubMed:25778398). {ECO:0000250|UniProtKB:O15392, ECO:0000269|PubMed:25778398}.
|
Mus musculus (Mouse)
|
O70209
|
PDLI3_MOUSE
|
MPQNVVLPGPAPWGFRLSGGIDFNQPLVITRITPGSKAAAANLCPGDVILAIDGFGTESMTHADAQDRIKAASYQLCLKIDRAETRLWSPQVSEDGKAHPFKINLEAEPQEFKPIGTAHNRRAQPFVAAANIDDKRQVVSASYNSPIGLYSTSNIQDALHGQLRGLIPGSLQNEPTASVPPQSDVYRMLHDNRDDPAAPRQSGSFRVLQDLVNDGPDDRPAGTRSVRAPVTKVHGGAGSAQRMPLCDKCGSGIVGAVVKARDKYRHPECFVCADCNLNLKQKGYFFVEGELYCETHARARTRPPEGYDTVTLYPKA
| null | null |
actin cytoskeleton organization [GO:0030036]; actin filament organization [GO:0007015]; heart development [GO:0007507]; muscle structure development [GO:0061061]
|
actin cytoskeleton [GO:0015629]; adherens junction [GO:0005912]; filamentous actin [GO:0031941]; stress fiber [GO:0001725]; Z disc [GO:0030018]
|
actin binding [GO:0003779]; actinin binding [GO:0042805]; cytoskeletal protein binding [GO:0008092]; metal ion binding [GO:0046872]; muscle alpha-actinin binding [GO:0051371]; structural constituent of muscle [GO:0008307]
|
PF15936;PF00412;PF00595;
|
2.30.42.10;2.10.110.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Note=Localizes to myofiber Z-lines. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May play a role in the organization of actin filament arrays within muscle cells. {ECO:0000250}.
|
Mus musculus (Mouse)
|
O70212
|
5HT3A_CAVPO
|
MVLWLQLALLALLLPTSLAQGEVRGKGTAQAHNSTRPALQRLSDHLLADYRKSVRPVRDWRKPTTVSIDAIVYAILSVDEKNQVLTTYIWYRQFWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYVRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDKSVFMNQGEWELLGVLTEFLEFSDRESRGSFAEMKFYVVIRRRPLFYAVTLLLPSIFLMIVDIVGFYLPPDSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLISVYFVVCMALLVISLAETILIVRLVHKQDLQQPVPLWLRHLVLERIAGLLCLGEQLTSHRGPATLQATKTDDFSGSTLLPAMGNHCGPLGGPQDLEKTSRGRGSPPPPPREASLAMCGLLQELASIRHFLEKREETREVARDWLRVGSVLDKLLFRVYLLAVLAYSITLVTLWSVWHYA
| null | null |
monoatomic cation transport [GO:0006812]
|
neuron projection [GO:0043005]; postsynaptic membrane [GO:0045211]; synaptic vesicle membrane [GO:0030672]
|
acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; GABA-A receptor activity [GO:0004890]; serotonin-gated monoatomic cation channel activity [GO:0022850]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, 5-hydroxytryptamine receptor (TC 1.A.9.2) subfamily, HTR3A sub-subfamily
| null |
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P46098}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23979}. Cell membrane {ECO:0000250|UniProtKB:P46098}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23979}.
|
CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P46098}; CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P46098}; CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P46098}; CATALYTIC ACTIVITY: Reaction=Mg(2+)(in) = Mg(2+)(out); Xref=Rhea:RHEA:29827, ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P46098};
| null | null | null | null |
FUNCTION: Forms serotonin (5-hydroxytryptamine/5-HT3)-activated cation-selective channel complexes, which when activated cause fast, depolarizing responses in neurons. {ECO:0000269|PubMed:9463477}.
|
Cavia porcellus (Guinea pig)
|
O70215
|
NKG2D_RAT
|
MSKCHNYDLKPAKWDTSQEHQKQRSALPTSRPGENGIIRRRSSIEELKISPLFVVRVLVAAMTIRFTVITLTWLAVFITLLCNKEVSVSSREGYCGPCPNDWICHRNNCYQFFNENKAWNQSQASCLSQNSSLLKIYSKEEQDFLKLVKSYHWMGLVQSPANGSWQWEDGSSLSPNELTLVKTPSGTCAVYGSSFKAYTEDCSNPNTYICMKRAV
| null | null |
adaptive immune response [GO:0002250]; cell differentiation [GO:0030154]; cellular response to lipopolysaccharide [GO:0071222]; defense response to Gram-positive bacterium [GO:0050830]; natural killer cell activation [GO:0030101]; natural killer cell mediated cytotoxicity [GO:0042267]; negative regulation of natural killer cell chemotaxis [GO:2000502]; nitric oxide biosynthetic process [GO:0006809]; positive regulation of apoptotic process [GO:0043065]; positive regulation of myeloid dendritic cell activation [GO:0030887]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]; positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target [GO:0002860]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of type II interferon production [GO:0032729]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]
|
cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]
|
carbohydrate binding [GO:0030246]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; MHC class I protein binding [GO:0042288]; MHC class Ib receptor activity [GO:0032394]; signaling receptor activity [GO:0038023]
|
PF00059;
|
3.10.100.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Colocalized with HCST on the cell surface. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Functions as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress-inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. Provides both stimulatory and costimulatory innate immune responses on activated killer (NK) cells, leading to cytotoxic activity. Acts as a costimulatory receptor for T-cell receptor (TCR) in CD8(+) T-cell-mediated adaptive immune responses by amplifying T-cell activation. Stimulates perforin-mediated elimination of ligand-expressing tumor cells. Signaling involves calcium influx, culminating in the expression of TNF-alpha. Participates in NK cell-mediated bone marrow graft rejection. May play a regulatory role in differentiation and survival of NK cells. Binds to ligands belonging to various subfamilies of MHC class I-related glycoproteins. {ECO:0000269|PubMed:15048723}.
|
Rattus norvegicus (Rat)
|
O70220
|
FOXQ1_MOUSE
|
MKLEVFVPRAAHGDKMGSDLEGAGSSDVPSPLSAAGDDSLGSDGDCAANSPAAGSGAGDLEGGGGERNSSGGPSAQDGPEATDDSRTQASAAGPCAGGVGGGEGARSKPYTRRPKPPYSYIALIAMAIRDSAGGRLTLAEINEYLMGKFPFFRGSYTGWRNSVRHNLSLNDCFVKVLRDPSRPWGKDNYWMLNPNSEYTFADGVFRRRRKRLSHRTTVSASGLRPEEAPPGPAGTPQPAPAARSSPIARSPARQEERSSPASKFSSSFAIDSILSKPFRSRRDGDSALGVQLPWGAAPCPPLRAYPALLPAAPGGALLPLCAYGASEPTLLASRGTEVQPAAPLLLAPLSTAAPAKPFRGPETAGAAHLYCPLRLPTALQAAAACGPGPHLSYPVETLLA
| null | null |
anatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; hair follicle morphogenesis [GO:0031069]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00250;
|
1.10.10.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
| null | null | null | null | null |
FUNCTION: Plays a role in hair follicle differentiation. {ECO:0000269|PubMed:16835220}.
|
Mus musculus (Mouse)
|
O70228
|
ATP9A_MOUSE
|
MTDSIPLQPVRHKKRVDSRPRAGCCEWLRCCGGGEPRPRTVWLGHPEKRDQRYPRNVINNQKYNFFTFLPGVLFSQFRYFFNFYFLLLACSQFVPEMRLGALYTYWVPLGFVLAVTIIREAVEEIRCYVRDKEMNSQVYSRLTSRGTVKVKSSNIQVGDLILVEKNQRVPADMIFLRTSEKNGSCFLRTDQLDGETDWKLRLPVACTQRLPTAADLLQIRSYVYAEEPNIDIHNFLGTFTREDSDPPISESLSIENTLWAGTVIASGTVVGVVLYTGRELRSVMNTSDPRSKIGLFDLEVNCLTKILFGALVVVSLVMVALQHFAGRWYLQIIRFLLLFSNIIPISLRVNLDMGKIVYSWVIRRDSKIPGTVVRSSTIPEQLGRISYLLTDKTGTLTQNEMVFKRLHLGTVAYGLDSMDEVQSHIFSIYTQQSQDPPAQKGPTVTTKVRRTMSSRVHEAVKAIALCHNVTPVYESNGVTDQAEAEKQFEDSCRVYQASSPDEVALVQWTESVGLTLVGRDQSSMQLRTPGDQVLNLTILQVFPFTYESKRMGIIVRDESTGEITFYMKGADVVMAGIVQYNDWLEEECGNMAREGLRVLVVAKKSLTEEQYQDFEARYVQAKLSVHDRSLKVATVIESLEMEMELLCLTGVEDQLQADVRPTLETLRNAGIKVWMLTGDKLETATCTAKNAHLVTRNQDIHVFRLVTNRGEAHLELNAFRRKHDCALVISGDSLEVCLKYYEYEFMELACQCPAVVCCRCAPTQKAQIVRLLQERTGKLTCAVGDGGNDVSMIQESDCGVGVEGKEGKQASLAADFSITQFKHLGRLLMVHGRNSYKRSAALSQFVIHRSLCISTMQAVFSSVFYFASVPLYQGFLIIGYSTIYTMFPVFSLVLDKDVKSEVAMLYPELYKDLLKGRPLSYKTFLIWVLISIYQGSTIMYGALLLFESEFVHIVAISFTSLILTELLMVALTIQTWHWLMTVAELLSLACYIASLVFLHEFIDVYFIATLSFLWKVSVITLVSCLPLYVLKYLRRRFSPPSYSKLTS
|
7.6.2.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P40527};
|
endocytosis [GO:0006897]; negative regulation of exosomal secretion [GO:1903542]; neuron projection morphogenesis [GO:0048812]; phospholipid translocation [GO:0045332]; regulation of endocytic recycling [GO:2001135]; regulation of retrograde transport, endosome to Golgi [GO:1905279]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]
|
early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; magnesium ion binding [GO:0000287]
|
PF13246;PF00122;PF00702;PF16212;PF16209;
|
3.40.1110.10;2.70.150.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily
| null |
SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:36604604}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:36604604}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:36604604}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:O75110}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O75110}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O75110}. Note=Efficient exit from the endoplasmic reticulum does not require TMEM30A, nor TMEM30B. Transiently expressed in the cell membrane. {ECO:0000250|UniProtKB:O75110}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:O75110};
| null | null | null | null |
FUNCTION: Plays a role in regulating membrane trafficking of cargo proteins, namely endosome to plasma membrane recycling, probably acting through RAB5 and RAB11 activation (PubMed:36604604). Also involved in endosome to trans-Golgi network retrograde transport (By similarity). In complex with MON2 and DOP1B, regulates SNX3 retromer-mediated endosomal sorting of WLS, a transporter of Wnt morphogens in developing tissues. Participates in the formation of endosomal carriers that direct WLS trafficking back to Golgi, away from lysosomal degradation. Appears to be implicated in intercellular communication by negatively regulating the release of exosomes. The flippase activity towards membrane lipids and its role in membrane asymmetry remains to be proved. Required for the maintenance of neurite morphology and synaptic transmission (PubMed:36604604). {ECO:0000250|UniProtKB:O75110, ECO:0000269|PubMed:36604604}.
|
Mus musculus (Mouse)
|
O70230
|
ZN143_MOUSE
|
MLLAQINRDSQGMTEFPGGGMEAQHVTLCLTEAVTVADGDNLENMEGVSLQAVTLADGSTAYIQHNSKDGRLIDGQVIQLEDGSAAYVQHVPIPKSTGDSLRLEDGQAVQLEDGTTAFIHHTSKDSYDQSSLQAVQLEDGTTAYIHHAVQVPQSDTILAIQADGTVAGLHTGDATIDPDTISALEQYAAKVSIDGSDGVTSTGMIGENEQEKKMQIVLQGHATRVTPKSQQSGEKAFRCKYDGCGKLYTTAHHLKVHERSHTGDRPYQCEHSGCGKAFATGYGLKSHFRTHTGEKPYRCSEDNCTKSFKTSGDLQKHIRTHTGERPFKCPIEGCGRSFTTSNIRKVHIRTHTGERPYYCTEPGCGRAFASATNYKNHVRIHTGEKPYVCTVPGCDKRFTEYSSLYKHHVVHTHSKPYNCNHCGKTYKQISTLAMHKRTAHNDTEPIEEEQEAFFEPPPGQGDDVLKGSQITYVTGVDGEDIVSTQVATVTQSGLSQQVTLISQDGTQHVNISQADMQAIGNTITMVTQDGTPITVPTHDAVISSAGTHSVAMVTAEGTEGQQVAIVAQDLAAFHTASSEMGHQQHSHHLVTTETRPLTLVATSNGTQIAVQLGEQPSLEEAIRIASRIQQGETPGLDD
| null | null |
positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
|
PcG protein complex [GO:0031519]; transcription regulator complex [GO:0005667]
|
chromatin binding [GO:0003682]; 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]
|
PF00096;
|
3.30.160.60;
|
GLI C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator. Activates the gene for selenocysteine tRNA (tRNAsec). Binds to the SPH motif of small nuclear RNA (snRNA) gene promoters. Participates in efficient U6 RNA polymerase III transcription via its interaction with CHD8 (By similarity). {ECO:0000250, ECO:0000269|PubMed:9535833}.
|
Mus musculus (Mouse)
|
O70237
|
GFI1B_MOUSE
|
MPRSFLVKSKKAHTYHQPRAQGDELVWPPAVIPVAKEHSQSASPLLSTPLPSQTLDWNTIKQEREMLLNQSLPKMASAPEGPLVTPQPQDGESPLSESPPFYKPSFSWDTLASSYSHSYTQTPSTMQSAFLERSVRLYGSPLVPSTESPLDFRLRYSPGMDTYHCVKCNKVFSTPHGLEVHVRRSHSGTRPFACDVCGKTFGHAVSLEQHTHVHSQERSFECRMCGKAFKRSSTLSTHLLIHSDTRPYPCQFCGKRFHQKSDMKKHTYIHTGEKPHKCQVCGKAFSQSSNLITHSRKHTGFKPFSCELCTKGFQRKVDLRRHRESQHNLK
| null | null |
positive regulation of granulocyte differentiation [GO:0030854]; regulation of erythrocyte differentiation [GO:0045646]; regulation of hemopoiesis [GO:1903706]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00096;
|
3.30.160.60;
| null |
PTM: Methylation at Lys-8 in the SNAG domain seems required for the recruitment of the corepressor complex. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12594258}. Note=Localized at foci of pericentric heterochromatin.
| null | null | null | null | null |
FUNCTION: Essential proto-oncogenic transcriptional regulator necessary for development and differentiation of erythroid and megakaryocytic lineages. Component of a RCOR-GFI-KDM1A-HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development and controls hematopoietic differentiation. Transcriptional repressor or activator depending on both promoter and cell type context; represses promoter activity of SOCS1 and SOCS3 and thus, may regulate cytokine signaling pathways. Cooperates with GATA1 to repress target gene transcription, such as the apoptosis regulator BCL2L1; GFI1B silencing in leukemic cell lines markedly increase apoptosis rate. Inhibits down-regulation of MYC and MYB as well as the cyclin-dependent kinase inhibitor CDKN1A/P21WAF1 in IL6-treated myelomonocytic cells. Represses expression of GATA3 in T-cell lymphomas and inhibits GATA1-mediated transcription; as GATA1 also mediates erythroid GFI1B transcription, both GATA1 and GFI1B participate in a feedback regulatory pathway controlling the expression of GFI1B gene in erythroid cells. Suppresses GATA1-mediated stimulation of GFI1B promoter through protein interaction. Binds to gamma-satellite DNA and to its own promoter, auto-repressing its own expression. Alters histone methylation by recruiting histone methyltransferase to target genes promoters. Plays a role in heterochromatin formation. {ECO:0000269|PubMed:11696536, ECO:0000269|PubMed:12351384, ECO:0000269|PubMed:12594258, ECO:0000269|PubMed:15718298, ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:9566867}.
|
Mus musculus (Mouse)
|
O70239
|
AXIN1_RAT
|
MNVQEQGFPLDLGASFTEDAPRPPVPGEEGELVSTDSRPVNHSFCSGKGTSIKSETSTATPRRSDLDLGYEPEGSASPTPPYLRWAESLHSLLDDQDGISLFRTFLKQEGCADLLDFWFACSGFRKLEPCDSNEEKRLKLARAIYRKYILDSNGIVSRQTKPATKSFIKDCVMKQQIDPAMFDQAQTEIQSTMEENTYPSFLKSDIYLEYTRTGSESPKVCSDQSSGSGTGKGMSGYLPTLNEDEEWKCDQDADEDDGRDSVPPSRLTQKLLLETAAPRAPSSRRYNEGRELRYGSWREPVNPYYVNSGYALAPATSANDSEQQSLSSDADTLSLTDSSVDGIPPYRIRKQHRREMQESVQVNGRVPLPHIPRTYRMPKEIRVEPQKFAEELIHRLEAVQRTREAEEKLEERLKRVRMEEEGEDGEMPSGPMASHKLPSVPAWHHFPPRYVDMGCSGLRDAHEENPESILDEHVQRVMRTPGCQSPGPGHRSPDSGHVAKTAVLGGTASGHGKHAPKLGLKLDSAGLHHHRHVHHHVHHNSARPKEQMEAEAARRVQSSFSWGPETHGHAKPRSYSESTGTNPSAGDLAFGGKASAPSKRNTKKAESGKNASAEVPSTTEDAEKNQKIMQWIIEGEKEISRHRKAGHGSSGMRKQQAHESSRPLSIERPGAVHPWVSAQLRNSVQPSHLFIQDPTMPPNPAPNPLTQLEEARRRLEEEEKRANKLPSKQRTKSQRKAGGGSAPPCDSIVVAYYFCGEPIPYRTLVRGRAVTLGQFKELLTKKGSYRYYFKKVSDEFDCGVVFEEVREDEAILPVFEEKIIGKVEKVD
| null | null |
adult walking behavior [GO:0007628]; apoptotic process [GO:0006915]; axial mesoderm development [GO:0048318]; axial mesoderm formation [GO:0048320]; canonical Wnt signaling pathway [GO:0060070]; cell development [GO:0048468]; cytoplasmic microtubule organization [GO:0031122]; dorsal/ventral axis specification [GO:0009950]; dorsal/ventral pattern formation [GO:0009953]; embryonic skeletal joint morphogenesis [GO:0060272]; epigenetic programming in the zygotic pronuclei [GO:0044725]; erythrocyte homeostasis [GO:0034101]; head development [GO:0060322]; hemoglobin metabolic process [GO:0020027]; in utero embryonic development [GO:0001701]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of gene expression [GO:0010629]; negative regulation of protein metabolic process [GO:0051248]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; negative regulation of Wnt signaling pathway [GO:0030178]; nervous system process [GO:0050877]; nucleocytoplasmic transport [GO:0006913]; positive regulation of JNK cascade [GO:0046330]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; positive regulation of ubiquitin-dependent protein catabolic process [GO:2000060]; post-anal tail morphogenesis [GO:0036342]; protein catabolic process [GO:0030163]; protein polyubiquitination [GO:0000209]; protein-containing complex assembly [GO:0065003]; regulation of canonical Wnt signaling pathway [GO:0060828]; regulation of protein phosphorylation [GO:0001932]; response to quercetin [GO:1905235]; sensory perception of sound [GO:0007605]; Wnt signaling pathway [GO:0016055]
|
beta-catenin destruction complex [GO:0030877]; cell cortex [GO:0005938]; cell periphery [GO:0071944]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; lateral plasma membrane [GO:0016328]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; synapse [GO:0045202]; Wnt signalosome [GO:1990909]
|
armadillo repeat domain binding [GO:0070016]; beta-catenin binding [GO:0008013]; enzyme binding [GO:0019899]; I-SMAD binding [GO:0070411]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; p53 binding [GO:0002039]; protein domain specific binding [GO:0019904]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein self-association [GO:0043621]; R-SMAD binding [GO:0070412]; signaling receptor binding [GO:0005102]; SMAD binding [GO:0046332]; ubiquitin ligase-substrate adaptor activity [GO:1990756]; ubiquitin protein ligase binding [GO:0031625]
|
PF16646;PF08833;PF00778;PF00615;
|
1.10.196.10;2.40.240.130;1.10.167.10;
| null |
PTM: Phosphorylation and dephosphorylation of AXIN1 regulates assembly and function of the beta-catenin complex. Phosphorylated by CK1 and GSK3B. Dephosphorylated by PPP1CA and PPP2CA. Phosphorylation by CK1 enhances binding of GSK3B to AXIN1. Also phosphorylated by CDK2 which regulates interaction with CTNBB1 (By similarity). {ECO:0000250}.; PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination and subsequent activation of the Wnt signaling pathway (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation and subsequent activation of the Wnt signaling pathway. Sumoylation at Lys-858 and Lys-861 prevents ubiquitination and degradation. Sumoylation is required for AXIN1-mediated JNK activation. Deubiquitinated by USP34, deubiquitinated downstream of beta-catenin stabilization step: deubiquitination is important for nuclear accumulation during Wnt signaling to positively regulate beta-catenin (CTNBB1)-mediated transcription (By similarity). Ubiquitination by SIAH1 and SIAH2 induces its proteasomal degradation as part of the activation of the Wnt signaling pathway (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O15169}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15169}. Nucleus {ECO:0000250|UniProtKB:O15169}. Cell membrane {ECO:0000269|PubMed:16815997}. Membrane {ECO:0000250|UniProtKB:O35625}. Note=On UV irradiation, translocates to the nucleus and colocalizes with DAAX (By similarity). MACF1 is required for its translocation to cell membrane (By similarity). {ECO:0000250|UniProtKB:O15169, ECO:0000250|UniProtKB:O35625}.
| null | null | null | null | null |
FUNCTION: Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (By similarity). Controls dorsoventral patterning via two opposing effects; down-regulates beta-catenin to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway (By similarity). Also facilitates the phosphorylation of APC by GSK3B (By similarity). Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation (By similarity). Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7 (By similarity). {ECO:0000250|UniProtKB:O15169}.
|
Rattus norvegicus (Rat)
|
O70240
|
AXIN2_RAT
|
MSSAVLVTLLPDPSSSFREDAPRPPVPGEEGETPPCQPSVGKVQSTKPMPVSSNARRNEDGLGEPEGRASPDSPLTRWTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRVAKAIYKRYIENNSVVSKQLKPATKTYIRDGIKKQQIGSVMFDQAQTEIQAVMEENAYQVFLTSDIYLEYVRSGGENTAYMSNGGLGSLKVLCGYLPTLNEEEEWTCADLKCKLSPTVVGLSSKTLRATASVRSTETAENGFRSFKRSEPVNPYHVGSGYVFAPATSANDSELSSDALTDDSMSMTDSSVDGIPPYRMGSKKQLQREMHRSVKANGQVSLPHFPRTHRLPKEMTPVEPAAFAAELISRLEKLKLELESRHSLEERLQQIREDEEKEGSEQALSSRDGAPVQHPLALLPSGSYEEDPQTILDDHLSRVLKTPGCQSPGVGRYSPRSRSPDHHHHHHQQCHALLPTGGKLPPEAACPLLGGKSFLTKQTTKHVHHHYIHHHAVPKTKEEIEAEATQRVRCLCPGGTDYYCYSKCKSHSKPPEPLPGEQFCGSRGGTLPKRNTKGTEPGLALPAREGGMSSAAGAPQLPGEEGDRSQDVWQWMLESERQSKSKPHSTQSIRKSYPLESARAPPGERVSRHHLLGASGHPRSAARAHPFTQDPAMPPLTPPNTLAQLEEACRRLAEVSKPQKQRCCVASQQRDRNHPATGQAGPTSFSNPSLASEDHKEPKRLASVHALQASELIVTYFFCGEEIPYRRMLKAQSLTLGHFKEQLSKKGNYRYYFKKASDEFACGAVFEEIWDDETVLPMYEGRILGKVERID
| null | null |
aortic valve morphogenesis [GO:0003180]; bone mineralization [GO:0030282]; canonical Wnt signaling pathway [GO:0060070]; cell development [GO:0048468]; cell population proliferation [GO:0008283]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to organic cyclic compound [GO:0071407]; chondrocyte differentiation involved in endochondral bone morphogenesis [GO:0003413]; dorsal/ventral axis specification [GO:0009950]; intramembranous ossification [GO:0001957]; maintenance of DNA repeat elements [GO:0043570]; mitral valve morphogenesis [GO:0003183]; mRNA stabilization [GO:0048255]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of osteoblast proliferation [GO:0033689]; negative regulation of Wnt signaling pathway [GO:0030178]; odontogenesis [GO:0042476]; osteoblast differentiation [GO:0001649]; osteoblast proliferation [GO:0033687]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein phosphorylation [GO:0001934]; protein localization [GO:0008104]; regulation of centromeric sister chromatid cohesion [GO:0070602]; regulation of chondrocyte development [GO:0061181]; regulation of extracellular matrix organization [GO:1903053]; regulation of mismatch repair [GO:0032423]; regulation of Wnt signaling pathway [GO:0030111]; response to steroid hormone [GO:0048545]; secondary heart field specification [GO:0003139]; somitogenesis [GO:0001756]; stem cell proliferation [GO:0072089]
|
beta-catenin destruction complex [GO:0030877]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
beta-catenin binding [GO:0008013]; enzyme binding [GO:0019899]; I-SMAD binding [GO:0070411]; molecular adaptor activity [GO:0060090]; protein kinase binding [GO:0019901]; ubiquitin protein ligase binding [GO:0031625]
|
PF16646;PF08833;PF00778;PF00615;
|
1.10.196.10;2.40.240.130;1.10.167.10;
| null |
PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination and subsequent activation of the Wnt signaling pathway. {ECO:0000250|UniProtKB:Q9Y2T1}.; PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation and subsequent activation of the Wnt signaling pathway. Deubiquitinated by USP34, deubiquitinated downstream of beta-catenin stabilization step: deubiquitination is important Wnt signaling to positively regulate beta-catenin (CTNBB1)-mediated transcription. {ECO:0000250|UniProtKB:Q9Y2T1}.; PTM: Probably phosphorylated by GSK3B and dephosphorylated by PP2A. {ECO:0000250|UniProtKB:O15169}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2T1}.
| null | null | null | null | null |
FUNCTION: Inhibitor of the Wnt signaling pathway. Down-regulates beta-catenin. Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B. {ECO:0000250|UniProtKB:O15169}.
|
Rattus norvegicus (Rat)
|
O70244
|
CUBN_RAT
|
MSSQFLWGFVTLLMIAELDGKTGKPEQRGQKRIADLHQPRMTTEEGNLVFLTSSTQNIEFRTGSLGKIKLNDEDLGECLHQIQRNKDDIIDLRKNTTGLPQNILSQVHQLNSKLVDLERDFQNLQQNVERKVCSSNPCLNGGTCVNLHDSFVCICPSQWKGLFCSEDVNECVVYSGTPFGCQSGSTCVNTVGSFRCDCTPDTYGPQCASKYNDCEQGSKQLCKHGICEDLQRVHHGQPNFHCICDAGWTTPPNGISCTEDKDECSLQPSPCSEHAQCFNTQGSFYCGACPKGWQGNGYECQDINECEINNGGCSQAPLVPCLNTPGSFSCGNCPAGFSGDGRVCTPVDICSIHNGGCHPEATCSSSPVLGSFLPVCTCPPGYTGNGYGSNGCVRLSNICSRHPCVNGQCIETVSSYFCKCDSGWSGQNCTENINDCSSNPCLNGGTCIDGINGFTCDCTSSWTGYYCQTPQAACGGILSGTQGTFAYHSPNDTYIHNVNCFWIVRTDEEKVLHVTFTFFDLESASNCPREYLQIHDGDSSADFPLGRYCGSRPPQGIHSSANALYFHLYSEYIRSGRGFTARWEAKLPECGGILTDNYGSITSPGYPGNYPPGRDCVWQVLVNPNSLITFTFGTLSLESHNDCSKDYLEIRDGPFHQDPVLGKFCTSLSTPPLKTTGPAARIHFHSDSETSDKGFHITYLTTQSDLDCGGNYTDTDGELLLPPLSGPFSHSRQCVYLITQAQGEQIVINFTHVELESQMGCSHTYIEVGDHDSLLRKICGNETLFPIRSVSNKVWIRLRIDALVQKASFRADYQVACGGMLRGEGFFRSPFYPNAYPGRRTCRWTISQPQRQVVLLNFTDFQIGSSASCDTDYIEIGPSSVLGSPGNEKFCSSNIPSFITSVYNILYVTFVKSSSMENRGFTAKFSSDKLECGEVLTASTGIIESPGHPNVYPRGVNCTWHVVVQRGQLIRLEFSSFYLEFHYNCTNDYLEIYDTAAQTFLGRYCGKSIPPSLTSNSNSIKLIFVSDSALAHEGFSINYEAIDASSVCLYDYTDNFGMLSSPNFPNNYPSNWECIYRITVGLNQQIALHFTDFTLEDYFGSQCVDFVEIRDGGYETSPLVGIYCGSVLPPTIISHSNKLWLKFKSDAALTAKGFSAYWDGSSTGCGGNLTTPTGVLTSPNYPMPYYHSSECYWRLEASHGSPFELEFQDFHLEHHPSCSLDYLAVFDGPTTNSRLIDKLCGDTTPAPIRSNKDVVLLKLRTDAGQQGRGFEINFRQRCDNVVIVNKTSGILESINYPNPYDKNQRCNWTIQATTGNTVNYTFLGFDVESYMNCSTDYVELYDGPQWMGRYCGNNMPPPGATTGSQLHVLFHTDGINSGEKGFKMQWFTHGCGGEMSGTAGSFSSPGYPNSYPHNKECIWNIRVAPGSSIQLTIHDFDVEYHTSCNYDSLEIYAGLDFNSPRIAQLCSQSPSANPMQVSSTGNELAIRFKTDSTLNGRGFNASWRAVPGGCGGIIQLSRGEIHSPNYPNNYRANTECSWIIQVERHHRVLLNITDFDLEAPDSCLRLMDGSSSTNARVASVCGRQQPPNSIIASGNSLFVRFRSGSSSQNRGFRAEFREECGGRIMTDSSDTIFSPLYPHNYLHNQNCSWIIEAQPPFNHITLSFTHFQLQNSTDCTRDFVEILDGNDYDAPVQGRYCGFSLPHPIISFGNALTVRFVTDSTRSFEGFRAIYSASTSSCGGSFYTLDGIFNSPDYPADYHPNAECVWNIASSPGNRLQLSFLSFNLENSLNCNKDFVEIREGNATGHLIGRYCGNSLPGNYSSAEGHSLWVRFVSDGSGTGMGFQARFKNIFGNNNIVGTHGKIASPFWPGKYPYNSNYKWVVNVDAYHIIHGRILEMDIEPTTNCFYDSLKIYDGFDTHSRLIGTYCGTQTESFSSSRNSLTFQFSSDSSVSGRGFLLEWFAVDVSDSTPPTIAPGACGGFMVTGDTPVHIFSPGWPREYANGADCIWIIYAPDSTVELNILSLDIEPQQSCNYDKLIVKDGDSDLSPELAVLCGVSPPGPIRSTGEYMYIRFTSDTSVAGTGFNASFHKSCGGYLHADRGVITSPKYPDTYLPNLNCSWHVLVQTGLTIAVHFEQPFQIQNRDSFCSQGDYLVLRNGPDNHSPPLGPSGRNGRFCGMYAPSTLFTSGNEMFVQFISDSSNGGQGFKIRYEAKSLACGGTVYIHDADSDGYLTSPNYPANYPQHAECIWILEAPPGRSIQLQFEDQFNIEDTPNCSVSYLELRDGANSNARLVSKLCGHTLPHSWVSSRERIYLKFHTDGGSSYMGFKAKYSIASCGGTVSGDSGVIESIGYPTLPYANNVFCQWFIRGLPGHYLTLSFEDFNLQSSPGCTKDFVEIWENHTSGRVLGRYCGNSTPSSVDTSSNVASVKFVTDGSVTASGFRLQFKSSRQVCGGDLHGPTGTFTSPNYPNPNPHARICEWTITVQEGRRIVLTFTNLRLSTQPSCNSEHLIVFNGIRSNSPLLQKLCSRVNVTNEFKSSGNTMKVVFFTDGSRPYGGFTASYTSTEDAVCGGFLPSVSGGNFSSPGYNGIRDYARNLDCEWTLSNPNRENSSISIYFLELSIESHQDCTFDVLEFRVGDADGPLIEKFCSLSAPTAPLVIPYPQVWIHFVSNERVEYTGFYIEYSFTDCGGIRTGDNGVISSPNYPNLYSAWTHCSWLLKAPEGHTITLTFSDFLLEAHPTCTSDSVTVRNGDSPGSPVIGRYCGQSVPRPIQSGSNQLIVTFNTNNQGQTRGFYATWTTNALGCGGTFHSANGTIKSPHWPQTFPENSRCSWTVITHESKHWEISFDSNFRIPSSDSQCQNSFVKVWEGRLMINKTLLATSCGDVAPSPIVTSGNIFTAVFQSEEMAAQGFSASFISRCGRTFNTSPGDIISPNFPKQYDNNMNCTYLIDADPQSLVILTFVSFHLEDRSAITGTCDHDGLHIIKGRNLSSTPLVTICGSETLRPLTVDGPVLLNFYSDAYTTDFGFKISYRAITCGGIYNESSGILRSPSYSYSNYPNNLYCVYSLHVRSSRVIIIRFNDFDVAPSNLCAHDFLEVFDGPSIGNRSLGKFCGSTRPQTVKSTNSSLTLLFKTDSSQTARGWKIFFRETIGPQQGCGGYLTEDNQSFVSPDSDSNGRYDKGLSCIWYIVAPENKLVKLTFNVFTLEGPSSAGSCVYDYVQIADGASINSYLGGKFCGSRMPAPFISSGNFLTFQFVSDVTVEMRGFNATYTFVDMPCGGTYNATSTPQNASSPHLSNIGRPYSTCTWVIAAPPQQQVQITVWDLQLPSQDCSQSYLELQDSVQTGGNRVTQFCGANYTTLPVFYSSMSTAVVVFKSGVLNRNSQVQFSYQIADCNREYNQTFGNLKSPGWPQNYDNNLDCTIILRAPQNHSISLFFYWFQLEDSRQCMNDFLEVRNGGSSTSPLLDKYCSNLLPNPVFSQSNELYLHFHSDHSVTNNGYEIIWTSSAAGCGGTLLGDEGIFTNPGFPDSYPNNTHCEWTIVAPSGRPVSVGFPFLSIDSSGGCDQNYLIVFNGPDANSPPFGPLCGINTGIAPFYASSNRVFIRFHAEYTTRLSGFEIMWSS
| null | null |
cholesterol metabolic process [GO:0008203]; cobalamin catabolic process [GO:0042366]; cobalamin metabolic process [GO:0009235]; cobalamin transport [GO:0015889]; endocytic hemoglobin import into cell [GO:0020028]; establishment of localization in cell [GO:0051649]; in utero embryonic development [GO:0001701]; lipoprotein transport [GO:0042953]; receptor-mediated endocytosis [GO:0006898]; response to bacterium [GO:0009617]; response to nutrient [GO:0007584]
|
apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; brush border [GO:0005903]; brush border membrane [GO:0031526]; clathrin-coated pit [GO:0005905]; coated vesicle [GO:0030135]; cytoplasm [GO:0005737]; endocytic vesicle [GO:0030139]; endocytic vesicle membrane [GO:0030666]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi-associated vesicle [GO:0005798]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; microvillus membrane [GO:0031528]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; receptor complex [GO:0043235]
|
calcium ion binding [GO:0005509]; cargo receptor activity [GO:0038024]; cobalamin binding [GO:0031419]; hemoglobin binding [GO:0030492]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]
|
PF00431;PF00008;PF12947;PF07645;PF12661;
|
2.10.25.10;2.60.120.290;
| null |
PTM: The precursor is cleaved by a trans-Golgi proteinase furin, removing a propeptide. {ECO:0000250|UniProtKB:O60494}.; PTM: N-glycosylated. {ECO:0000269|PubMed:29402915, ECO:0000269|PubMed:9478979}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29402915}; Peripheral membrane protein {ECO:0000305|PubMed:29402915}. Endosome membrane {ECO:0000269|PubMed:9478979}; Peripheral membrane protein {ECO:0000269|PubMed:9478979}. Lysosome membrane {ECO:0000269|PubMed:9478979}; Peripheral membrane protein {ECO:0000269|PubMed:9478979}. Note=Lacks a transmembrane domain and depends on interaction with AMN for location at the plasma membrane (By similarity). Colocalizes with AMN and LRP2 in the endocytotic apparatus of epithelial cells (PubMed:9478979). {ECO:0000250|UniProtKB:O60494, ECO:0000269|PubMed:9478979}.
| null | null | null | null | null |
FUNCTION: Endocytic receptor which plays a role in lipoprotein, vitamin and iron metabolism by facilitating their uptake. Acts together with LRP2 to mediate endocytosis of high-density lipoproteins, GC, hemoglobin, ALB, TF and SCGB1A1. Acts together with AMN to mediate endocytosis of the CBLIF-cobalamin complex. Binds to ALB, MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density lipoprotein, and the CBLIF-cobalamin complex. Ligand binding requires calcium. Serves as important transporter in several absorptive epithelia, including intestine, renal proximal tubules and embryonic yolk sac. May play an important role in the development of the peri-implantation embryo through internalization of APOA1 and cholesterol. Binds to LGALS3 at the maternal-fetal interface. {ECO:0000269|PubMed:10811843, ECO:0000269|PubMed:11805171, ECO:0000269|PubMed:12724130, ECO:0000269|PubMed:15616221, ECO:0000269|PubMed:9153271, ECO:0000269|PubMed:9478979}.
|
Rattus norvegicus (Rat)
|
O70247
|
SC5A6_RAT
|
MTVASTAAPSYTTSDTNRVISTFSVVDYVVFGLLLVLSLVIGLYHACRGWGRHTVGELLMADRKMGCLPVALSLLATFQSAVAILGGPAEIYRFGTQYWFLGCSYFLGLLIPAHIFIPVFYRLHLTSAYEYLELRFNKAVRICGTVTFIFQMVVYMGVALYAPSLALNAVTGFDLWLSVLALGIVCNIYTALGGLKAVIWTDVFQTLIMFLGQLVVIIVGAAKVGGLGHVWAVASQHGLISGIELDPDPFVRHTFWTLAFGGVFMMLSLYGVNQAQVQRYLSSHSEKAAVLSCYAVFPCQQVALCMSCLIGLVMFAYYKKYSMSPQQEQAAPDQLVLYFVMDLLKDMPGLPGLFVACLFSGSLSTISSAFNSLATVTMEDLIQPWFPQLTETRAIMLSRSLAFAYGLVCLGMAYVSSHLGSVLQAALSIFGMVGGPLLGLFCLGMFFPCANPLGAIVGLLTGLTMAFWIGIGSIVSRMSSAAASPPLNGSSSFLPSNLTVATVTTLMPSTLSKPTGLQQFYSLSYLWYSAHNSTTVIAVGLIVSLLTGGMRGRSLNPGTIYPVLPKLLALLPLSCQKRLCWRSHNQDIPVVTNLFPEKMGNGALQDSRDKERMAEDGLVHQPCSPTYIVQETSL
| null | null |
biotin import across plasma membrane [GO:1905135]; biotin metabolic process [GO:0006768]; biotin transport [GO:0015878]; iodide transmembrane transport [GO:1904200]; pantothenate transmembrane transport [GO:0015887]; sodium ion transport [GO:0006814]; transport across blood-brain barrier [GO:0150104]
|
apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; plasma membrane [GO:0005886]
|
amide transmembrane transporter activity [GO:0042887]; biotin transmembrane transporter activity [GO:0015225]; iodide transmembrane transporter activity [GO:0015111]; monocarboxylate:sodium symporter activity [GO:0140161]; pantothenate transmembrane transporter activity [GO:0015233]; pantothenate:sodium symporter activity [GO:0015498]; salt transmembrane transporter activity [GO:1901702]; sodium-dependent multivitamin transmembrane transporter activity [GO:0008523]; sulfur compound transmembrane transporter activity [GO:1901682]; vitamin transmembrane transporter activity [GO:0090482]
|
PF00474;
|
1.20.1730.10;
|
Sodium:solute symporter (SSF) (TC 2.A.21) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Y289}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q9Y289}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=biotin(out) + 2 Na(+)(out) = biotin(in) + 2 Na(+)(in); Xref=Rhea:RHEA:73375, ChEBI:CHEBI:29101, ChEBI:CHEBI:57586; Evidence={ECO:0000269|PubMed:9516450}; CATALYTIC ACTIVITY: Reaction=(R)-pantothenate(out) + 2 Na(+)(out) = (R)-pantothenate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:73371, ChEBI:CHEBI:29032, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:9516450}; CATALYTIC ACTIVITY: Reaction=(R)-lipoate(out) + 2 Na(+)(out) = (R)-lipoate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:73379, ChEBI:CHEBI:29101, ChEBI:CHEBI:83088; Evidence={ECO:0000250|UniProtKB:Q9Y289}; CATALYTIC ACTIVITY: Reaction=iodide(out) + 2 Na(+)(out) = iodide(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71207, ChEBI:CHEBI:16382, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q9Y289};
| null | null | null | null |
FUNCTION: Sodium-dependent multivitamin transporter that mediates the electrogenic transport of pantothenate, biotin, lipoate and iodide (PubMed:9516450). Functions as a Na(+)-coupled substrate symporter where the stoichiometry of Na(+):substrate is 2:1, creating an electrochemical Na(+) gradient used as driving force for substrate uptake. Required for biotin and pantothenate uptake in the intestine across the brush border membrane (By similarity). Plays a role in the maintenance of intestinal mucosa integrity, by providing the gut mucosa with biotin (By similarity). Contributes to the luminal uptake of biotin and pantothenate into the brain across the blood-brain barrier (By similarity). {ECO:0000250|UniProtKB:Q5U4D8, ECO:0000250|UniProtKB:Q9Y289, ECO:0000269|PubMed:9516450}.
|
Rattus norvegicus (Rat)
|
O70249
|
OGG1_RAT
|
MLFSSSLSSSMRHRTLTSSPALWASIPCPRSELRLDLVLASGQSFRWREQSPAHWSGVLADQVWTLTQTEDQLYCTVYRGDKGQVGRPTLEELETLHKYFQLDVSLTQLYSHWASVDSHFQSVAQKFQGVRLLRQDPTECLFSFICSSNNNIARITGMVERLCQAFGPRLVQLDDVTYHGFPNLHALAGPEVETHLRKLGLGYRARYVCASAKAILEEQGGPAWLQQLRVASYEEAHKALCTLPGVGTKVADCICLMALDKPQAVPVDIHVWQIAHRDYGWQPKTSQTKGPSPLANKELGNFFRNLWGPYAGWAQAVLFSADLRQQNLSREPPAKRKKGSKKTEG
|
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 N-glycosylase activity [GO:0019104]; enzyme binding [GO:0019899]; microtubule binding [GO:0008017]; 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.
|
Rattus norvegicus (Rat)
|
O70250
|
PGAM2_MOUSE
|
MTTHRLVMVRHGESLWNQENRFCGWFDAELSEKGAEEAKRGATAIKDAKIEFDICYTSVLKRAIRTLWTILDVTDQMWVPVVRTWRLNERHYGGLTGLNKAETAAKHGEEQVKIWRRSFDTPPPPMDEKHNYYTSISKDRRYAGLKPEELPTCESLKDTIARALPFWNEEIAPKIKAGQRVLIAAHGNSLRGIVKHLEGMSDQAIMELNLPTGIPIVYELDQNLKPTKPMRFLGDEETVRKAMEAVAAQGKAK
|
5.4.2.11; 5.4.2.4
| null |
canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; Notch signaling pathway [GO:0007219]; response to inorganic substance [GO:0010035]; response to mercury ion [GO:0046689]; spermatogenesis [GO:0007283]; striated muscle contraction [GO:0006941]
|
cytosol [GO:0005829]
|
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity [GO:0046538]; bisphosphoglycerate mutase activity [GO:0004082]; hydrolase activity [GO:0016787]; identical protein binding [GO:0042802]; phosphoglycerate mutase activity [GO:0004619]
|
PF00300;
|
3.40.50.1240;
|
Phosphoglycerate mutase family, BPG-dependent PGAM subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate; Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289; EC=5.4.2.11; Evidence={ECO:0000250|UniProtKB:P18669}; CATALYTIC ACTIVITY: Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378, ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4; Evidence={ECO:0000250|UniProtKB:P18669};
| null | null | null | null |
FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a reduced activity.
|
Mus musculus (Mouse)
|
O70252
|
HMOX2_MOUSE
|
MSSEVETSEGVDESEKNSMAPEKENHTKMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMDRNKDHPAFAPLYFPTELHRKAALIKDMKYFFGENWEEQVKCSEAAQKYVDRIHYVGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFEHVDNAQQFKQFYRARMNALDLNLKTKERIVEEANKAFEYNMQIFSELDQAGSMLARETLEDGLPVHDGKGDIRKCPFYAAQPDKGTLGGSNCPFQTTVAVLRKPSLQLILAASVALVAGLLAWYYM
|
1.14.14.18
| null |
heme catabolic process [GO:0042167]; heme oxidation [GO:0006788]; response to hypoxia [GO:0001666]; response to oxidative stress [GO:0006979]
|
endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
|
heme binding [GO:0020037]; heme oxygenase (decyclizing) activity [GO:0004392]; metal ion binding [GO:0046872]
|
PF01126;
|
1.20.910.10;
|
Heme oxygenase family
|
PTM: A soluble form arises by proteolytic removal of the membrane anchor. {ECO:0000250|UniProtKB:P30519}.; PTM: S-nitrosylated by BLVRB. {ECO:0000250|UniProtKB:P30519}.
|
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:P30519}; Single-pass type IV membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:P09601}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P09601}; Single-pass type IV membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:P09601}.
|
CATALYTIC ACTIVITY: Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29033, ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, ChEBI:CHEBI:58210, ChEBI:CHEBI:60344; EC=1.14.14.18; Evidence={ECO:0000250|UniProtKB:P30519}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21765; Evidence={ECO:0000250|UniProtKB:P30519};
| null | null | null | null |
FUNCTION: [Heme oxygenase 2]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron. {ECO:0000250|UniProtKB:P30519}.; FUNCTION: [Heme oxygenase 2 soluble form]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron. {ECO:0000250|UniProtKB:P30519}.
|
Mus musculus (Mouse)
|
O70255
|
MPZL2_MOUSE
|
MYGKSPALVLPLLLSLQLTALCPTEAVEIYTSGALEAVNGTDVRLKCTFSSFAPVGDALTVTWNFRPRDGGREQFVFYYHMDPFRPMSGRFKDRVVWDGNPERYDVSILLWKLQFDDNGTYTCQVKNPPDVDGLVGTIRLSVVHTVPFSEIYFLAVAIGSACALMIIVVIVVVLFQHFRKKRWADRADKAEGTKSKEEEKLNQGNKVSVFVEDTD
| null | null |
cell-cell adhesion [GO:0098609]; T cell differentiation in thymus [GO:0033077]
|
plasma membrane [GO:0005886]
| null |
PF07686;
|
2.60.40.10;
|
Myelin P0 protein family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Mediates homophilic cell-cell adhesion.
|
Mus musculus (Mouse)
|
O70257
|
STX7_RAT
|
MSYTPGIGGDPAQLAQRISSNIQKITQCSAEIQRTLNQLGTPQDTPELRQQLQQEQQYTNQLAKETDKYIKEFGFLPTTPSEQRQRKIQKDRLVAEFTTALTNFQKVQRQAAEREKEFVARVRASSRVSGGFPEDSSKEKNFVSWESQTQPQVQVQDEEITEDDLRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQGDVIDSIEANVESAEVHVQQANQQLSRAANYQRKSRKTLCIIILILVVGIVIIFFIVWGLKG
| null | null |
endosome to lysosome transport [GO:0008333]; intracellular protein transport [GO:0006886]; organelle assembly [GO:0070925]; organelle localization [GO:0051640]; positive regulation of receptor localization to synapse [GO:1902685]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; regulation of protein localization to plasma membrane [GO:1903076]; synaptic vesicle exocytosis [GO:0016079]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906]; vesicle-mediated transport [GO:0016192]
|
azurophil granule [GO:0042582]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endocytic vesicle [GO:0030139]; endomembrane system [GO:0012505]; endosome [GO:0005768]; immunological synapse [GO:0001772]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; SNARE complex [GO:0031201]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]; terminal bouton [GO:0043195]; tertiary granule [GO:0070820]; vesicle [GO:0031982]
|
chloride channel inhibitor activity [GO:0019869]; protein-containing complex binding [GO:0044877]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]; syntaxin binding [GO:0019905]
|
PF05739;PF14523;
|
1.20.5.110;1.20.58.70;
|
Syntaxin family
| null |
SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O70258
|
SGCE_MOUSE
|
MLLFWWWELGDPCAWTGKGRGTLKMSPATTGTFLLTVYTLFSKVHSDRNVYPSAGVLFVHVLEREYFKGEFPPYPKPGEVSNDPITFNTNLMGYPDRPGWLRYIQRTPYSDGVLYGSPTAENVGKPTIIEITAYNRRTFETARHNLIINIMSAEEFPLPYQAEFFIKNMNVEEMLASEVLGDFLGAVKNVWQPERLNAINITSALDRGGRVPLPINDMKEGVYVMVGADVAFSSCLREVENPQNQLRCSQEMEPVITCDKKFRTHFHIDWCKISLVDKTKQVSTYQEVVRGEGILPDGGEYKPPSDSLKSRDYYTDFLVTLAVPSAVALVLFLILAYIMCCRREGVEKRDMQTPDIQLVHHSSIQKSTKELRDMSKNREIAWPLSTLPVFHPVTGEVIPPTHTDNYDSTNMPLMQAQQNLPHQTQIPQPQTTGKWYP
| null | null | null |
cytoskeleton [GO:0005856]; dendrite membrane [GO:0032590]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; sarcoglycan complex [GO:0016012]; sarcolemma [GO:0042383]
| null |
PF05510;PF20989;
| null |
Sarcoglycan alpha/epsilon family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:17200151}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. {ECO:0000269|PubMed:17200151}.
|
SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000269|PubMed:17200151}; Single-pass membrane protein {ECO:0000269|PubMed:17200151}. Golgi apparatus {ECO:0000269|PubMed:17200151}. Cell projection, dendrite {ECO:0000269|PubMed:17200151}. Cytoplasm, cytoskeleton {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
|
Mus musculus (Mouse)
|
O70260
|
PIAS3_RAT
|
MAELGELKHMVMSFRVSELQVLLGFAGRNKSGRKHELLAKALHLLKSSCAPSVQMKIKELYRRRFPRKTLGPSDLSLLSLPPGTSPVGSPSPLASIPPTLLTPGTLLGPKREVDMHPPLPQPVHPDVTMKPLPFYEVYGELIRPTTLASTSSQRFEEAHFTFALTPQQLQQILTSREVLPGAKCDYTIQVQLRFCLCETSCPQEDYFPPNLFVKVNGKLCPLPGYLPPTKNGAEPKRPSRPINITPLARLSATVPNTIVVNWSSEFGRNYSLSVYLVRQLTAGTLLQKLRAKGIRNPDHSRALIKEKLTADPDSEVATTSLRVSLMCPLGKMRLTVPCRALTCAHLQSFDAALYLQMNEKKPTWTCPVCDKKAPYESLIIDGLFMEILNSCSDCDEIQFMEDGSWCPMKPKKEASEVCPPPGYGLDGLQYSPVQEGNQSENKKRVEVIDLTIESSSDEEDLPPTKKHCPVTSAAIPALPGSKGALTSGHQPSSVLRSPAMGTLGSDFLSSLPLHEYPPAFPLGADIQGLDLFSFLQTESQHYSPSVITSLDEQDTLGHFFQFRGTPPHFLGPLAPTLGSSHRSATPAPAPGRVSSIVAPGSSLREGHGGPLPSGPSLTGCRSDVISLD
|
2.3.2.-
| null |
negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of protein sumoylation [GO:0033234]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of gene expression [GO:0010628]; positive regulation of membrane potential [GO:0045838]; positive regulation of protein sumoylation [GO:0033235]; protein sumoylation [GO:0016925]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of tumor necrosis factor-mediated signaling pathway [GO:0010803]; response to hormone [GO:0009725]
|
cytoplasm [GO:0005737]; dendrite [GO:0030425]; nuclear speck [GO:0016607]; nucleus [GO:0005634]
|
ionotropic glutamate receptor binding [GO:0035255]; NF-kappaB binding [GO:0051059]; potassium channel regulator activity [GO:0015459]; SUMO ligase activity [GO:0061665]; SUMO transferase activity [GO:0019789]; transcription coregulator activity [GO:0003712]; transmembrane transporter binding [GO:0044325]; zinc ion binding [GO:0008270]
|
PF14324;PF02891;
|
2.60.120.780;1.10.720.30;3.30.40.10;
|
PIAS family
|
PTM: Sumoylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O54714}. Nucleus {ECO:0000269|PubMed:9565597}. Nucleus speckle {ECO:0000250|UniProtKB:O54714}. Note=Colocalizes with MITF in the nucleus. Colocalizes with GFI1 in nuclear dots. Colocalizes with SUMO1 in nuclear granules. {ECO:0000250|UniProtKB:O54714}.
| null | null |
PATHWAY: Protein modification; protein sumoylation.
| null | null |
FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Sumoylates CCAR2 which promotes its interaction with SIRT1. Diminishes the sumoylation of ZFHX3 by preventing the colocalization of ZFHX3 with SUMO1 in the nucleus (By similarity). {ECO:0000250|UniProtKB:O54714, ECO:0000250|UniProtKB:Q9Y6X2}.
|
Rattus norvegicus (Rat)
|
O70263
|
LNX1_MOUSE
|
MNQPDLADDPDPSPEPLCIVCGQNHSPEENHFYTYTEDVDDDLICHICLQALLDPLDTPCGHTYCTLCLTNFLVEKDFCPVDRKPVVLQHCKKSSILVNKLLNKLLVTCPFTEHCTEVLQRCDLQHHFQTSCKGASHYGLTKDRKRRSQDGCPDGCASLMATTLSPEVSAAATISLMTDEPGLDNPAYVSSVEDGEPVANSSDSGRSNRTRARPFERSTMRSRSFKKINRALSALRRTKSGSVVANHVDQGRDNSENTTVPEVFPRLFHLIPDGEITSIKINRADPSESLSIRLVGGSETPLVHIIIQHIYRDGVIARDGRLLPGDIILKVNGMDISNVPHNYAVRLLRQPCQVLRLTVLREQKFRSRSNAHVPDSYGPRDDSFHVILNKSSPEEQLGIKLVRRVDEPGVFIFNVLNGGVADRHGQLEENDRVLAINGHDLRFGSPESAAHLIQASERRVHLVVSRQVRQSSPDIFQEAGWISNGQQSPGPGERNTASKPAATCHEKVVSVWKDPSESLGMTVGGGASHREWDLPIYVISVEPGGVISRDGRIKTGDILLNVNGIELTEVSRTEAVAILKSAPSSVVLKALEVKEQEAQEDCSPAALDSNHNVTPPGDWSPSWVMWLELPQYLCNCKDVILRRNTAGSLGFCIVGGYEEYSGNKPFFIKSIVEGTPAYNDGRIRCGDILLAVNGRSTSGMIHACLARMLKELKGRITLTIASWPGTFL
|
2.3.2.27
| null |
protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cytoplasm [GO:0005737]
|
identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; PDZ domain binding [GO:0030165]; ubiquitin-protein transferase activity [GO:0004842]
|
PF00595;PF13920;
|
2.30.42.10;3.30.40.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm.
|
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;
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NUMB. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of isoform p66 and isoform p72 of NUMB, but not that of isoform p71 or isoform p65. {ECO:0000269|PubMed:11782429, ECO:0000269|PubMed:14990566, ECO:0000269|PubMed:9535908}.; FUNCTION: Isoform 2 provides an endocytic scaffold for IGSF5/JAM4. {ECO:0000269|PubMed:9535908}.
|
Mus musculus (Mouse)
|
O70274
|
TP4A2_MOUSE
|
MNRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDDWLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFRDTNGHCCVQ
|
3.1.3.48
| null |
dephosphorylation [GO:0016311]
|
cytoplasm [GO:0005737]; early endosome [GO:0005769]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
protein tyrosine phosphatase activity [GO:0004725]
|
PF00102;
|
3.90.190.10;
|
Protein-tyrosine phosphatase family
|
PTM: Farnesylated. Farnesylation is required for membrane targeting and for interaction with RABGGTB (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10747914}. Early endosome {ECO:0000269|PubMed:10747914}. Cytoplasm {ECO:0000269|PubMed:10747914}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48;
| null | null | null | null |
FUNCTION: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O70276
|
RPE65_RAT
|
MSIQIEHPAGGYKKLFETVEELSTPLTAHVTGRIPLWLTGSLLRCGPGLFEVGSEPFYHLFDGQALLHKFDFKEGHVTYYRRFIRTDAYVRAMTEKRIVITEFGTCAFPDPCKNIFSRFFSYFRGVEITDNALVNIYPVGEDYYACTETNFITKINPETLETIKQVDLCNYVSVNGATAHPHIESDGTVYNIGNCFGKNFTVAYNIIKIPPLKADKEDPINKSEVVVQFPCSDRFKPSYVHSFGLTPNYIVFVETPVKINLFKFLSSWSLWGANYMDCFESNESMGVWLHVADKKRRKYFNNKYRTSPFNLFHHINTYEDNGFLIVDLCCWKGFEFVYNYLYLANLRENWEEVKRNAMKAPQPEVRRYVLPLTIDKADTGRNLVTLPHTTATAILCSDETIWLEPEVLFSGPRQAFEFPQINYQKCGGKPYTYAYGLGLNHFVPDKLCKLNVKTKEIWMWQEPDSYPSEPIFVSQPDALEEDDGVVLSVVVSPGAGQKPAYLLVLNAKDLSEIARAEVETNIPVTFHGLFKKP
|
3.1.1.64; 5.3.3.22
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q28175}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q28175};
|
camera-type eye development [GO:0043010]; circadian rhythm [GO:0007623]; detection of light stimulus involved in visual perception [GO:0050908]; neural retina development [GO:0003407]; response to light stimulus [GO:0009416]; retina homeostasis [GO:0001895]; retinal metabolic process [GO:0042574]; retinoid metabolic process [GO:0001523]; retinol metabolic process [GO:0042572]; zeaxanthin biosynthetic process [GO:1901827]
|
cell body [GO:0044297]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity [GO:0052885]; all-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity [GO:0052884]; beta-carotene 15,15'-dioxygenase activity [GO:0003834]; cardiolipin binding [GO:1901612]; isomerase activity [GO:0016853]; metal ion binding [GO:0046872]; phosphatidylcholine binding [GO:0031210]; phosphatidylserine binding [GO:0001786]; retinol isomerase activity [GO:0050251]
|
PF03055;
| null |
Carotenoid oxygenase family
|
PTM: Palmitoylation by LRAT regulates ligand binding specificity; the palmitoylated form (membrane form) specifically binds all-trans-retinyl-palmitate, while the soluble unpalmitoylated form binds all-trans-retinol (vitamin A). {ECO:0000250|UniProtKB:Q28175}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A9C3R9}. Cell membrane {ECO:0000250|UniProtKB:Q28175}; Lipid-anchor {ECO:0000250|UniProtKB:Q28175}. Microsome membrane {ECO:0000250|UniProtKB:Q28175}. Note=Attached to the membrane by a lipid anchor when palmitoylated (membrane form), soluble when unpalmitoylated. Undergoes light-dependent intracellular transport to become more concentrated in the central region of the retina pigment epithelium cells (By similarity). {ECO:0000250|UniProtKB:Q16518, ECO:0000250|UniProtKB:Q28175}.
|
CATALYTIC ACTIVITY: Reaction=an all-trans-retinyl ester + H2O = 11-cis-retinol + a fatty acid + H(+); Xref=Rhea:RHEA:31771, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16302, ChEBI:CHEBI:28868, ChEBI:CHEBI:63410; EC=3.1.1.64; Evidence={ECO:0000250|UniProtKB:Q28175}; CATALYTIC ACTIVITY: Reaction=lutein = (3R,3'S)-zeaxanthin; Xref=Rhea:RHEA:12729, ChEBI:CHEBI:28838, ChEBI:CHEBI:138919; EC=5.3.3.22; Evidence={ECO:0000250|UniProtKB:Q16518}; CATALYTIC ACTIVITY: Reaction=all-trans-retinyl hexadecanoate + H2O = 11-cis-retinol + H(+) + hexadecanoate; Xref=Rhea:RHEA:31775, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16302, ChEBI:CHEBI:17616; EC=3.1.1.64; Evidence={ECO:0000250|UniProtKB:Q16518};
| null | null | null | null |
FUNCTION: Critical isomerohydrolase in the retinoid cycle involved in regeneration of 11-cis-retinal, the chromophore of rod and cone opsins. Catalyzes the cleavage and isomerization of all-trans-retinyl fatty acid esters to 11-cis-retinol which is further oxidized by 11-cis retinol dehydrogenase to 11-cis-retinal for use as visual chromophore. Essential for the production of 11-cis retinal for both rod and cone photoreceptors. Also capable of catalyzing the isomerization of lutein to meso-zeaxanthin an eye-specific carotenoid. The soluble form binds vitamin A (all-trans-retinol), making it available for LRAT processing to all-trans-retinyl ester. The membrane form, palmitoylated by LRAT, binds all-trans-retinyl esters, making them available for IMH (isomerohydrolase) processing to all-cis-retinol. The soluble form is regenerated by transferring its palmitoyl groups onto 11-cis-retinol, a reaction catalyzed by LRAT. {ECO:0000250|UniProtKB:Q16518, ECO:0000250|UniProtKB:Q28175}.
|
Rattus norvegicus (Rat)
|
O70277
|
TRIM3_RAT
|
MAKREDSPGPEVQPMDKQFLVCSICLDRYRCPKVLPCLHTFCERCLQNYIPPQSLTLSCPVCRQTSILPEQGVSALQNNFFISSLMEAMQQAPDGAHDPEDPHPLSAVAGRPLSCPNHEGKTMEFYCEACETAMCGECRAGEHREHGTVLLRDVVEQHKAALQRQLEAVRGRLPQLSAAIALVGGISQQLQERKAEALAQISAAFEDLEQALQQRKQALVSDLESICGAKQKVLQTQLDTLRQGQEHIGSSCSFAEQALRLGSAPEVLLVRKHMRERLAALAAQAFPERPHENAQLELVLEVDGLRRSVLNLGALLTTSAAAHETVATGEGLRQALVGQPASLTVTTKDKDGRLVRTGSAELCAEITGPDGMRLAVPVVDHKNGTYELVYTARTEGDLLLSVLLYGQPVRGSPFRVRALRPGDLPPSPDDVKRRVKSPGGPGSHVRQKAVRRPSSMYSTGGKRKDNPIVDELVFRVGSRGREKGEFTNLHPLSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTKIGAGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSAEPLYGPQGLALTSDGHVVVADAGNHCFKAYRYLQ
|
2.3.2.27
| null |
negative regulation of translation [GO:0017148]; positive regulation of toll-like receptor 3 signaling pathway [GO:0034141]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K63-linked ubiquitination [GO:0070534]; protein polyubiquitination [GO:0000209]; protein transport [GO:0015031]; protein ubiquitination [GO:0016567]; regulation protein catabolic process at postsynapse [GO:0140252]
|
cytoplasm [GO:0005737]; dendrite [GO:0030425]; early endosome [GO:0005769]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; postsynapse [GO:0098794]
|
identical protein binding [GO:0042802]; translation repressor activity [GO:0030371]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]
|
PF00630;PF01436;PF00643;PF00097;
|
3.30.160.60;2.60.40.10;2.120.10.30;3.30.40.10;
|
TRIM/RBCC family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75382}. Early endosome {ECO:0000250|UniProtKB:O75382}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9R1R2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9R1R2}. Note=Mainly located in the Golgi apparatus and transported to the early endosomes upon stimulation with dsRNA. {ECO:0000250|UniProtKB:O75382}.
|
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:20352094};
| null | null | null | null |
FUNCTION: E3 ubiquitin ligase that plays essential roles in neuronal functions such as regulation of neuronal plasticity, learning, and memory (PubMed:20352094). In addition to its neuronal functions, participates in other biological processes such as innate immunity or cell cycle regulation. Component of the cytoskeleton-associated recycling or transport complex in neurons, polyubiquitinates gamma-actin, thus regulating neuronal plasticity, learning, and memory (By similarity). Ubiquitinates postsynaptic scaffold GKAP, a neuronal substrate involved in synaptic remodeling and thereby modulates dendritic spine morphology (PubMed:20352094). Positively regulates motility of microtubule-dependent motor protein KIF21B (By similarity). Induces growth arrest via its RING-dependent E3 ligase activity and ubiquinates CDKN1A. Positively regulates TLR3-mediated signaling by mediating 'Lys-63'-linked polyubiquitination of TLR3. In turn, promotes the recognition and sorting of polyubiquitinated TLR3 by the ESCRT complexes (By similarity). {ECO:0000250|UniProtKB:O75382, ECO:0000250|UniProtKB:Q9R1R2, ECO:0000269|PubMed:20352094}.
|
Rattus norvegicus (Rat)
|
O70281
|
TPST1_MOUSE
|
MVGKLKQNLLLACLVISSVTVFYLGQHAMECHHRIEERSQPARLENPKATVRAGLDIKANKTFTYHKDMPLIFIGGVPRSGTTLMRAMLDAHPDIRCGEETRVIPRILALKQMWSRSSKEKIRLDEAGVTDEVLDSAMQAFLLEVIVKHGEPAPYLCNKDPFALKSLTYLARLFPNAKFLLMVRDGRASVHSMISRKVTIAGFDLNSYRDCLTKWNRAIETMYNQCMEVGYKKCMLVHYEQLVLHPERWMRTLLKFLHIPWNHSVLHHEEMIGKAGGVSLSKVERSTDQVIKPVNVGALSKWVGKIPPDVLQDMAVIAPMLAKLGYDPYANPPNYGKPDPKILENTRRVYKGEFQLPDFLKEKPQTEQVE
|
2.8.2.20
| null |
post-translational protein modification [GO:0043687]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
protein homodimerization activity [GO:0042803]; protein-tyrosine sulfotransferase activity [GO:0008476]
|
PF13469;
|
3.40.50.300;
|
Protein sulfotransferase family
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:O60507}.
|
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O60507}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O60507}.
|
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein]; Xref=Rhea:RHEA:16801, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:11688, ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:65286; EC=2.8.2.20; Evidence={ECO:0000269|PubMed:9501187};
| null | null | null | null |
FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate. {ECO:0000269|PubMed:9501187}.
|
Mus musculus (Mouse)
|
O70283
|
WNT2B_MOUSE
|
MLKLQGEDEAAQLAPRRARVPVPRPTAPDVSPSSARLGLACLLLLLLLTLPARVDTSWWYIGALGARVICDNIPGLVSRQRQLCQRYPDIMRSVGEGAREWIRECQHQFRHHRWNCTTLDRDHTVFGRAMLRSSREAAFVYAISSAGVVHAITRACSQGELSVCSCDPYTRGRHHDQRGDFDWGGCSDNIHYGVRFAKAFVDAKEKRLKDARALMNLHNNRCGRTAVRRFLKLECKCHGVSGSCTLRTCWRALSDFRRTGDYLRRRYDGAVQVTATQDGANFTAARQGYRHATRTDLVYFDNSPDYCVLDKAAGSLGTAGRVCSKTSKGTDGCEIMCCGRGYDTTRVTRVTQCECKFHWCCAVRCKECRNTVDVHTCKAPKKAEWLDQT
| null | null |
animal organ morphogenesis [GO:0009887]; canonical Wnt signaling pathway [GO:0060070]; cell fate commitment [GO:0045165]; cell-cell signaling [GO:0007267]; cellular response to starvation [GO:0009267]; chondrocyte differentiation [GO:0002062]; forebrain regionalization [GO:0021871]; hematopoietic stem cell proliferation [GO:0071425]; lung induction [GO:0060492]; male gonad development [GO:0008584]; mesenchymal-epithelial cell signaling [GO:0060638]; neuron differentiation [GO:0030182]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; signal transduction [GO:0007165]
|
extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]
|
cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; signaling receptor binding [GO:0005102]
|
PF00110;
|
3.30.2460.20;
|
Wnt family
|
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q93097}. Secreted {ECO:0000250|UniProtKB:Q93097}.
| null | null | null | null | null |
FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt/beta-catenin signaling pathway (PubMed:19686689). Plays a redundant role in embryonic lung development (PubMed:19686689). {ECO:0000269|PubMed:19686689, ECO:0000305}.
|
Mus musculus (Mouse)
|
O70291
|
GRK4_MOUSE
|
MELENFVANNLLLKARLGFNKQTGRSKKWRELLKFPPVSMCTELRWSIEKDFSSLCDKQPIGRLLFRQFCDTKPDLKRCIEFLDAVAEYEVTIEEEQREFGLAIFSRFFKEKSEVPLPEIPPDIVKECKWNLKQNSPSQNVFEECAGIVCKYLSETPFEEYQESTYFNRFLQWKWLERRPVTKNTFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKLHSRFVVSLAYTYETKDALCLVLTIMNGGDLKYHIYNLGDPGFEEPRAVFYAAELCCGLEDLQRKRIVYRDLKPENILLDDHGHIRISDLGLAMEVPEGEMVRGRVGTVGYMAPEIINHEKYTFSPDWWGLGCLIYEMIAGHSPFRKYKEKVNREELERRVKNETEEYSERFSEDAKSICSMLLIKDPSKRLGCQRDGVSAVKQHPIFKDINFSRLEANMLDPPFIPDPQAIYCRNILDIGQFSVVKGVNLDTNDEIFYAEFATGSVTIPWQNEMIESGCFKDLNENEDDLSSLEKYKMCSSILRPKRNFFRRLFRRTGCLNIALSEEREPTEH
|
2.7.11.16
| null |
desensitization of G protein-coupled receptor signaling pathway [GO:0002029]; G protein-coupled receptor internalization [GO:0002031]; phosphorylation [GO:0016310]; regulation of signal transduction [GO:0009966]; signal transduction [GO:0007165]
|
cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; rhodopsin kinase activity [GO:0050254]
|
PF00069;PF00615;
|
1.10.167.10;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, GPRK subfamily
|
PTM: Palmitoylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cell cortex {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=[G-protein-coupled receptor] + ATP = [G-protein-coupled receptor]-phosphate + ADP + H(+); Xref=Rhea:RHEA:12008, Rhea:RHEA-COMP:11260, Rhea:RHEA-COMP:11261, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.16;
| null | null | null | null |
FUNCTION: Specifically phosphorylates the activated forms of G protein-coupled receptors.
|
Mus musculus (Mouse)
|
O70293
|
GRK6_MOUSE
|
MELENIVANTVLLKAREGGGGNRKGKSKKWRQMLQFPHISQCEELRLSLERDYHSLCERQPIGRLLFREFCATRPELTRCTAFLDGVSEYEVTPDEKRKACGRRLMQNFLSHTGPDLIPEVPRQLVSNCAQRLEQGPCKDLFQELTRLTHEYLSTAPFADYLDSIYFNRFLQWKWLERQPVTKNTFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGRVGTVGYMAPEVVRNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVAEEYTDRFSSQARSLCSQLLSKDPAERLGCRGGGAREVKEHPLFKKLNFKRLGAGMLEPPFKPDPQAIYCKDVLDIEQFSTVKGVDLEPTDQDFYQKFATGSVSIPWQNEMVETECFQELNVFGLDGSVPPDLDWKGQPTAPPKKGLLQRLFSRQDCCGNCSDSEEELPTRL
|
2.7.11.16
| null |
desensitization of G protein-coupled receptor signaling pathway [GO:0002029]; phosphorylation [GO:0016310]; regulation of signal transduction [GO:0009966]; Wnt signaling pathway [GO:0016055]
|
cytoplasm [GO:0005737]; membrane [GO:0016020]
|
ATP binding [GO:0005524]; beta-adrenergic receptor kinase activity [GO:0047696]; G protein-coupled receptor kinase activity [GO:0004703]
|
PF00069;PF00615;
|
6.10.250.2260;1.10.167.10;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, GPRK subfamily
| null |
SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
|
CATALYTIC ACTIVITY: Reaction=[G-protein-coupled receptor] + ATP = [G-protein-coupled receptor]-phosphate + ADP + H(+); Xref=Rhea:RHEA:12008, Rhea:RHEA-COMP:11260, Rhea:RHEA-COMP:11261, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.16;
| null | null | null | null |
FUNCTION: Specifically phosphorylates the activated forms of G protein-coupled receptors. Such receptor phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events leading to their desensitization. Seems to be involved in the desensitization of D2-like dopamine receptors in striatum and chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis (By similarity). Phosphorylates rhodopsin (RHO) (in vitro) and a non G-protein-coupled receptor, LRP6 during Wnt signaling (in vitro) (By similarity). {ECO:0000250, ECO:0000269|PubMed:12032308, ECO:0000269|PubMed:12718862, ECO:0000269|PubMed:14634128}.
|
Mus musculus (Mouse)
|
O70299
|
MB211_MOUSE
|
MIAAQAKLVYHLNKYYNEKCQARKAAIAKTIREVCKVVSDVLKEVEVQEPRFISSLNEMDNRYEGLEVISPTEFEVVLYLNQMGVFNFVDDGSLPGCAVLKLSDGRKRSMSLWVEFITASGYLSARKIRSRFQTLVAQAVDKCSYRDVVKMVADTSEVKLRIRDRYVVQITPAFKCTGIWPRSAAHWPLPHIPWPGPNRVAEVKAEGFNLLSKECHSLAGKQSSAESDAWVLQFAEAENRLQMGGCRKKCLSILKTLRDRHLELPGQPLNNYHMKTLVSYECEKHPRESDWDESCLGDRLNGILLQLISCLQCRRCPHYFLPNLDLFQGKPHSALENAAKQTWRLAREILTNPKSLEKL
|
2.7.7.-
| null |
camera-type eye development [GO:0043010]; cell population proliferation [GO:0008283]; eye development [GO:0001654]; positive regulation of cell population proliferation [GO:0008284]
|
nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; nucleotidyltransferase activity [GO:0016779]
|
PF03281;PF20266;
|
1.10.1410.40;3.30.460.90;
|
Mab-21 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10556287}.
| null | null | null | null | null |
FUNCTION: Putative nucleotidyltransferase required for several aspects of embryonic development including normal development of the eye, notochord, neural tube and other organ tissues, and for embryonic turning (PubMed:11857508, PubMed:12642482). It is unclear whether it displays nucleotidyltransferase activity in vivo (By similarity). Binds single-stranded RNA (ssRNA) (By similarity). {ECO:0000250|UniProtKB:Q13394, ECO:0000269|PubMed:11857508, ECO:0000269|PubMed:12642482}.
|
Mus musculus (Mouse)
|
O70302
|
CIDEA_MOUSE
|
METARDYAGALIRPLTFMGLQTKKVLLTPLIHPARPFRVSNHDRSSRRGVMASSLQELISKTLDVLVITTGLVTLVLEEDGTVVDTEEFFQTLRDNTHFMILEKGQKWTPGSKYVPVCKQPKKSGIARVTFDLYRLNPKDFLGCLNVKATMYEMYSVSYDIRCTSFKAVLRNLLRFMSYAAQMTGQFLVYAGTYMLRVLGDTEEQPSPKPSTKGWFM
| null | null |
apoptotic process [GO:0006915]; cellular response to cold [GO:0070417]; lipid droplet fusion [GO:0160077]; lipid metabolic process [GO:0006629]; lipid storage [GO:0019915]; negative regulation of cold-induced thermogenesis [GO:0120163]; negative regulation of execution phase of apoptosis [GO:1900118]; negative regulation of lipid catabolic process [GO:0050995]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; negative regulation of tumor necrosis factor production [GO:0032720]; positive regulation of sequestering of triglyceride [GO:0010890]; regulation of apoptotic DNA fragmentation [GO:1902510]; regulation of apoptotic process [GO:0042981]; response to stilbenoid [GO:0035634]; temperature homeostasis [GO:0001659]
|
cytoplasm [GO:0005737]; lipid droplet [GO:0005811]; mitochondrial envelope [GO:0005740]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
lipid transfer activity [GO:0120013]; phosphatidic acid binding [GO:0070300]; protein homodimerization activity [GO:0042803]
|
PF02017;
|
3.10.20.10;
|
CIDE family
| null |
SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:18509062, ECO:0000269|PubMed:20810722, ECO:0000269|PubMed:22144693, ECO:0000269|PubMed:26609809}. Nucleus {ECO:0000269|PubMed:22245780}. Note=Enriched at lipid droplet contact sites (PubMed:18509062, PubMed:22144693). Using a GFP-tagged construct, has been shown to localize to mitochondria, where it could interact with UCP1 and hence inhibit UCP1 uncoupling activity (PubMed:12910269). These data could not be confirmed (PubMed:18509062, PubMed:22245780). {ECO:0000269|PubMed:12910269, ECO:0000269|PubMed:18509062, ECO:0000269|PubMed:22144693, ECO:0000269|PubMed:22245780}.
|
CATALYTIC ACTIVITY: Reaction=a triacyl-sn-glycerol(in) = a triacyl-sn-glycerol(out); Xref=Rhea:RHEA:39011, ChEBI:CHEBI:64615; Evidence={ECO:0000305|PubMed:26609809};
| null | null | null | null |
FUNCTION: Lipid transferase that promotes unilocular lipid droplet formation by mediating lipid droplet fusion (PubMed:18509062, PubMed:22144693, PubMed:26609809, PubMed:36477540). Lipid droplet fusion promotes their enlargement, restricting lipolysis and favoring lipid storage (PubMed:18509062, PubMed:22144693, PubMed:26609809). Localizes on the lipid droplet surface, at focal contact sites between lipid droplets, and mediates atypical lipid droplet fusion by promoting directional net neutral lipid transfer from the smaller to larger lipid droplets (PubMed:18509062, PubMed:22144693, PubMed:26609809). The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair and occurs at a lower rate than that promoted by CIDEC (PubMed:18509062, PubMed:22144693). May also act as a CEBPB coactivator in epithelial cells to control the expression of a subset of CEBPB downstream target genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH, but not casein (PubMed:22245780). By interacting with CEBPB, strengthens the association of CEBPB with the XDH promoter, increases histone acetylation and dissociates HDAC1 from the promoter (PubMed:22245780). When overexpressed, induces apoptosis; the physiological significance of its role in apoptosis is unclear (PubMed:9564035). {ECO:0000269|PubMed:18509062, ECO:0000269|PubMed:22144693, ECO:0000269|PubMed:22245780, ECO:0000269|PubMed:26609809, ECO:0000269|PubMed:36477540, ECO:0000269|PubMed:9564035}.
|
Mus musculus (Mouse)
|
O70303
|
CIDEB_MOUSE
|
MEYLSAFNPNGLLRSVSTVSSELSRRVWNSAPPPQRPFRVCDHKRTVRKGLTAASLQELLDKVLETLLLRGVLTLVLEEDGTAVDSEDFFQLLEDDTCLMVLEQGQSWSPKSGMLSYGLGREKPKHSKDIARITFDVYKQNPRDLFGSLNVKATFYGLYSMSCDFQGVGPKRVLRELLRWTSSLLQGLGHMLLGISSTLRHVVEGADRWQWHGQRHLHS
| null | null |
apoptotic process [GO:0006915]; COPII-coated vesicle cargo loading [GO:0090110]; execution phase of apoptosis [GO:0097194]; lipid droplet fusion [GO:0160077]; lipid storage [GO:0019915]; positive regulation of apoptotic process [GO:0043065]; regulation of apoptotic process [GO:0042981]; regulation of triglyceride metabolic process [GO:0090207]; very-low-density lipoprotein particle assembly [GO:0034379]
|
COPI-coated vesicle [GO:0030137]; COPII vesicle coat [GO:0030127]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; lipid droplet [GO:0005811]; perinuclear region of cytoplasm [GO:0048471]
|
identical protein binding [GO:0042802]; lipid transfer activity [GO:0120013]; molecular adaptor activity [GO:0060090]; phosphatidic acid binding [GO:0070300]
|
PF02017;
|
3.10.20.10;
|
CIDE family
| null |
SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:19187774, ECO:0000269|PubMed:26733203}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19187774, ECO:0000269|PubMed:23297397}; Peripheral membrane protein {ECO:0000269|PubMed:19187774}; Cytoplasmic side {ECO:0000269|PubMed:19187774}. Golgi apparatus {ECO:0000269|PubMed:23297397}. Cytoplasmic vesicle, COPI-coated vesicle {ECO:0000269|PubMed:23297397, ECO:0000269|PubMed:30858281}. Note=Enriched at lipid droplet contact sites. {ECO:0000269|PubMed:26733203}.
| null | null | null | null | null |
FUNCTION: Lipid transferase specifically expressed in hepatocytes, which promotes unilocular lipid droplet formation by mediating lipid droplet fusion (PubMed:26733203). Lipid droplet fusion promotes their enlargement, restricting lipolysis and favoring lipid storage (PubMed:26733203). Localizes on the lipid droplet surface, at focal contact sites between lipid droplets, and mediates atypical lipid droplet fusion by promoting directional net neutral lipid transfer from the smaller to larger lipid droplets (By similarity). The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair (By similarity). Promotes lipid exchange and lipid droplet fusion in both small and large lipid droplet-containing hepatocytes (PubMed:26733203). In addition to its role in lipid droplet fusion, also involved in cytoplasmic vesicle biogenesis and transport (PubMed:19187774, PubMed:23297397, PubMed:30858281). Required for very-low-density lipoprotein (VLDL) lipidation and maturation (PubMed:19187774, PubMed:23297397). Probably involved in the biogenesis of VLDL transport vesicles by forming a COPII vesicle coat and facilitating the formation of endoplasmic reticulum-derived large vesicles (PubMed:23297397). Also involved in sterol-regulated export of the SCAP-SREBP complex, composed of SCAP, SREBF1/SREBP1 and SREBF2/SREBP2, by promoting loading of SCAP-SREBP into COPII vesicles (PubMed:30858281). May also activate apoptosis (PubMed:9564035). {ECO:0000250|UniProtKB:P56198, ECO:0000269|PubMed:19187774, ECO:0000269|PubMed:23297397, ECO:0000269|PubMed:26733203, ECO:0000269|PubMed:30858281, ECO:0000269|PubMed:9564035}.
|
Mus musculus (Mouse)
|
O70305
|
ATX2_MOUSE
|
MRSSTAAVQRPAAGDPEPRRPAGWAARRSLPRTARRGGRGGAVAYPSAGPPPRGPGAPPRGPRSPPCASDCFGSNGHGASRPGSRRLLGVCGPPRPFVVVLLALAPAATPARACPPGVRASPPRSGVSSSARPAPGCPRPACEPVYGPLTMSLKPQPQPPAPATGRKPGGGLLSSPGAAPASAAVTSASVVPAPAAPVASSSAAAGGGRPGLGRGRNSSKGLPQPTISFDGIYANVRMVHILTSVVGSKCEVQVKNGGIYEGVFKTYSPKCDLVLDAAHEKSTESSSGPKREEIMESVLFKCSDFVVVQFKDTDSSYARRDAFTDSALSAKVNGEHKEKDLEPWDAGELTASEELELENDVSNGWDPNDMFRYNEENYGVVSTYDSSLSSYTVPLERDNSEEFLKREARANQLAEEIESSAQYKARVALENDDRSEEEKYTAVQRNCSDREGHGPNTRDNKYIPPGQRNREVLSWGSGRQSSPRMGQPGPGSMPSRAASHTSDFNPNAGSDQRVVNGGVPWPSPCPSHSSRPPSRYQSGPNSLPPRAATHTRPPSRPPSRPSRPPSHPSAHGSPAPVSTMPKRMSSEGPPRMSPKAQRHPRNHRVSAGRGSMSSGLEFVSHNPPSEAAAPPVARTSPAGGTWSSVVSGVPRLSPKTHRPRSPRQSSIGNSPSGPVLASPQAGIIPAEAVSMPVPAASPTPASPASNRALTPSIEAKDSRLQDQRQNSPAGSKENVKASETSPSFSKADNKGMSPVVSEHRKQIDDLKKFKNDFRLQPSSTSESMDQLLSKNREGEKSRDLIKDKTEASAKDSFIDSSSSSSNCTSGSSKTNSPSISPSMLSNAEHKRGPEVTSQGVQTSSPACKQEKDDREEKKDTTEQVRKSTLNPNAKEFNPRSFSQPKPSTTPTSPRPQAQPSPSMVGHQQPAPVYTQPVCFAPNMMYPVPVSPGVQPLYPIPMTPMPVNQAKTYRAGKVPNMPQQRQDQHHQSTMMHPASAAGPPIVATPPAYSTQYVAYSPQQFPNQPLVQHVPHYQSQHPHVYSPVIQGNARMMAPPAHAQPGLVSSSAAQFGAHEQTHAMYACPKLPYNKETSPSFYFAISTGSLAQQYAHPNAALHPHTPHPQPSATPTGQQQSQHGGSHPAPSPVQHHQHQAAQALHLASPQQQSAIYHAGLAPTPPSMTPASNTQSPQSSFPAAQQTVFTIHPSHVQPAYTTPPHMAHVPQAHVQSGMVPSHPTAHAPMMLMTTQPPGPKAALAQSALQPIPVSTTAHFPYMTHPSVQAHHQQQL
| null | null |
cerebellar Purkinje cell differentiation [GO:0021702]; homeostasis of number of cells [GO:0048872]; negative regulation of multicellular organism growth [GO:0040015]; neuromuscular process [GO:0050905]; neuron projection morphogenesis [GO:0048812]; stress granule assembly [GO:0034063]
|
cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; perinuclear region of cytoplasm [GO:0048471]
|
mRNA binding [GO:0003729]
|
PF06741;PF07145;PF14438;
| null |
Ataxin-2 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9668173}.
| null | null | null | null | null |
FUNCTION: Involved in EGFR trafficking, acting as negative regulator of endocytic EGFR internalization at the plasma membrane. {ECO:0000269|PubMed:18602463}.
|
Mus musculus (Mouse)
|
O70306
|
TBX15_MOUSE
|
MSERRRSAVALSSRAHAFSVEALIGSNKKRKLRDWEEKGLDLSMEALSPAGPLGDTDDPATHGLEPHPDSEQSTGSDSEVLTERTSCSFSTHTDLASGAAGPVPAAMSSMEEIQVELQCADLWKRFHDIGTEMIITKAGRRMFPAMRVKITGLDPHQQYYIAMDIVPVDNKRYRYVYHSSKWMVAGNADSPVPPRVYIHPDSLASGDTWMRQVVSFDKLKLTNNELDDQGHIILHSMHKYQPRVHVIRKDFSSDLSPTKPVPVGDGVKTFNFPETVFTTVTAYQNQQITRLKIDRNPFAKGFRDSGRNRTGLEAIMETYAFWRPPVRTLTFEDFTTMQKQQGGSTGTSPTTSSTGTPSPSASSHLLSPSCSPPTFHLAPNTFNVGCRESQLCNLNLSDYPPCARSNMAALQSYPGLSDSGYNRLQSGTASATQPSETFMPQRTPSLISGIPTPPSLPSNSKMEAYGGQLGSFPTSQFQYVMQAGNAASSSSSPHMFGGSHMQQSSYNAFSLHNPYNLYGYNFPTSPRLAASPEKLSASQSTLLCSSPSNGAFGERQYLPTGMEHSMHMISPSTNNQQATNTCDGRQYGAVPGSASQMSVHMV
| null | null |
cell fate specification [GO:0001708]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic skeletal system morphogenesis [GO:0048704]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; nucleus [GO:0005634]; RNA polymerase II transcription repressor complex [GO:0090571]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00907;
|
2.60.40.820;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
| null | null | null | null | null |
FUNCTION: Probable transcriptional regulator involved in the development of the skeleton of the limb, vertebral column and head. Acts by controlling the number of mesenchymal precursor cells and chondrocytes.
|
Mus musculus (Mouse)
|
O70309
|
ITB5_MOUSE
|
MPRVPATLYACLLGLCALVPRLAGLNICTSGSATSCEECLLIHPKCAWCSKEYFGNPRSITSRCDLKANLIRNGCEGEIESPASSTHVLRNLPLSSKGSSATGSDVIQMTPQEIAVSLRPGEQTTFQLQVRQVEDYPVDLYYLMDLSLSMKDDLENIRSLGTKLAEEMRKLTSNFRLGFGSFVDKDISPFSYTAPRYQTNPCIGYKLFPNCVPSFGFRHLLPLTDRVDSFNEEVRKQRVSRNRDAPEGGFDAVLQAAVCKEKIGWRKDALHLLVFTTDDVPHIALDGKLGGLVQPHDGQCHLNEANEYTASNQMDYPSLALLGEKLAENNINLIFAVTKNHYMLYKNFTALIPGTTVEILHGDSKNIIQLIINAYSSIRAKVELSVWDQPEDLNLFFTATCQDGISYPGQRKCEGLKIGDTASFEVSVEARSCPGRQAAQSFTLRPVGFRDSLQVEVAYNCTCGCSTGLEPNSARCSGNGTYTCGLCECDPGYLGTRCECQEGENQSGYQNLCREAEGKPLCSGRGECSCNQCSCFESEFGRIYGPFCECDSFSCARNKGVLCSGHGECHCGECKCHAGYIGDNCNCSTDVSTCKAKDGQICSDRGRCVCGQCQCTEPGAFGETCEKCPTCPDACSSKRDCVECLLLHQGKPDNQTCHHQCKDEVITWVDTIVKDDQEAVLCFYKTAKDCVMMFSYTELPNGRSNLTVLREPECGSAPNAMTILLAVVGSILLIGMALLAIWKLLVTIHDRREFAKFQSERSRARYEMASNPLYRKPISTHTVDFAFNKFNKSYNGSV
| null | null |
cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; integrin-mediated signaling pathway [GO:0007229]; stress fiber assembly [GO:0043149]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
cell leading edge [GO:0031252]; cell surface [GO:0009986]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; integrin alphav-beta5 complex [GO:0034684]; integrin complex [GO:0008305]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; synaptic membrane [GO:0097060]
|
integrin binding [GO:0005178]; metal ion binding [GO:0046872]
|
PF07974;PF18372;PF08725;PF07965;PF00362;PF17205;
|
4.10.1240.30;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410;
|
Integrin beta chain family
| null |
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Integrin alpha-V/beta-5 (ITGAV:ITGB5) is a receptor for fibronectin. It recognizes the sequence R-G-D in its ligand.
|
Mus musculus (Mouse)
|
O70310
|
NMT1_MOUSE
|
MADESETAVKLPAPSLPLMMEGNGNGHEHCSDCENEEDNSHNRSGLSPANDTGAKKKKKKQKKKKEKGSDMESTQDQPVKMTSLPAERIQEIQKAIELFSVGQGPAKTMEEASKRSYQFWDTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEKKMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLNPRKLIEVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMEKKDIPVVHQLLSRYLKQFHLTPVMNQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAYSFYNVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWKCPSMGAEKVGLVLQ
|
2.3.1.97
| null |
cellular ketone metabolic process [GO:0042180]; in utero embryonic development [GO:0001701]; N-terminal peptidyl-glycine N-myristoylation [GO:0018008]; protein localization to membrane [GO:0072657]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
glycylpeptide N-tetradecanoyltransferase activity [GO:0004379]; myristoyltransferase activity [GO:0019107]; peptidyl-lysine N6-myristoyltransferase activity [GO:0018030]
|
PF01233;PF02799;
|
3.40.630.170;
|
NMT family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30419}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P30419}. Membrane {ECO:0000250|UniProtKB:P30419}; Peripheral membrane protein {ECO:0000250|UniProtKB:P30419}. Note=Copurifies with ribosomes. {ECO:0000250|UniProtKB:P30419}.
|
CATALYTIC ACTIVITY: Reaction=N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) + N-tetradecanoylglycyl-[protein]; Xref=Rhea:RHEA:15521, Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12667, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:64723, ChEBI:CHEBI:133050; EC=2.3.1.97; Evidence={ECO:0000269|PubMed:15753093}; CATALYTIC ACTIVITY: Reaction=N-terminal glycyl-L-lysyl-[protein] + tetradecanoyl-CoA = CoA + H(+) + N-terminal glycyl-(N(6)-tetradecanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:70671, Rhea:RHEA-COMP:17947, Rhea:RHEA-COMP:17948, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:189855, ChEBI:CHEBI:189856; Evidence={ECO:0000250|UniProtKB:P30419}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70672; Evidence={ECO:0000250|UniProtKB:P30419};
| null | null | null | null |
FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins (PubMed:15753093). Also able to mediate N-terminal lysine myristoylation of proteins: catalyzes myristoylation of ARF6 on both 'Gly-2' and 'Lys-3' (By similarity). Lysine myristoylation is required to maintain ARF6 on membranes during the GTPase cycle (By similarity). Required for normal embryogenesis (PubMed:15753093). {ECO:0000250|UniProtKB:P30419, ECO:0000269|PubMed:15753093}.
|
Mus musculus (Mouse)
|
O70318
|
E41L2_MOUSE
|
MTTEVGSASEVKKGSDQAGADASKEKAKEVENEQTPVSEPEEEKGSQPGPPVERQSTPRLRKRGKDPSENRGISRFIPPWLKKQRSYNLVVAKDGGDKKEPTQADVEDQILGKEESLPEEESRAKGDAEEMAQRKHLEVQVEVREAKPALKSSVETQPAEEVRKDKEETIQDTQEEKLEGGAAKRETKEVQTSELKAEVASQKATKKTKTVLAKVTLLDGTEYSCDLEKRAKGQVLFDRVCEHLNLLEKDYFGLLFQDHPEQKNWLDPAKEIKRQLKNLPWLFTFNVKFYPPDPSQLTEDITRYFLCLQLRQDIASGRLPCSFVTHALLGSYTLQAEHGDYDPEEYDSIDLGDFQFAPAHTKELEEKVSELHKTHRGLSPAQADSQFLENAKRLSMYGVDLHHAKDSEGVDIKLGVCANGLLIYKDRLRINRFAWPKILKISYKRSNFYIKVRPAELEQFESTIGFKLPNHRAAKRLWKVCVEHHTFYRLVSPEQPPKTKFLTLGSKFRYSGRTQAQTREASTLIDRPAPQFERASSKRVSRSLDGAPIGVVDQSPPGEGSVPGPGVISYTTIQDGRRDSKSPTKATPLPAEGKKNTLRVDGDNIYVRHSNLMLEDLDKAQEAILKHQASISELKRNFMASTPEPRPSEWEKRRVTPLPFQPQASSHETLNVVEEKKRAEVGKDESVITEEMNGKEMSPGHGPGETRKVEPVAHKDSTSLSSESSSSSSESEEDVGEYQPHHRVTEGTIREEQEECDEELEEEPGQGAKVVEREAAVPDAVPDRQAGASVLPVETEAQEHVVAQKLPGEKGAHGGTAEQDPREEAEEDPHRVNGEVPHLDLDGLPEIICCSEPPVVKTEMVTISDASQRTEISTKEVPIVQTETKTITYESPQIDGGAGGDSGVLLTAQTITSESASTTTTTHITKTVKGGISETRIEKRIVITGDAALDHDQALAQAIREAREQHPDMSVTRVVVHKETELAEEGEE
| null | null |
actin cytoskeleton organization [GO:0030036]; actomyosin structure organization [GO:0031032]; cell cycle [GO:0007049]; cell division [GO:0051301]; cortical actin cytoskeleton organization [GO:0030866]; positive regulation of protein localization to cell cortex [GO:1904778]; regulation of cell shape [GO:0008360]
|
actin cytoskeleton [GO:0015629]; cell cortex [GO:0005938]; cell junction [GO:0030054]; COP9 signalosome [GO:0008180]; cytoskeleton [GO:0005856]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
|
actin binding [GO:0003779]; PH domain binding [GO:0042731]; spectrin binding [GO:0030507]; structural molecule activity [GO:0005198]
|
PF05902;PF08736;PF09380;PF00373;PF09379;PF04382;
|
1.20.80.10;2.30.29.30;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:O43491}. Cell membrane {ECO:0000250|UniProtKB:O43491}.
| null | null | null | null | null |
FUNCTION: Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. {ECO:0000250|UniProtKB:O43491}.
|
Mus musculus (Mouse)
|
O70320
|
PLB1_CAVPO
|
MGLQPGVLLVGLLLLGQGITQIHTSSGKSTLEGQLWPETKKNFPFSCSPKKLGLNMPSESVHTLTPADIKLIAAIGDMETPPDSGAVNLDTSERTEKEPWRGCMGMMTVLSDIISHFNPSVLLPTCPPWRSAAVRGGVEELRTQAEELVSSLKKNPQLDFQQDWKLINVFFSNASLCYLCPSAHENGPLMSNMDKLAGILHYLHQEVPRAFVNLVDLFEVVAMPRWHQGTMLSRPSPEACGCSGETSKLDTVVMQWSYQETWDSLLASSSFNDQESFAVVFQPFFYEVSSPVEEPPSQDPTTLALSLWNNMMKPVGQKDEPFSTIERRPMKCPSQESPYLFTYRNSNYQSRLLKRQRQHKEREGTEIRCPDKDPSDSTPTSVHRLKPADIKVIGALGDSLTAGNGAGSRPGNILDVLTEYRGLSWSIGADHNISSVTTLPNILREFNPSLKGFSTGTGKANSVGAFFNQAVAGARAGDLIPQARTLVDLMKNHTSINFEEDWKIITVFIGGNDLCDFCSDPVTNSPENFTDNIRQALDILHAEVPRAFVNMVKVLQIVNLRELYKDSRVSCPRLILRNLCRCVLLPDDNSTELESLIDINKKYQERTHQLIESGRYDTREDFTVVLQPFFEKVDIPKTSEGLPDNTSFAPDCFHFSSKTHARAASALWKNMLEPVGQKTTQNNFENSIDIICPNQAFPYLSTYKNGIEGHGTWLTCRERTPSASPPTSVHALRPADVRVVAALGDSLTAGSGIGSKPGDLADVITQYRGLSYSSGGDGSLMNVTTLPNILREFNSNLTGYAVGTGDASNTNAFLNQAVPGAKAEELMSQVKTLVQKMKDDPRINFHEDWKVITVLIGTNDLCNHCTDLDLYSSANFFNHLLNALDILHREVPRALVNLVDFMNPSIMRQVFLGNPDKCPVQQASILCNCVLSLRENSYELARMDALTRAYQSSMRELVESGRYDTREDFSVVLQPFFLNIRLPILEDGRPDTSFFAPDCINPGQKFHSQLSRALWVNMLEPVGSKTDTLDLTADISLPCPTQEEPFLRTPQNSDYTYPTKPAIENWGSDFLCTEWKPSNSVPTSVHKLQPADIKVVAALGDSLTTAVGARASNSSDLLMSWRGLSWSIGGDGALETHTTLPNILKKFNPSIFGFSTGTLEETAGFNVAVEEARARDMPAQARDLVERMKASTEINLEMDWKLITLFIGSNDLCHYCDNPENHSAEEYVQHIRQALDILYEELPRAFINVVDIIMELAGLHQGQGGHCTALLPAQSTCSCLRHFPSSPVIQELKKVTWNLQSDMSRLSYQEKYTQREDFAVVVQPFFQNTLIPLDKLGSTDPTFFSEDCLHFSERGHAEMAIALWNNMLEPVGHKTTFNNFTYNRTKLKCPSTESPYLYTLQNSLSLPVQTEKASGVAPGIVSAAAAGGLLVGLIVGILAVSLWSSFRRRQKKSPPESVPVANF
|
3.1.1.3; 3.1.1.4; 3.1.1.5
| null |
phospholipid metabolic process [GO:0006644]
|
apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]
|
lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; phospholipase A2 activity [GO:0004623]; retinyl-palmitate esterase activity [GO:0050253]; triglyceride lipase activity [GO:0004806]
|
PF00657;
|
3.40.50.1110;
|
'GDSL' lipolytic enzyme family, Phospholipase B1 subfamily
|
PTM: Undergoes proteolytic cleavage in the ileum. {ECO:0000269|PubMed:9593672}.
|
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:O54728}; Single-pass type I membrane protein {ECO:0000255}. Note=Present in the intestinal brush border membranes. {ECO:0000269|PubMed:9593672}.
|
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:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000250|UniProtKB:O54728}; 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:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40923, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669; Evidence={ECO:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40924; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + a 1-acyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40643, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:58168, ChEBI:CHEBI:60000; Evidence={ECO:0000269|PubMed:2722844, ECO:0000269|PubMed:9593672}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40644; Evidence={ECO:0000305|PubMed:2722844, ECO:0000305|PubMed:9593672}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; Evidence={ECO:0000250|UniProtKB:Q05017}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; Evidence={ECO:0000250|UniProtKB:Q05017}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:40971, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73002, ChEBI:CHEBI:76084; Evidence={ECO:0000250|UniProtKB:Q05017}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40972; Evidence={ECO:0000250|UniProtKB:Q05017}; CATALYTIC ACTIVITY: Reaction=1-acyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + a 1-acyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40639, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:64381, ChEBI:CHEBI:75069; Evidence={ECO:0000269|PubMed:2722844}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40640; Evidence={ECO:0000305|PubMed:2722844}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40911, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:73004, ChEBI:CHEBI:73007; Evidence={ECO:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72841, ChEBI:CHEBI:75158; Evidence={ECO:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + 2 H2O = 2 H(+) + 2 hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40975, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72999; Evidence={ECO:0000269|PubMed:2722844}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40976; Evidence={ECO:0000305|PubMed:2722844}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40915, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:34112, ChEBI:CHEBI:64496; Evidence={ECO:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40916; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + H(+) + octadecanoate; Xref=Rhea:RHEA:41111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75466, ChEBI:CHEBI:77623; Evidence={ECO:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41112; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = (9Z)-octadecenoate + 1,3-dihexadecanoylglycerol + H(+); Xref=Rhea:RHEA:40983, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75688, ChEBI:CHEBI:77619; Evidence={ECO:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40984; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:40979, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75585, ChEBI:CHEBI:75688; Evidence={ECO:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40980; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-3-octadecanoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:41103, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77623, ChEBI:CHEBI:77624; Evidence={ECO:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41104; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + H2O = 2-(9Z-octadecenoyl)-3-octadecanoyl-sn-glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:41107, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75558, ChEBI:CHEBI:77623; Evidence={ECO:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41108; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + H2O = (9Z,12Z)-octadecadienoate + 1-octadecanoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:40927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:75550, ChEBI:CHEBI:77097; Evidence={ECO:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40928; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:41219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:75757; Evidence={ECO:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41220; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=2,3-di-(9Z)-octadecenoyl-sn-glycerol + H2O = (9Z)-octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:42604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75824, ChEBI:CHEBI:75938; Evidence={ECO:0000250|UniProtKB:O54728}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42605; Evidence={ECO:0000250|UniProtKB:O54728}; CATALYTIC ACTIVITY: Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:39939, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342, ChEBI:CHEBI:75735; Evidence={ECO:0000250|UniProtKB:Q05017}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39940; Evidence={ECO:0000250|UniProtKB:Q05017}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q05017}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000250|UniProtKB:Q05017}; CATALYTIC ACTIVITY: Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:Q05017}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492; Evidence={ECO:0000250|UniProtKB:Q05017};
| null | null | null | null |
FUNCTION: Calcium-independent membrane-associated phospholipase that catalyzes complete diacylation of phospholipids by hydrolyzing both sn-1 and sn-2 fatty acyl chains attached to the glycerol backbone (phospholipase B activity) (PubMed:2722844). Has dual phospholipase and lysophospholipase activities toward diacylphospholipids. Preferentially cleaves sn-2 ester bonds over sn-1 bonds (PubMed:2722844, PubMed:9593672). Acts as a lipase toward glycerolipid substrates (By similarity). Hydrolyzes fatty acyl chains of diacylglycerols with preference for the sn-2 position and of triacylglycerols with not positional selectivity (By similarity). May also hydrolyze long chain retinyl esters such as retinyl palmitate (By similarity). May contribute to digestion of dietary phospholipids, glycerolipids and retinoids, facilitating lipid absorption at the brush border (By similarity). {ECO:0000250|UniProtKB:O54728, ECO:0000250|UniProtKB:Q05017, ECO:0000269|PubMed:2722844, ECO:0000269|PubMed:9593672}.
|
Cavia porcellus (Guinea pig)
|
O70324
|
MOT8_MOUSE
|
MALPSPASEEAEGPCQEANQEYQEPVCSPVPEPEPEPEPEPEPDPEPVPVPPPEPQPEPEPQPLPDPAPLPELGFEAEPVQEPEPTPTVETRGTARGFQPPEGGFGWIVVFAATWCNGSIFGIHNSVGILYSMLLEEEKEKNRQVEFQAAWVGALAMGMIFFCSPIVSIFTDRLGCRITATTGAAVAFIGLHTSSFTSSLSLRYFTYGILFGCGCSFAFQPSLVILGHYFQRRLGLANGVVSAGSSIFSMSFPFLIKMLGDKIKLAQTFQVLSTFMFVLTLLSLTYRPLLPSSQDTPSKRGAHTLRQRFLVQFRKYFNMRVFRQRTYRIWAFGIAAAALGYFVPYVHLMKYVEDKFKEIKETWVLLVCIGATSGLGRLVSGHISDSIPGLKKIYLQVLSFLLLGLMSMMIPLCRDFGGLIVVCLFLGLCDGFFITIMAPIAFELVGPMQASQAIGYLLGMMALPMIAGPPIAGLLRNCFGDYHVAFYFAGVPPIIGAVILFFVPLMHQRMFKKEQRDSSKDKMLSHDPDPNGELLPGSPTPEEPI
| null | null |
amino acid import across plasma membrane [GO:0089718]; amino acid metabolic process [GO:0006520]; hormone transport [GO:0009914]; negative regulation of neural precursor cell proliferation [GO:2000178]; thyroid hormone generation [GO:0006590]; thyroid hormone transport [GO:0070327]; thyroid-stimulating hormone secretion [GO:0070460]; transport across blood-brain barrier [GO:0150104]
|
apical plasma membrane [GO:0016324]; plasma membrane [GO:0005886]
|
amino acid transmembrane transporter activity [GO:0015171]; identical protein binding [GO:0042802]; monocarboxylic acid transmembrane transporter activity [GO:0008028]; thyroid hormone transmembrane transporter activity [GO:0015349]
|
PF07690;
|
1.20.1250.20;
|
Major facilitator superfamily, Monocarboxylate porter (TC 2.A.1.13) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18687783}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:18687783}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=3,3',5-triiodo-L-thyronine(out) = 3,3',5-triiodo-L-thyronine(in); Xref=Rhea:RHEA:71811, ChEBI:CHEBI:533015; Evidence={ECO:0000269|PubMed:31436139}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71812; Evidence={ECO:0000305|PubMed:31436139}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71813; Evidence={ECO:0000305|PubMed:31436139}; CATALYTIC ACTIVITY: Reaction=3,3',5'-triiodo-L-thyronine(out) = 3,3',5'-triiodo-L-thyronine(in); Xref=Rhea:RHEA:71815, ChEBI:CHEBI:57261; Evidence={ECO:0000269|PubMed:31436139}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71816; Evidence={ECO:0000305|PubMed:31436139}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71817; Evidence={ECO:0000305|PubMed:31436139}; CATALYTIC ACTIVITY: Reaction=L-thyroxine(out) = L-thyroxine(in); Xref=Rhea:RHEA:71819, ChEBI:CHEBI:58448; Evidence={ECO:0000269|PubMed:31436139}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71820; Evidence={ECO:0000305|PubMed:31436139}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71821; Evidence={ECO:0000305|PubMed:31436139}; CATALYTIC ACTIVITY: Reaction=3,3'-diiodo-L-thyronine(out) = 3,3'-diiodo-L-thyronine(in); Xref=Rhea:RHEA:71823, ChEBI:CHEBI:176514; Evidence={ECO:0000269|PubMed:31436139}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71824; Evidence={ECO:0000305|PubMed:31436139}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71825; Evidence={ECO:0000305|PubMed:31436139};
| null | null | null | null |
FUNCTION: Specific thyroid hormone transmembrane transporter, that mediates both uptake and efflux of thyroid hormones across the cell membrane independently of pH or a Na(+) gradient (PubMed:31436139). Major substrates are the iodothyronines T3 and T4 and to a lesser extent rT3 and 3,3-diiodothyronine (3,3'-T2). Acts as an important mediator of thyroid hormone transport, especially T3, through the blood-brain barrier (PubMed:19147674). {ECO:0000269|PubMed:19147674, ECO:0000269|PubMed:31436139}.
|
Mus musculus (Mouse)
|
O70325
|
GPX4_MOUSE
|
MSWGRLSRLLKPALLCGALAAPGLAGTMCASRDDWRCARSMHEFSAKDIDGHMVCLDKYRGFVCIVTNVASQUGKTDVNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKEFAAGYNVKFDMYSKICVNGDDAHPLWKWMKVQPKGRGMLGNAIKWNFTKFLIDKNGCVVKRYGPMEEPQVIEKDLPCYL
|
1.11.1.12; 1.11.1.9
| null |
arachidonic acid metabolic process [GO:0019369]; cellular response to oxidative stress [GO:0034599]; chromatin organization [GO:0006325]; lipoxygenase pathway [GO:0019372]; negative regulation of ferroptosis [GO:0110076]; protein polymerization [GO:0051258]; response to estradiol [GO:0032355]; response to oxidative stress [GO:0006979]; spermatogenesis [GO:0007283]
|
cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
glutathione peroxidase activity [GO:0004602]; identical protein binding [GO:0042802]; phospholipid-hydroperoxide glutathione peroxidase activity [GO:0047066]; selenium binding [GO:0008430]
|
PF00255;
|
3.40.30.10;
|
Glutathione peroxidase family
| null |
SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion {ECO:0000269|PubMed:12566075, ECO:0000269|PubMed:22207760}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm {ECO:0000269|PubMed:12566075}.; SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus {ECO:0000269|PubMed:11344099}.
|
CATALYTIC ACTIVITY: Reaction=a hydroperoxy polyunsaturated fatty acid + 2 glutathione = a hydroxy polyunsaturated fatty acid + glutathione disulfide + H2O; Xref=Rhea:RHEA:19057, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:131871, ChEBI:CHEBI:134019; EC=1.11.1.12; Evidence={ECO:0000269|PubMed:29290465}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19058; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O; Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9; Evidence={ECO:0000269|PubMed:12566075}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834; Evidence={ECO:0000305|PubMed:12566075}; CATALYTIC ACTIVITY: Reaction=2 glutathione + tert-butyl hydroperoxide = glutathione disulfide + H2O + tert-butanol; Xref=Rhea:RHEA:69412, ChEBI:CHEBI:15377, ChEBI:CHEBI:45895, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:64090; Evidence={ECO:0000269|PubMed:12566075}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69413; Evidence={ECO:0000305|PubMed:12566075}; CATALYTIC ACTIVITY: Reaction=cumene hydroperoxide + 2 glutathione = 2-phenylpropan-2-ol + glutathione disulfide + H2O; Xref=Rhea:RHEA:69651, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:78673, ChEBI:CHEBI:131607; Evidence={ECO:0000250|UniProtKB:P36969}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69652; Evidence={ECO:0000250|UniProtKB:P36969}; CATALYTIC ACTIVITY: Reaction=(9S)-hydroperoxy-(10E,12Z)-octadecadienoate + 2 glutathione = (9S)-hydroxy-(10E,12Z)-octadecadienoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76687, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:60955, ChEBI:CHEBI:77852; Evidence={ECO:0000250|UniProtKB:P36969}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76688; Evidence={ECO:0000250|UniProtKB:P36969}; CATALYTIC ACTIVITY: Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate + 2 glutathione = (13S)-hydroxy-(9Z,11E)-octadecadienoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:48888, ChEBI:CHEBI:15377, ChEBI:CHEBI:57466, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90850; Evidence={ECO:0000250|UniProtKB:P36969}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48889; Evidence={ECO:0000250|UniProtKB:P36969}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90632; Evidence={ECO:0000250|UniProtKB:P36969}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48621; Evidence={ECO:0000250|UniProtKB:P36969}; CATALYTIC ACTIVITY: Reaction=(12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2 glutathione = (12R)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76691, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:75230, ChEBI:CHEBI:83343; Evidence={ECO:0000250|UniProtKB:P36969}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76692; Evidence={ECO:0000250|UniProtKB:P36969}; CATALYTIC ACTIVITY: Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2 glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:50708, ChEBI:CHEBI:15377, ChEBI:CHEBI:57444, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90680; Evidence={ECO:0000250|UniProtKB:P36969}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50709; Evidence={ECO:0000250|UniProtKB:P36969}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + 2 glutathione = (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76695, ChEBI:CHEBI:15377, ChEBI:CHEBI:57409, ChEBI:CHEBI:57446, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; Evidence={ECO:0000250|UniProtKB:P36969}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76696; Evidence={ECO:0000250|UniProtKB:P36969}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z,17Z)-eicosapentaenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z,17Z)-eicosapentaenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76699, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:195399, ChEBI:CHEBI:195400; Evidence={ECO:0000250|UniProtKB:P36969}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76700; Evidence={ECO:0000250|UniProtKB:P36969}; CATALYTIC ACTIVITY: Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z,17Z)-eicosapentaenoate + 2 glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z,17Z)-eicosapentaenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76703, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90772, ChEBI:CHEBI:195401; Evidence={ECO:0000250|UniProtKB:P36969}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76704; Evidence={ECO:0000250|UniProtKB:P36969}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + 2 glutathione = (15S)-hydroxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76707, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:132087, ChEBI:CHEBI:194369; Evidence={ECO:0000250|UniProtKB:P36969}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76708; Evidence={ECO:0000250|UniProtKB:P36969}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(11Z,13E)-eicosadienoate + 2 glutathione = (15S)-hydroxy-(11Z,13E)-eicosadienoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76711, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:144832, ChEBI:CHEBI:195402; Evidence={ECO:0000250|UniProtKB:P36969}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76712; Evidence={ECO:0000250|UniProtKB:P36969}; CATALYTIC ACTIVITY: Reaction=(17S)-hydroperoxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate + 2 glutathione = (17S)-hydroxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:76715, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:133795, ChEBI:CHEBI:195403; Evidence={ECO:0000250|UniProtKB:P36969}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76716; Evidence={ECO:0000250|UniProtKB:P36969}; CATALYTIC ACTIVITY: Reaction=a hydroperoxy-1,2-diacyl-glycero-3-phosphocholine + 2 glutathione = a hydroxy-1,2-diacyl-glycero-3-phosphocholine + glutathione disulfide + H2O; Xref=Rhea:RHEA:76731, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:195423, ChEBI:CHEBI:195424; Evidence={ECO:0000269|PubMed:25922076}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76732; Evidence={ECO:0000305|PubMed:25922076};
| null | null | null | null |
FUNCTION: Essential antioxidant peroxidase that directly reduces phospholipid hydroperoxide even if they are incorporated in membranes and lipoproteins (PubMed:29290465). Can also reduce fatty acid hydroperoxide, cholesterol hydroperoxide and thymine hydroperoxide (By similarity). Plays a key role in protecting cells from oxidative damage by preventing membrane lipid peroxidation (PubMed:12566075). Required to prevent cells from ferroptosis, a non-apoptotic cell death resulting from an iron-dependent accumulation of lipid reactive oxygen species (PubMed:12566075, PubMed:24439385, PubMed:25402683, PubMed:25922076, PubMed:29290465). The presence of selenocysteine (Sec) versus Cys at the active site is essential for life: it provides resistance to overoxidation and prevents cells against ferroptosis (PubMed:29290465). The presence of Sec at the active site is also essential for the survival of a specific type of parvalbumin-positive interneurons, thereby preventing against fatal epileptic seizures (PubMed:29290465). May be required to protect cells from the toxicity of ingested lipid hydroperoxides (PubMed:12566075). Required for normal sperm development and male fertility (PubMed:19783653, PubMed:25922076). Essential for maturation and survival of photoreceptor cells (PubMed:22207760). Plays a role in a primary T-cell response to viral and parasitic infection by protecting T-cells from ferroptosis and by supporting T-cell expansion (PubMed:25824823). Plays a role of glutathione peroxidase in platelets in the arachidonic acid metabolism (By similarity). Reduces hydroperoxy ester lipids formed by a 15-lipoxygenase that may play a role as down-regulator of the cellular 15-lipoxygenase pathway (By similarity). Can also reduce small soluble hydroperoxides such as H2O2 and tert-butyl hydroperoxide (PubMed:12566075). {ECO:0000250|UniProtKB:P36968, ECO:0000250|UniProtKB:P36969, ECO:0000269|PubMed:12566075, ECO:0000269|PubMed:18762024, ECO:0000269|PubMed:19783653, ECO:0000269|PubMed:22207760, ECO:0000269|PubMed:24439385, ECO:0000269|PubMed:25402683, ECO:0000269|PubMed:25824823, ECO:0000269|PubMed:25922076, ECO:0000269|PubMed:29290465}.; FUNCTION: [Isoform Cytoplasmic]: Specifically able to suppress the production of leukotriene and prostaglandin in response to several stimuli by reducing fatty acid hydroperoxide. {ECO:0000250|UniProtKB:P36970}.; FUNCTION: [Isoform Mitochondrial]: Specifically required to prevent mitochondrial cell death by mediating reduction of cardiolipin hydroperoxide (By similarity). Also required for normal sperm development and male fertility (PubMed:19417079). {ECO:0000250|UniProtKB:P36970, ECO:0000269|PubMed:19417079}.; FUNCTION: [Isoform Nuclear]: Required for male fertility by stabilizing the condensed chromatin in sperm nuclei (PubMed:12566075). {ECO:0000269|PubMed:12566075}.
|
Mus musculus (Mouse)
|
O70326
|
GREM1_MOUSE
|
MNRTAYTVGALLLLLGTLLPTAEGKKKGSQGAIPPPDKAQHNDSEQTQSPPQPGSRTRGRGQGRGTAMPGEEVLESSQEALHVTERKYLKRDWCKTQPLKQTIHEEGCNSRTIINRFCYGQCNSFYIPRHIRKEEGSFQSCSFCKPKKFTTMMVTLNCPELQPPTKKKRVTRVKQCRCISIDLD
| null | null |
angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; cardiac muscle cell differentiation [GO:0055007]; cardiac muscle cell myoblast differentiation [GO:0060379]; cell migration involved in sprouting angiogenesis [GO:0002042]; cell morphogenesis [GO:0000902]; cell-cell signaling [GO:0007267]; collagen fibril organization [GO:0030199]; determination of dorsal identity [GO:0048263]; embryonic limb morphogenesis [GO:0030326]; endothelial cell migration [GO:0043542]; mesenchymal to epithelial transition involved in metanephros morphogenesis [GO:0003337]; negative regulation of apoptotic process [GO:0043066]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of bone mineralization involved in bone maturation [GO:1900158]; negative regulation of bone remodeling [GO:0046851]; negative regulation of bone trabecula formation [GO:1900155]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell growth [GO:0030308]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of leukocyte chemotaxis [GO:0002689]; negative regulation of monocyte chemotaxis [GO:0090027]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of osteoblast proliferation [GO:0033689]; negative regulation of osteoclast proliferation [GO:0090291]; negative regulation of SMAD protein signal transduction [GO:0060392]; positive regulation of angiogenesis [GO:0045766]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of peptidyl-tyrosine autophosphorylation [GO:1900086]; positive regulation of protein tyrosine kinase activity [GO:0061098]; positive regulation of receptor internalization [GO:0002092]; positive regulation of signaling receptor activity [GO:2000273]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proximal/distal pattern formation [GO:0009954]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of focal adhesion assembly [GO:0051893]; sequestering of BMP from receptor via BMP binding [GO:0038098]; signal transduction [GO:0007165]; ureteric bud formation [GO:0060676]
|
cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
BMP binding [GO:0036122]; cytokine activity [GO:0005125]; heparan sulfate proteoglycan binding [GO:0043395]; protein homodimerization activity [GO:0042803]; receptor ligand activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]; vascular endothelial growth factor receptor 2 binding [GO:0043184]
|
PF03045;
|
2.10.90.10;
|
DAN family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Cytokine that may play an important role during carcinogenesis and metanephric kidney organogenesis, as BMP a antagonist required for early limb outgrowth and patterning in maintaining the FGF4-SHH feedback loop (PubMed:12808456, PubMed:15201225). Down-regulates the BMP4 signaling in a dose-dependent manner (PubMed:15133038). Antagonist of BMP2; inhibits BMP2-mediated differentiation of osteoblasts (in vitro) (By similarity). Acts as inhibitor of monocyte chemotaxis (By similarity). {ECO:0000250|UniProtKB:O35793, ECO:0000250|UniProtKB:O60565, ECO:0000269|PubMed:12808456, ECO:0000269|PubMed:15133038, ECO:0000269|PubMed:15201225}.
|
Mus musculus (Mouse)
|
O70333
|
CRIPT_MOUSE
|
MVCEKCEKKLGRVITPDTWKDGARNTTESGGRKLNENKALTSKKARFDPYGKNKFSTCRICKSSVHQPGSHYCQGCAYKKGICAMCGKKVLDTKNYKQTSV
| null | null |
cytoplasmic microtubule organization [GO:0031122]; establishment of protein localization [GO:0045184]; mRNA processing [GO:0006397]; protein localization to microtubule [GO:0035372]; regulation of postsynaptic density assembly [GO:0099151]; regulation of postsynaptic density protein 95 clustering [GO:1902897]; RNA splicing [GO:0008380]
|
cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; postsynaptic density [GO:0014069]; postsynaptic density, intracellular component [GO:0099092]; spliceosomal complex [GO:0005681]
|
microtubule binding [GO:0008017]; PDZ domain binding [GO:0030165]; protein-containing complex binding [GO:0044877]; scaffold protein binding [GO:0097110]
|
PF10235;
| null |
CRIPT family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Synapse {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Note=Colocalizes with DLG4 in asymmetric synapses. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (By similarity). Involved in the cytoskeletal anchoring of DLG4 in excitatory synapses (By similarity). {ECO:0000250|UniProtKB:Q792Q4, ECO:0000250|UniProtKB:Q9P021}.
|
Mus musculus (Mouse)
|
O70337
|
BIK_MOUSE
|
MSEARLMARDVIKTVPHDQVPQPPVASETPSMKEPVRDVDLMECVEGRNQVALRLACIGDEMDLCLRSPRLVQLPGIAIHRLAVTYSRTGVRGIFRSLIRSLTNLRENIWSWRVLTPGAWVSPDQDPGQLFPMVLLVFLLLGGAWYLQLQ
| null | null |
apoptotic mitochondrial changes [GO:0008637]; male gonad development [GO:0008584]; regulation of apoptotic process [GO:0042981]; spermatogenesis [GO:0007283]
|
Bcl-2 family protein complex [GO:0097136]; endomembrane system [GO:0012505]; mitochondrial envelope [GO:0005740]; mitochondrial membrane [GO:0031966]
|
BH domain binding [GO:0051400]; protein-containing complex binding [GO:0044877]
|
PF12201;
| null | null |
PTM: Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced cleavage is a necessary step prior its degradation by the proteosome-dependent mechanism (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Mitochondrion membrane {ECO:0000269|PubMed:9525867}; Single-pass membrane protein {ECO:0000269|PubMed:9525867}. Note=Around the nuclear envelope, and in cytoplasmic membranes. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Accelerates programmed cell death. Binding to the apoptosis repressors Bcl-X(L), BHRF1 or Bcl-2 suppresses this death-promoting activity. {ECO:0000269|PubMed:9525867}.
|
Mus musculus (Mouse)
|
O70342
|
NPY5R_MOUSE
|
MEVKLEEHFNKTFVTENNTAASQNTASPAWEDYRGTENNTSAARNTAFPVWEDYRGSVDDLQYFLIGLYTFVSLLGFMGNLLILMAVMKKRNQKTTVNFLIGNLAFSDILVVLFCSPFTLTSVLLDQWMFGKAMCHIMPFLQCVSVLVSTLILISIAIVRYHMIKHPISNNLTANHGYFLIATVWTLGFAICSPLPVFHSLVELKETFGSALLSSKYLCVESWPSDSYRIAFTISLLLVQYILPLVCLTVSHTSVCRSISCGLSHKENRLEENEMINLTLHPSKKSRDQAKPPSTQKWSYSFIRKHRRRYSKKTACVLPAPAGPSQEKHLTVPENPGSVRSQLSPSSKVIPGVPICFEVKPEESSDAQEMRVKRSLTRIKKRSRSVFYRLTILILVFAVSWMPLHVFHVVTDFNDNLISNRHFKLVYCICHLLGMMSCCLNPILYGFLNNGIKADLRALIHCLHMS
| null | null |
cardiac left ventricle morphogenesis [GO:0003214]; chemical synaptic transmission [GO:0007268]; eating behavior [GO:0042755]; G protein-coupled receptor signaling pathway [GO:0007186]; generation of ovulation cycle rhythm [GO:0060112]; negative regulation of acute inflammatory response to antigenic stimulus [GO:0002865]; negative regulation of apoptotic process [GO:0043066]; negative regulation of glutamate secretion [GO:0014050]; negative regulation of synaptic transmission, GABAergic [GO:0032229]; outflow tract morphogenesis [GO:0003151]; positive regulation of acute inflammatory response [GO:0002675]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of smooth muscle cell proliferation [GO:0048661]; synaptic signaling via neuropeptide [GO:0099538]
|
GABA-ergic synapse [GO:0098982]; membrane [GO:0016020]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
|
neuropeptide binding [GO:0042923]; neuropeptide Y receptor activity [GO:0004983]; pancreatic polypeptide receptor activity [GO:0001602]; peptide YY receptor activity [GO:0001601]
|
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 neuropeptide Y and peptide YY. The activity of this receptor is mediated by G proteins that inhibit adenylate cyclase activity. Seems to be associated with food intake. Could be involved in feeding disorders (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O70343
|
PRGC1_MOUSE
|
MAWDMCSQDSVWSDIECAALVGEDQPLCPDLPELDLSELDVNDLDTDSFLGGLKWCSDQSEIISNQYNNEPANIFEKIDEENEANLLAVLTETLDSLPVDEDGLPSFDALTDGAVTTDNEASPSSMPDGTPPPQEAEEPSLLKKLLLAPANTQLSYNECSGLSTQNHAANHTHRIRTNPAIVKTENSWSNKAKSICQQQKPQRRPCSELLKYLTTNDDPPHTKPTENRNSSRDKCASKKKSHTQPQSQHAQAKPTTLSLPLTPESPNDPKGSPFENKTIERTLSVELSGTAGLTPPTTPPHKANQDNPFKASPKLKPSCKTVVPPPTKRARYSECSGTQGSHSTKKGPEQSELYAQLSKSSGLSRGHEERKTKRPSLRLFGDHDYCQSLNSKTDILINISQELQDSRQLDFKDASCDWQGHICSSTDSGQCYLRETLEASKQVSPCSTRKQLQDQEIRAELNKHFGHPCQAVFDDKSDKTSELRDGDFSNEQFSKLPVFINSGLAMDGLFDDSEDESDKLSYPWDGTQPYSLFDVSPSCSSFNSPCRDSVSPPKSLFSQRPQRMRSRSRSFSRHRSCSRSPYSRSRSRSPGSRSSSRSCYYYESSHYRHRTHRNSPLYVRSRSRSPYSRRPRYDSYEAYEHERLKRDEYRKEHEKRESERAKQRERQKQKAIEERRVIYVGKIRPDTTRTELRDRFEVFGEIEECTVNLRDDGDSYGFITYRYTCDAFAALENGYTLRRSNETDFELYFCGRKQFFKSNYADLDTNSDDFDPASTKSKYDSLDFDSLLKEAQRSLRR
| null | null |
adipose tissue development [GO:0060612]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cellular response to oxidative stress [GO:0034599]; cellular response to thyroid hormone stimulus [GO:0097067]; cellular response to transforming growth factor beta stimulus [GO:0071560]; circadian regulation of gene expression [GO:0032922]; energy homeostasis [GO:0097009]; gluconeogenesis [GO:0006094]; mitochondrion organization [GO:0007005]; negative regulation of glycolytic process [GO:0045820]; negative regulation of mitochondrial fission [GO:0090258]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of smooth muscle cell migration [GO:0014912]; negative regulation of smooth muscle cell proliferation [GO:0048662]; neuron apoptotic process [GO:0051402]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of fatty acid oxidation [GO:0046321]; positive regulation of gene expression [GO:0010628]; positive regulation of mitochondrion organization [GO:0010822]; positive regulation of podocyte apoptotic process [GO:1904635]; positive regulation of progesterone biosynthetic process [GO:2000184]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; regulation of circadian rhythm [GO:0042752]; regulation of DNA-templated transcription [GO:0006355]; respiratory electron transport chain [GO:0022904]; response to activity [GO:0014823]; response to dietary excess [GO:0002021]; response to muscle activity [GO:0014850]
|
apical dendrite [GO:0097440]; chromatin [GO:0000785]; cytosolic ribosome [GO:0022626]; euchromatin [GO:0000791]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]
|
alpha-tubulin binding [GO:0043014]; chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; lncRNA binding [GO:0106222]; nuclear estrogen receptor binding [GO:0030331]; nuclear receptor coactivator activity [GO:0030374]; peroxisome proliferator activated receptor binding [GO:0042975]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565]; transcription coactivator activity [GO:0003713]; transcription coregulator activity [GO:0003712]; ubiquitin protein ligase binding [GO:0031625]
|
PF00076;
|
3.30.70.330;
| null |
PTM: Phosphorylation by AMPK in skeletal muscle increases activation of its own promoter (PubMed:17609368). Phosphorylated by CLK2 (PubMed:20074525). {ECO:0000269|PubMed:17609368, ECO:0000269|PubMed:20074525}.; PTM: Heavily acetylated by KAT2A/GCN5 under conditions of high nutrients, leading to inactivation of PPARGC1A (PubMed:15744310). Deacetylated by SIRT1 in low nutrients/high NAD conditions, leading to its activation (PubMed:15716268, PubMed:15744310). {ECO:0000269|PubMed:15716268, ECO:0000269|PubMed:15744310}.; PTM: Ubiquitinated. Ubiquitination by RNF34 induces proteasomal degradation. {ECO:0000250|UniProtKB:Q9UBK2}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22886304, ECO:0000269|PubMed:23217713}. Nucleus, PML body {ECO:0000269|PubMed:22886304}.
| null | null | null | null | null |
FUNCTION: Transcriptional coactivator for steroid receptors and nuclear receptors (PubMed:12754525, PubMed:15744310, PubMed:23217713, PubMed:9529258). Greatly increases the transcriptional activity of PPARG and thyroid hormone receptor on the uncoupling protein promoter (PubMed:12754525, PubMed:15744310, PubMed:23217713, PubMed:9529258). Can regulate key mitochondrial genes that contribute to the program of adaptive thermogenesis (PubMed:12754525, PubMed:15744310, PubMed:23217713, PubMed:9529258). Plays an essential role in metabolic reprogramming in response to dietary availability through coordination of the expression of a wide array of genes involved in glucose and fatty acid metabolism (PubMed:12754525, PubMed:15744310, PubMed:23217713, PubMed:9529258). Acts as a key regulator of gluconeogenesis: stimulates hepatic gluconeogenesis by increasing the expression of gluconeogenic enzymes, and acting together with FOXO1 to promote the fasting gluconeogenic program (PubMed:12754525). Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner (By similarity). Also involved in the integration of the circadian rhythms and energy metabolism (PubMed:17476214). Required for oscillatory expression of clock genes, such as BMAL1 and NR1D1, through the coactivation of RORA and RORC, and metabolic genes, such as PDK4 and PEPCK (PubMed:17476214). {ECO:0000250|UniProtKB:Q9UBK2, ECO:0000269|PubMed:12754525, ECO:0000269|PubMed:15744310, ECO:0000269|PubMed:17476214, ECO:0000269|PubMed:23217713, ECO:0000269|PubMed:9529258}.
|
Mus musculus (Mouse)
|
O70344
|
KCNQ1_CAVPO
|
MAAASSPPRTERKRGGWGRLLGSRRGSASLAKKCPFSLELAEGGPAGGTLYAPVAPPGALSPGSPAPPASPAAPPAGLELGPRPPVSLDPRVSIYSARRPLLARTHIQGRVYNFLERPTGWKCFVYHFAVFLIVLACLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGIWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYADALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLIQTAWRCYAAENPDSSTWKIYVRKPARSHTLLSPSPKPKKSAMVRKKKFKPDKDNGVSPGEKMLTVPHITCDPPEERRPDHFSVDGYDSSVRKSPTLLEVSPTHFMRTNSFAEDLDLEGETLLTPITHVSQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFIPISEKSKDRGSNTIGARLNRVEDKVTQLDQRLVVITDMLHQLLSLHQGGPHSGGGPQMVQPCSEDGSIHPELFLPSNSLPTYEQLTVPQRGPDEAS
| null | null |
adrenergic receptor signaling pathway [GO:0071875]; auditory receptor cell development [GO:0060117]; cellular response to cAMP [GO:0071320]; cellular response to epinephrine stimulus [GO:0071872]; cellular response to xenobiotic stimulus [GO:0071466]; cochlea development [GO:0090102]; corticosterone secretion [GO:0035934]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; erythrocyte differentiation [GO:0030218]; gastrin-induced gastric acid secretion [GO:0001698]; glucose metabolic process [GO:0006006]; heart development [GO:0007507]; inner ear development [GO:0048839]; inner ear morphogenesis [GO:0042472]; intestinal absorption [GO:0050892]; intracellular chloride ion homeostasis [GO:0030644]; iodide transport [GO:0015705]; membrane repolarization [GO:0086009]; membrane repolarization during atrial cardiac muscle cell action potential [GO:0098914]; non-motile cilium assembly [GO:1905515]; positive regulation of cardiac muscle contraction [GO:0060452]; positive regulation of heart rate [GO:0010460]; 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]; regulation of atrial cardiac muscle cell membrane repolarization [GO:0060372]; regulation of blood pressure [GO:0008217]; regulation of gastric acid secretion [GO:0060453]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of ventricular cardiac muscle cell membrane repolarization [GO:0060307]; renal absorption [GO:0070293]; renal sodium ion absorption [GO:0070294]; response to insulin [GO:0032868]; rhythmic behavior [GO:0007622]; social behavior [GO:0035176]; stomach development [GO:0062094]
|
apical plasma membrane [GO:0016324]; basolateral part of cell [GO:1990794]; basolateral plasma membrane [GO:0016323]; ciliary base [GO:0097546]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; late endosome [GO:0005770]; lumenal side of membrane [GO:0098576]; lysosome [GO:0005764]; membrane raft [GO:0045121]; monoatomic ion channel complex [GO:0034702]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; transport vesicle [GO:0030133]; voltage-gated potassium channel complex [GO:0008076]
|
calmodulin binding [GO:0005516]; delayed rectifier potassium channel activity [GO:0005251]; outward rectifier potassium channel activity [GO:0015271]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; protein kinase A catalytic subunit binding [GO:0034236]; protein kinase A regulatory subunit binding [GO:0034237]; protein phosphatase 1 binding [GO:0008157]; scaffold protein binding [GO:0097110]; transmembrane transporter binding [GO:0044325]; voltage-gated potassium channel activity [GO:0005249]; voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization [GO:0086089]; voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization [GO:1902282]
|
PF00520;PF03520;
|
1.10.287.70;6.10.140.1910;1.20.120.350;
|
Potassium channel family, KQT (TC 1.A.1.15) subfamily, Kv7.1/KCNQ1 sub-subfamily
|
PTM: Phosphorylation at Ser-27 by PKA; increases delayed rectifier potassium channel activity of the KCNQ1-KCNE1 complex through a macromolecular complex that includes PKA, PP1, and the targeting protein AKAP9. {ECO:0000250|UniProtKB:P51787}.; PTM: Ubiquitinated by NEDD4L; promotes internalization. The ubiquitinylated form is internalized through a clathrin-mediated endocytosis by interacting with AP2M1 and is recycled back to the cell membrane via RAB4A and RAB11A. {ECO:0000250|UniProtKB:P51787}.; PTM: Deubiquitinated by USP2; counteracts the NEDD4L-specific down-regulation of I(Ks) and restores the membrane localization. {ECO:0000250|UniProtKB:P51787}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51787}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P51787}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P51787}. Early endosome {ECO:0000250|UniProtKB:P51787}. Membrane raft {ECO:0000250|UniProtKB:P51787}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P51787}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51787}. Note=Colocalized with KCNE3 at the plasma membrane. Upon 17beta-oestradiol treatment, colocalizes with RAB5A at early endosome. Heterotetramer with KCNQ5 is highly retained at the endoplasmic reticulum and is localized outside of lipid raft microdomains. During the early stages of epithelial cell polarization induced by the calcium switch it is removed from the plasma membrane to the endoplasmic reticulum, where it is retained, and redistributed to the basolateral cell surface in a PI3K-dependent manner at a later stage. {ECO:0000250|UniProtKB:P51787}.
| null | null | null | null | null |
FUNCTION: Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity). Associates with KCNE beta subunits that modulates current kinetics (By similarity). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity). Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity). During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity). Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current (By similarity). When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (By similarity). This interaction with KCNE3 is reduced by 17beta-estradiol, resulting in the reduction of currents (By similarity). During conditions of increased substrate load, maintains the driving force for proximal tubular and intestinal sodium ions absorption, gastric acid secretion, and cAMP-induced jejunal chloride ions secretion (By similarity). Allows the provision of potassium ions to the luminal membrane of the secretory canaliculus in the resting state as well as during stimulated acid secretion (By similarity). When associated with KCNE2, forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity). When associated with KCNE4, inhibits voltage-gated potassium channel activity (By similarity). When associated with KCNE5, this complex only conducts current upon strong and continued depolarization (By similarity). Also forms a heterotetramer with KCNQ5 that has a voltage-gated potassium channel activity (By similarity). Binds with phosphatidylinositol 4,5-bisphosphate (By similarity). {ECO:0000250|UniProtKB:P51787, ECO:0000250|UniProtKB:P97414, ECO:0000250|UniProtKB:Q9Z0N7}.
|
Cavia porcellus (Guinea pig)
|
O70348
|
DXO_MOUSE
|
MEPRGTKRKAEKTEVEKPLNKLPRAVPSLRTQPSLYSGPFPFYRRPSELGCFSLDAQRQYHGDARALRYYSPPPINGPGPDFDLRDGYPDRYQPRDEEVQERLDHLLRWVLEHRNQLEGGPGWLAGATVTWRGHLTKLLTTPYERQEGWQLAASRFQGTLYLSEVETPAARAQRLARPPLLRELMYMGYKFEQYMCADKPGGSPDPSGEVNTNVAYCSVLRSRLGNHPLLFSGEVDCLNPQAPCTQPPSCYVELKTSKEMHSPGQWRSFYRHKLLKWWAQSFLPGVPHVVAGFRNPEGFVCSLKTFPTMEMFENVRNDREGWNPSVCMNFCAAFLSFAQSTVVQDDPRLVHLFSWEPGGPVTVSVHRDAPYAFLPSWYVETMTQDLPPLSKTPSPKD
|
3.1.13.-; 3.6.1.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23523372, ECO:0000269|PubMed:30180947}; Note=Binds 2 magnesium ions. {ECO:0000269|PubMed:23523372, ECO:0000269|PubMed:30180947};
|
mRNA catabolic process [GO:0006402]; NAD-cap decapping [GO:0110155]; nuclear mRNA surveillance [GO:0071028]; nuclear-transcribed mRNA catabolic process [GO:0000956]; nucleic acid metabolic process [GO:0090304]; RNA destabilization [GO:0050779]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
5'-3' exonuclease activity [GO:0008409]; magnesium ion binding [GO:0000287]; mRNA 5'-diphosphatase activity [GO:0034353]; mRNA binding [GO:0003729]; nucleotide binding [GO:0000166]; RNA NAD-cap (NAD-forming) hydrolase activity [GO:0110152]
|
PF08652;
| null |
DXO/Dom3Z family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O77932}.
|
CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + diphosphate + H(+); Xref=Rhea:RHEA:78683, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:138282, ChEBI:CHEBI:167618; Evidence={ECO:0000269|PubMed:23523372}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78684; Evidence={ECO:0000269|PubMed:23523372}; CATALYTIC ACTIVITY: Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + H(+) + NAD(+); Xref=Rhea:RHEA:60880, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:15698, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:138282, ChEBI:CHEBI:144029; Evidence={ECO:0000269|PubMed:28283058, ECO:0000269|PubMed:32374864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60881; Evidence={ECO:0000269|PubMed:28283058}; CATALYTIC ACTIVITY: Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in snoRNA + H2O = a 5'-end phospho-ribonucleoside in snoRNA + H(+) + NAD(+); Xref=Rhea:RHEA:60892, Rhea:RHEA-COMP:15699, Rhea:RHEA-COMP:15700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:138282, ChEBI:CHEBI:144029; Evidence={ECO:0000269|PubMed:28283058}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60893; Evidence={ECO:0000269|PubMed:28283058}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside-ribonucleotide in mRNA + H2O = a (N(7)-methyl 5'-triphosphoguanosine)-nucleoside + a 5'-end phospho-ribonucleoside in mRNA + H(+); Xref=Rhea:RHEA:66928, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17313, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:138282, ChEBI:CHEBI:172876, ChEBI:CHEBI:172877; Evidence={ECO:0000269|PubMed:23523372}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66929; Evidence={ECO:0000269|PubMed:23523372}; CATALYTIC ACTIVITY: Reaction=a 5'-end FAD-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + FAD + H(+); Xref=Rhea:RHEA:67492, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17275, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:138282, ChEBI:CHEBI:172372; Evidence={ECO:0000269|PubMed:32374864, ECO:0000269|PubMed:32432673}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67493; Evidence={ECO:0000305|PubMed:32432673}; CATALYTIC ACTIVITY: Reaction=a 5'-end CoA-ribonucleoside in mRNA + H2O = 3'-dephospho-CoA + a 5'-end phospho-ribonucleoside in mRNA + H(+); Xref=Rhea:RHEA:67496, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57328, ChEBI:CHEBI:138282, ChEBI:CHEBI:172371; Evidence={ECO:0000305|PubMed:32374864, ECO:0000305|PubMed:32432673}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67497; Evidence={ECO:0000305|PubMed:32432673};
| null | null | null | null |
FUNCTION: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (PubMed:28283058, PubMed:32374864). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs (PubMed:28283058). In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (PubMed:28283058). Preferentially acts on NAD-capped transcripts in response to environmental stress (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs and mediates their subsequent degradation (PubMed:23523372, PubMed:28283058). Specifically degrades pre-mRNAs with a defective 5'-end m7G cap and is part of a pre-mRNA capping quality control (PubMed:23523372). Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1) (PubMed:23523372). In contrast to canonical decapping enzymes DCP2 and NUDT16, which cleave the cap within the triphosphate linkage, the decapping activity releases the entire cap structure GpppN and a 5'-end monophosphate RNA (PubMed:23523372). Also has 5'-3' exoribonuclease activities: The 5'-end monophosphate RNA is then degraded by the 5'-3' exoribonuclease activity, enabling this enzyme to decap and degrade incompletely capped mRNAs (PubMed:23523372, PubMed:30180947). Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates (PubMed:23523372). Exhibits decapping activity towards FAD-capped RNAs (PubMed:32374864, PubMed:32432673). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (PubMed:32374864, PubMed:32432673). {ECO:0000250|UniProtKB:O77932, ECO:0000269|PubMed:23523372, ECO:0000269|PubMed:28283058, ECO:0000269|PubMed:30180947, ECO:0000269|PubMed:32374864, ECO:0000269|PubMed:32432673}.
|
Mus musculus (Mouse)
|
O70351
|
HCD2_RAT
|
MAAAVRSVKGLVAVITGGASGLGLSTAKRLVGQGATAVLLDVPNSEGETEAKKLGGNCIFAPANVTSEKEVQAALTLAKEKFGRIDVAVNCAGIAVAIKTYHEKKNQVHTLEDFQRVINVNLIGTFNVIRLVAGVMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVVTIAPGLFATPLLTTLPDKVRNFLASQVPFPSRLGDPAEYAHLVQMVIENPFLNGEVIRLDGAIRMQP
|
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]; Leydig cell differentiation [GO:0033327]; male gonad development [GO:0008584]; mitochondrial tRNA 3'-end processing [GO:1990180]; mitochondrial tRNA 5'-end processing [GO:0097745]; mitochondrial tRNA methylation [GO:0070901]; mitochondrion organization [GO:0007005]; protein homotetramerization [GO:0051289]; steroid catabolic process [GO:0006706]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrial nucleoid [GO:0042645]; mitochondrial ribonuclease P complex [GO:0030678]; mitochondrion [GO:0005739]; tRNA methyltransferase complex [GO:0043527]
|
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. 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. 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. 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. 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 interacting with intracellular amyloid-beta, it may contribute to the neuronal dysfunction associated with Alzheimer disease (AD). Essential for structural and functional integrity of mitochondria. {ECO:0000250|UniProtKB:Q99714}.; 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}.
|
Rattus norvegicus (Rat)
|
O70355
|
BTNL2_MOUSE
|
MVDCPRYSLSGVAASFLFVLLTIKHPDDFRVVGPNLPILAKVGEDALLTCQLLPKRTTAHMEVRWYRSDPDMPVIMYRDGAEVTGLPMEGYGGRAEWMEDSTEEGSVALKIRQVQPSDDGQYWCRFQEGDYWRETSVLLQVAALGSSPNIHVEGLGEGEVQLVCTSRGWFPEPEVHWEGIWGEKLMSFSENHVPGEDGLFYVEDTLMVRNDSVETISCFIYSHGLRETQEATIALSERLQTELASVSVIGHSQPSPVQVGENIELTCHLSPQTDAQNLEVRWLRSRYYPAVHVYANGTHVAGEQMVEYKGRTSLVTDAIHEGKLTLQIHNARTSDEGQYRCLFGKDGVYQEARVDVQVMAVGSTPRITREVLKDGGMQLRCTSDGWFPRPHVQWRDRDGKTMPSFSEAFQQGSQELFQVETLLLVTNGSMVNVTCSISLPLGQEKTARFPLSGW
| null | null |
negative regulation of T cell receptor signaling pathway [GO:0050860]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of T cell proliferation [GO:0042102]; regulation of cytokine production [GO:0001817]; T cell receptor signaling pathway [GO:0050852]
|
external side of plasma membrane [GO:0009897]
|
signaling receptor binding [GO:0005102]
|
PF08205;PF07686;
|
2.60.40.10;
|
Immunoglobulin superfamily, BTN/MOG family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Negative regulator of T-cell proliferation. {ECO:0000269|PubMed:16751379, ECO:0000269|PubMed:17237401}.
|
Mus musculus (Mouse)
|
O70361
|
PER3_MOUSE
|
MDPCGDPAVPGGDCPQTRGPGLQGASGQEGPLQGTCVDSSHSEHEDRNRMSEELIMVVQEMKKYFPAERHTKPSTLDALNYALRCVHSVQANSDFFQSLGPRGAHQADVTVYSLEDLTALASEHTSKNTDTFAAVFSFLSGRLVHISEQAALILNSKRGFLKSVHFVDLLAPQDVRAFYAHTAPTQLPFWNNWTQRASQYECAPAKPFFCRICGGGDREKRHYSPFRILPYLVHVHSSAQPEPEPCCLTLVEKIHSGYEAPRIPVDKRIFTTTHTPGCVFLEVDERAVPLLGYLPQDLIGTSILTYLHPEDRPLMVAIHQKVLKYAGHPPFEHSPVRFCTQNGEYVILDSSWSSFVNPWSRKVSFIIGRHKVRTSPLNEDVFATRIKKAASNDKDIAELQEQIHKLLLQPVHASASSGYGSLGSSGSQEQHVSITSSSESSGHCPEEGQHEQMTLQQVYASVNKIKNVGQQLYIESMARSSVKPVAETCVEPQGGDEQKDFSSSQTLKNKSTTDTGSGGNLQQEQPSSSYQQMNCIDSVIRYLTSYSLPALKRKCISCTNTSSSSEEAKPIPEVDSSQRDTEQLLDIRKQETTGPSTDIEGGAARTLSTAALSVASGISQCSCSSTSGHAPPLQSESVAVACKPWALRTKASHLAAGGFKHVGLTAAVLSAHTQKEEQNYVDRFREKILTSPYGCYLQQESRNRAQYSCVQAGSTAKHSRCAGSERQKHKRKKLPAPVDTSSPGAHLCPHVTGLLPDEQHWGPSASPSPLGAGLAFPSALVVPSQTPYLLPSFPLQDMASQGVGVSAAWGAAAGCPPLSAGPQAVAAFPSAYVDTLMTIFLHNAPLFPLWPPSFSPYPSLGAAGSSELAPLVPAMAPNPEPTTSGHSQRRVEENWEAHSEELPFISSRSSSPLQLNLLQEEMPAPSESADAVRRGAGPDAKHHCVTGPSGSRSRHCTSGELATATAQQESAAASGSSASSIYFSSTDYASEVSENRQRPQDRQRDEALPGAAEESIWRMIERTPECVLMTYQVPERGREEVLKQDLEKLQSMEQQQPLFSPAQREELAKVRSWIHSHTAPQEGHLQSCVACEDRGSVGDTAEVLEQHPAEDTS
| null | null |
circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; entrainment of circadian clock by photoperiod [GO:0043153]; negative regulation of transcription by RNA polymerase II [GO:0000122]; protein stabilization [GO:0050821]; regulation of circadian sleep/wake cycle, sleep [GO:0045187]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
kinase binding [GO:0019900]; transcription cis-regulatory region binding [GO:0000976]; transcription corepressor binding [GO:0001222]; ubiquitin protein ligase binding [GO:0031625]
|
PF08447;PF21353;PF12114;
|
3.30.450.20;
| null |
PTM: Phosphorylation by CSNK1E is weak and appears to require association with PER1 and translocation to the nucleus. {ECO:0000269|PubMed:11865049, ECO:0000269|PubMed:14701732}.; PTM: Ubiquitinated. {ECO:0000269|PubMed:11865049}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:11591712, ECO:0000269|PubMed:11865049, ECO:0000269|PubMed:14701732}. Nucleus {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:11591712, ECO:0000269|PubMed:11865049, ECO:0000269|PubMed:14701732}. Note=Mainly cytoplasmic. Translocates to the nucleus through binding PER1, PER2, CRY1 or CRY2, but not TIMELESS. {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:11591712, ECO:0000269|PubMed:11865049, ECO:0000269|PubMed:14701732}.
| null | null | null | null | null |
FUNCTION: Originally described as 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, NR1D2, RORA, RORB and RORG, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Has a redundant role with the other PER proteins PER1 and PER2 and is not essential for the circadian rhythms maintenance. In contrast, plays an important role in sleep-wake timing and sleep homeostasis probably through the transcriptional regulation of sleep homeostasis-related genes, without influencing circadian parameters. Can bind heme. {ECO:0000269|PubMed:11395012, ECO:0000269|PubMed:21957163, ECO:0000269|PubMed:22331899}.
|
Mus musculus (Mouse)
|
O70362
|
PHLD_MOUSE
|
MSAGRLWSSLLLLLPLFCSKSSSCGLSTHVEIGHRALEFLRLQDGRINYKELILEHQDAYQAGTVFPDAFYPSICKRGKYHDVSERTHWTPFLNASIHYIRENYPLPWEKDTEKLVAFLFGITSHMVADLSWHNLGFLRTMGAIDFYNSYSDAHSAGDFGGDVLSQFEFNFNYLSRRWYVPVRDLLRIYDNLYGRKVITKDVLVDCTYLQFLEMHGEMFAVSKLYSTYSTKSPFLVEQFQDYFLGGLDDMAFWSTNIYRLTSFMLENGTSDCNLPENPLFISCDGRNHTLSGSKVQKNDFHRNLTMFISRDIRKNLNYTERGVFYSTGSWARPESVTFMYQTLERNLRLMLAGSSQKNLNHVSSPSASYTLSVPYARLGWVMTSADLNQDGHGDLVVGAPGYSHPGRFQIGRVYIIYGNDLGLPPIDLDLNKEGILEGFQPSGRFGSALAVLDFNQDGLPDLAVGAPSVGSGQLTYNGSVYVYYGSQQGRLSSSPNVTISCKDTYCNLGWTLLATDADGDGRHDLVISSPFAPGGRKQKGIVATFYSHPRRNDKELLTLEEADWKVNGEEDFSWFGYSLHGVTVANRSLLLIGSPTWKNVSRMARSSHKKNQEEKSLGKVYGYFLPNRQSTITISGDKAMGKLGTSLSSGYVRVNGTLTQVLLVGAPTHDDVSKMAFLTMTLHQGGATRMYELAPEKTQPALLSTFSGDRRFSRFGSVLHLTDLDDDGLDEIIMAAPLRITDVTSGLLGGEDGRVYIYNGMYTTLGDMTGKCKSWMTPCPEEKAQYVLTSPEASSRFGSSLVSVRSKGRNQVVVAAGRSSWGARLSGALHVYSFSSD
|
3.1.4.50
| null |
cell migration involved in sprouting angiogenesis [GO:0002042]; cellular response to calcium ion [GO:0071277]; cellular response to cholesterol [GO:0071397]; cellular response to inorganic substance [GO:0071241]; cellular response to insulin stimulus [GO:0032869]; cellular response to iron(II) ion [GO:0071282]; cellular response to pH [GO:0071467]; cellular response to triglyceride [GO:0071401]; cellular response to xenobiotic stimulus [GO:0071466]; chondrocyte differentiation [GO:0002062]; complement receptor mediated signaling pathway [GO:0002430]; GPI anchor release [GO:0006507]; insulin receptor signaling pathway [GO:0008286]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of triglyceride catabolic process [GO:0010897]; ossification [GO:0001503]; phosphatidylcholine metabolic process [GO:0046470]; positive regulation of alkaline phosphatase activity [GO:0010694]; positive regulation of apoptotic process [GO:0043065]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of glucose metabolic process [GO:0010907]; positive regulation of high-density lipoprotein particle clearance [GO:0010983]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; positive regulation of secretion [GO:0051047]; positive regulation of triglyceride biosynthetic process [GO:0010867]; regulation of cellular response to insulin stimulus [GO:1900076]; response to glucose [GO:0009749]; transepithelial transport [GO:0070633]
|
cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intracellular membrane-bounded organelle [GO:0043231]
|
glycosylphosphatidylinositol phospholipase D activity [GO:0004621]; phospholipase D activity [GO:0004630]; sodium channel regulator activity [GO:0017080]
|
PF01839;PF00882;
|
2.130.10.130;
|
GPLD1 family
| null |
SUBCELLULAR LOCATION: Secreted. Note=Associated with the High-Density Lipoproteins (HDL). {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol + a 1,2-diacyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:10832, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57997, ChEBI:CHEBI:58608, ChEBI:CHEBI:58700; EC=3.1.4.50;
| null | null | null | null |
FUNCTION: This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane. {ECO:0000269|PubMed:9716655}.
|
Mus musculus (Mouse)
|
O70370
|
CATS_MOUSE
|
MRAPGHAAIRWLFWMPLVCSVAMEQLQRDPTLDYHWDLWKKTHEKEYKDKNEEEVRRLIWEKNLKFIMIHNLEYSMGMHTYQVGMNDMGDMTNEEILCRMGALRIPRQSPKTVTFRSYSNRTLPDTVDWREKGCVTEVKYQGSCGACWAFSAVGALEGQLKLKTGKLISLSAQNLVDCSNEEKYGNKGCGGGYMTEAFQYIIDNGGIEADASYPYKATDEKCHYNSKNRAATCSRYIQLPFGDEDALKEAVATKGPVSVGIDASHSSFFFYKSGVYDDPSCTGNVNHGVLVVGYGTLDGKDYWLVKNSWGLNFGDQGYIRMARNNKNHCGIASYCSYPEI
|
3.4.22.27
| null |
antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; basement membrane disassembly [GO:0034769]; bone resorption [GO:0045453]; immune response [GO:0006955]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of cation channel activity [GO:2001259]; positive regulation of inflammatory response [GO:0050729]; proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603]
|
cell surface [GO:0009986]; early endosome lumen [GO:0031905]; extracellular space [GO:0005615]; lysosome [GO:0005764]; membrane [GO:0016020]; phagocytic vesicle [GO:0045335]
|
cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; peptidase activity [GO:0008233]
|
PF08246;PF00112;
|
3.90.70.10;
|
Peptidase C1 family
| null |
SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P25774}. Secreted {ECO:0000250|UniProtKB:P25774}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:P25774}.
|
CATALYTIC ACTIVITY: Reaction=Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val-Arg-|-Xaa compound.; EC=3.4.22.27;
| null | null | null | null |
FUNCTION: Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules and MHC class II antigen presentation. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L. {ECO:0000250|UniProtKB:P25774}.
|
Mus musculus (Mouse)
|
O70372
|
TERT_MOUSE
|
MTRAPRCPAVRSLLRSRYREVWPLATFVRRLGPEGRRLVQPGDPKIYRTLVAQCLVCMHWGSQPPPADLSFHQVSSLKELVARVVQRLCERNERNVLAFGFELLNEARGGPPMAFTSSVRSYLPNTVIETLRVSGAWMLLLSRVGDDLLVYLLAHCALYLLVPPSCAYQVCGSPLYQICATTDIWPSVSASYRPTRPVGRNFTNLRFLQQIKSSSRQEAPKPLALPSRGTKRHLSLTSTSVPSAKKARCYPVPRVEEGPHRQVLPTPSGKSWVPSPARSPEVPTAEKDLSSKGKVSDLSLSGSVCCKHKPSSTSLLSPPRQNAFQLRPFIETRHFLYSRGDGQERLNPSFLLSNLQPNLTGARRLVEIIFLGSRPRTSGPLCRTHRLSRRYWQMRPLFQQLLVNHAECQYVRLLRSHCRFRTANQQVTDALNTSPPHLMDLLRLHSSPWQVYGFLRACLCKVVSASLWGTRHNERRFFKNLKKFISLGKYGKLSLQELMWKMKVEDCHWLRSSPGKDRVPAAEHRLRERILATFLFWLMDTYVVQLLRSFFYITESTFQKNRLFFYRKSVWSKLQSIGVRQHLERVRLRELSQEEVRHHQDTWLAMPICRLRFIPKPNGLRPIVNMSYSMGTRALGRRKQAQHFTQRLKTLFSMLNYERTKHPHLMGSSVLGMNDIYRTWRAFVLRVRALDQTPRMYFVKADVTGAYDAIPQGKLVEVVANMIRHSESTYCIRQYAVVRRDSQGQVHKSFRRQVTTLSDLQPYMGQFLKHLQDSDASALRNSVVIEQSISMNESSSSLFDFFLHFLRHSVVKIGDRCYTQCQGIPQGSSLSTLLCSLCFGDMENKLFAEVQRDGLLLRFVDDFLLVTPHLDQAKTFLSTLVHGVPEYGCMINLQKTVVNFPVEPGTLGGAAPYQLPAHCLFPWCGLLLDTQTLEVFCDYSGYAQTSIKTSLTFQSVFKAGKTMRNKLLSVLRLKCHGLFLDLQVNSLQTVCINIYKIFLLQAYRFHACVIQLPFDQRVRKNLTFFLGIISSQASCCYAILKVKNPGMTLKASGSFPPEAAHWLCYQAFLLKLAAHSVIYKCLLGPLRTAQKLLCRKLPEATMTILKAAADPALSTDFQTILD
|
2.7.7.49
| null |
cellular response to hypoxia [GO:0071456]; DNA strand elongation [GO:0022616]; establishment of protein localization to telomere [GO:0070200]; mitochondrion organization [GO:0007005]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cellular senescence [GO:2000773]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of glial cell proliferation [GO:0060253]; negative regulation of neuron apoptotic process [GO:0043524]; positive regulation of angiogenesis [GO:0045766]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of glucose import [GO:0046326]; positive regulation of hair cycle [GO:0042635]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of protein localization to nucleolus [GO:1904751]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of transdifferentiation [GO:1903620]; positive regulation of vascular associated smooth muscle cell migration [GO:1904754]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; positive regulation of Wnt signaling pathway [GO:0030177]; regulation of protein stability [GO:0031647]; replicative senescence [GO:0090399]; response to cadmium ion [GO:0046686]; siRNA processing [GO:0030422]; siRNA transcription [GO:0140745]; telomere maintenance via telomerase [GO:0007004]
|
chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]; PML body [GO:0016605]; telomerase catalytic core complex [GO:0000333]; telomerase holoenzyme complex [GO:0005697]; TERT-RMRP complex [GO:1990572]
|
metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein-folding chaperone binding [GO:0051087]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968]; telomerase activity [GO:0003720]; telomerase RNA binding [GO:0070034]; telomerase RNA reverse transcriptase activity [GO:0003721]; telomeric DNA binding [GO:0042162]; template-free RNA nucleotidyltransferase [GO:0098680]; transcription coactivator binding [GO:0001223]; tRNA binding [GO:0000049]
|
PF00078;PF12009;PF21399;
|
1.10.132.70;1.10.357.90;3.30.70.2630;
|
Reverse transcriptase family, Telomerase subfamily
|
PTM: Phosphorylation at Tyr-697 under oxidative stress leads to translocation of TERT to the cytoplasm and reduces its antiapoptotic activity. Dephosphorylated by SHP2/PTPN11 leading to nuclear retention. Phosphorylation by the AKT pathway promotes nuclear location. Phosphorylation at the G2/M phase at Ser-447 by DYRK2 promotes ubiquitination by the EDVP complex and degradation (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by the EDVP complex, a E3 ligase complex following phosphorylation at Ser-447 by DYRK2. Ubiquitinated leads to proteasomal degradation (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:O14746}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus. Chromosome, telomere. Cytoplasm {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Note=Shuttling between nuclear and cytoplasm depends on cell cycle, phosphorylation states, transformation and DNA damage. Diffuse localization in the nucleoplasm. Enriched in nucleoli of certain cell types. Translocated to the cytoplasm via nuclear pores in a CRM1/RAN-dependent manner involving oxidative stress-mediated phosphorylation at Tyr-697. Dephosphorylation at this site by SHP2 retains TERT in the nucleus. Translocated to the nucleus by phosphorylation by AKT (By similarity). {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
| null | null | null | null |
FUNCTION: Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:17130244, ECO:0000269|PubMed:19571879, ECO:0000269|PubMed:9582020}.
|
Mus musculus (Mouse)
|
O70373
|
XIRP1_MOUSE
|
MADAQMQVAPTPTIQMRTEEDLSLPHPSAPEGLPPPPPKETFSKFQQQRQASELRRLYKHIHPELRKNLEEAVAEDLAEVLGSEEPTEGDVQCMRWIFENWRLDAIGDHERPAAREPVSGGNVQATSRKFEEGSFTNSSDQEPEGLRPSGGDVQAARQMFETKPLDALRGQEEATQTTMREPAATGDVQGTRKLFETRPLDRLGSRPSIQEQSPLELRSEIQELKGDVKKTVKLFQTEPLCAIQDAEGTIHEVKAACREEIQSNAVRSARWLFETRPLDAFNQDPSQVRVIRGISLEEGALPDVSATRWIFETQPLDAIREIEVDEKDFQPSPDLIPPGPDVQHQRHLFETCSLDTLKGERETEAEVPPKEEVIPGDVRSTLWLFETKPLDAFRDQVQVGHLQRVGHQEGEGLVTECLPSNGTSVLPLSQGVPQNDGLKGDVKTFKNLFETLPLDSIGQGEPSAYGNINRGQNTDSAEQSQGSDAPVYAMQDSRGQLHALTSVSREQVVGGDVQGYKWMFETQPLDTLGRSPSTIDVVRGITRQEVVAGDVGTTRWLFETQPLEMIHQQEQQKPEEEEGKGPGGPPPELPKKGDVQTIRWLFETYPMSELAEKRESEVTDPVSKAETQSCTWMFGPQSLNPAEGSGEQHLQTSQVPAGDRQTDRHVFETESLPASNQSSGRKPVRYCSRVEIPSGQVSRQKEVFQALEAGKKEVPETTINLGSIPTGSVHKFTWLFENCPMGSLAAESIRGDNLQEEQPKGSAGHGTPERQETAAERTLRTLHATPGILHHGGILMEARGPGELCLAKYVLPSPGQGRPYIRKEELVCGELPRIVRQVLRRTDVDQQGLLVQEDTAGQLQLHPLMLPGPGDPGNIEDMDPELQQLLACGLGVSVSKTGLVMQETGQGLVALTAYSLQPQLTSRAPERSSVQLLASCIDKGDLHSLHSLRWEPPTDPSSGPATEESQRVPPTESIIHVTPLDSTMEMGQLRISGSTPCPPPSRAAGKVVLPNGKPVAQAPLQEARKKRDISHAGQKGKAASGRPEASPLGSGAPDLQEAMQNLRLATAEAQSLHQQVLSRHPQGSDPVATSMPVQDVLQASTPATGVTQGSIRPVAGSEARIPAVPRKLL
| null | null |
actin filament organization [GO:0007015]; cardiac muscle cell development [GO:0055013]; heart morphogenesis [GO:0003007]; negative regulation of cell population proliferation [GO:0008285]; Notch signaling pathway [GO:0007219]; regulation of membrane potential [GO:0042391]; sarcomere organization [GO:0045214]
|
adherens junction [GO:0005912]; fascia adherens [GO:0005916]; focal adhesion [GO:0005925]; intercalated disc [GO:0014704]; stress fiber [GO:0001725]
|
actin filament binding [GO:0051015]; filamin binding [GO:0031005]
|
PF08043;
| null |
Xin family
| null |
SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250|UniProtKB:Q5PZ43}. Cell junction, desmosome {ECO:0000250|UniProtKB:Q5PZ43}. Note=Colocalizes with actin stress fibers. {ECO:0000250|UniProtKB:Q702N8}.
| null | null | null | null | null |
FUNCTION: Protects actin filaments from depolymerization (By similarity). Required for correct cardiac intercalated disk ultrastructure via maintenance of cell-cell adhesion stability, and as a result maintains cardiac organ morphology, conductance and heat beat rhythm (PubMed:17766470). {ECO:0000250|UniProtKB:Q702N8, ECO:0000269|PubMed:17766470}.
|
Mus musculus (Mouse)
|
O70374
|
MTG8R_MOUSE
|
MVGVPGAAAFQLGCEKRVPAMPGSPVEVKIQSRSSPPIMPPLPPINPGGPRPVSFTPTALSNGINHSPPTLNGAPSPPQRFSNGPASSTSSALTNQQLPATCGARQLSKLKRFLTTLQQFGNDISPEIGEKVRTLVLALVNSTVTIEEFHCKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARAAKQTPSQYLAQHEHLLLNTSIASPADSSELLMEVHGNGKRPSPERRDENNFERDTVPPEPPAKRVCTISPAPRHSPALTVPLMNPGGQFHPTPPPLQHYTLEDIATSHLYREPNKMLEHREVRERHHNLSLNGGYQDELVDHRLTEREWADEWKHLDHALNCIMEMVEKTRRSMAVLRRCQESDREELNYWKRRFNENTELRKTGTELVSRQHSPGSTDSLSNDSQREFTSRPATGYVPVEFWKKTEEAVNKVKIQAMSEVQKAVAEAEQKAFEVIATERARMEQTIADVKRQAAEDAFLVINEQEESTENCWNCGRKASETCSGCNIARYCGSFCQHKDWERHHRLCGQSLHGHSPHSQSRPLLPGGRGSARSADCSVPSPALDKTSATTSRSSTPASVTAIDANGL
| null | null |
DNA-templated transcription [GO:0006351]; epithelial cell differentiation [GO:0030855]; intestinal epithelial cell differentiation [GO:0060575]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of neuron projection development [GO:0010977]; negative regulation of Notch signaling pathway [GO:0045746]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of neuron projection development [GO:0010976]
|
nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714]
|
PF08788;PF07531;PF01753;
|
6.10.140.2220;6.10.250.230;1.20.120.1110;
|
CBFA2T family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00440}.
| null | null | null | null | null |
FUNCTION: Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes. Via association with PRDM14 is involved in regulation of embryonic stem cell (ESC) pluripotency. Involved in primordial germ cell (PCG) formation (PubMed:27281218). Stabilizes PRDM14 and OCT4 on chromatin in a homooligomerization-dependent mannerCan repress the expression of MMP7 in a ZBTB33-dependent manner (By similarity). Through heteromerization with CBFA2T3/MTG16 may be involved in regulation of the proliferation and the differentiation of erythroid progenitors by repressing the expression of TAL1 target genes (PubMed:19799863). Required for the maintenance of the secretory cell lineage in the small intestine (PubMed:16227606). Can inhibit Notch signaling probably by association with RBPJ and may be involved in GFI1-mediated Paneth cell differentiation (PubMed:25398765). {ECO:0000250|UniProtKB:O43439, ECO:0000269|PubMed:16227606, ECO:0000269|PubMed:25398765, ECO:0000269|PubMed:27281218}.
|
Mus musculus (Mouse)
|
O70377
|
SNP23_RAT
|
MDDLSPEEIQLRAHQVTDESLESTRRILGLAIESQDAGIKTITMLDEQGEQLNRIEEGMDQINKDMREAEKTLTELNKCCGLCVCPCNRTKNFESGKNYKATWGDGGDSSPSNVVSKQPSRITNGQPQQTTGAASGGYIKRITNDAREDEMEENLTQVGSILGNLKNMALDMGNEIDAQNQQIQKITEKADTNKNRIDIANTRAKKLIDS
| null | null |
exocytic insertion of neurotransmitter receptor to postsynaptic membrane [GO:0098967]; exocytosis [GO:0006887]; histamine secretion by mast cell [GO:0002553]; membrane fusion [GO:0061025]; protein-containing complex assembly [GO:0065003]; regulation of exocytosis [GO:0017157]; synaptic vesicle fusion to presynaptic active zone membrane [GO:0031629]; synaptic vesicle priming [GO:0016082]; vesicle-mediated transport [GO:0016192]; vesicle-mediated transport in synapse [GO:0099003]
|
adherens junction [GO:0005912]; azurophil granule [GO:0042582]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle membrane [GO:0030659]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; SNARE complex [GO:0031201]; specific granule [GO:0042581]; synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex [GO:0070032]; terminal bouton [GO:0043195]
|
SNAP receptor activity [GO:0005484]; syntaxin binding [GO:0019905]; syntaxin-1 binding [GO:0017075]
|
PF00835;
|
1.20.5.110;
|
SNAP-25 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Mainly localized to the plasma membrane. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion. {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O70394
|
I27RA_MOUSE
|
MNRLRVARLTPLELLLSLMSLLLGTRPHGSPGPLQCYSVGPLGILNCSWEPLGDLETPPVLYHQSQKYHPNRVWEVKVPSKQSWVTIPREQFTMADKLLIWGTQKGRPLWSSVSVNLETQMKPDTPQIFSQVDISEEATLEATVQWAPPVWPPQKVLICQFRYKECQAETWTRLEPQLKTDGLTPVEMQNLEPGTCYQVSGRCQVENGYPWGEWSSPLSFQTPFLDPEDVWVSGTVCETSGKRAALLVWKDPRPCVQVTYTVWFGAGDITTTQEEVPCCKSPVPAWMEWAVVSPGNSTSWVPPTNLSLVCLAPESAPCDVGVSSADGSPGIKVTWKQGTRKPLEYVVDWAQDGDSLDKLNWTRLPPGNLSTLLPGEFKGGVPYRITVTAVYSGGLAAAPSVWGFREELVPLAGPAVWRLPDDPPGTPVVAWGEVPRHQLRGQATHYTFCIQSRGLSTVCRNVSSQTQTATLPNLHLGSFKLWVTVSTVAGQGPPGPNLSLHLPDNRIRWKALPWFLSLWGLLLMGCGLSLASTRCLQARCLHWRHKLLPQWIWERVPDPANSNSGQPYIKEVSLPQPPKDGPILEVEEVELQPVVESPKASAPIYSGYEKHFLPTPEELGLLV
| null | null |
cytokine-mediated signaling pathway [GO:0019221]; defense response to Gram-positive bacterium [GO:0050830]; negative regulation of cellular extravasation [GO:0002692]; negative regulation of interleukin-17 production [GO:0032700]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of T cell extravasation [GO:2000408]; negative regulation of T-helper 17 type immune response [GO:2000317]; negative regulation of tumor necrosis factor production [GO:0032720]; negative regulation of type 2 immune response [GO:0002829]; positive regulation of T-helper 1 type immune response [GO:0002827]; positive regulation of type II interferon production [GO:0032729]; regulation of isotype switching to IgG isotypes [GO:0048302]
|
cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
cytokine binding [GO:0019955]; interleukin-27 receptor activity [GO:0045509]
| null |
2.60.40.10;
|
Type I cytokine receptor family, Type 2 subfamily
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor for IL27. Requires IL6ST/GP130 to mediate signal transduction in response to IL27. This signaling system acts through STAT3 and STAT1. Involved in the regulation of Th1-type immune responses. Also appears to be involved in innate defense mechanisms.
|
Mus musculus (Mouse)
|
O70397
|
P2RX2_CAVPO
|
MAATHPKAPTAQRLRQGWSAFWDYETPKVIVVRNRPLGVVYRAVQLLILLYFVWYVFIVQKSYQDSETGPESSIITKVKGITQSEHKVWDVEEYVKPPEGGSVFSIITRIEVTPFQTLGACPESIRVPNTTCHLDADCTAGELDMLGNGLRTGRCVPYYHGEAKTCEVSGWCPVEDGAAVSHFLGKMAPNFTILIKNSIHYPKFQFSKGNIAHRDMTYLRRCTFDQGFDPYCPIFRLGFIVEQAGENFTELAHRGGVIGVIINWDCDLDLPSSHCNPKYSFRRLDPKHVPASSGYNFRFAKYYRVNSTTTRTLIKAYGIRIDVIVHGQAGKFSLIPTIINLATALTSIGVGSFLCDWILLTFMNKNKVYSHKKFDKVCAPSRPSSSWPVTLALILGQAPPPPRHCSSPWHLAHQAVGPQGAEQAKLLGLQNPTPYRLSEQIADTPDRCVGQGLPSSESPLQDSTPTDPKGLAQL
| null | null |
calcium ion transmembrane transport [GO:0070588]; response to ATP [GO:0033198]; sensory perception of sound [GO:0007605]
|
apical plasma membrane [GO:0016324]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; extracellularly ATP-gated monoatomic cation channel activity [GO:0004931]; purinergic nucleotide receptor activity [GO:0001614]
|
PF00864;
|
1.10.287.940;2.60.490.10;
|
P2X receptor family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UBL9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P56373}.
|
CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q9UBL9}; CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P49653}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P49653};
| null | null | null | null |
FUNCTION: ATP-gated nonselective transmembrane cation channel permeable to potassium, sodium and calcium (By similarity). Activation by extracellular ATP induces a variety of cellular responses, such as excitatory postsynaptic responses in sensory neurons, neuromuscular junctions (NMJ) formation, hearing, perception of taste and peristalsis. In the inner ear, regulates sound transduction and auditory neurotransmission, outer hair cell electromotility, inner ear gap junctions, and K(+) recycling. Mediates synaptic transmission between neurons and from neurons to smooth muscle (By similarity). {ECO:0000250|UniProtKB:Q8K3P1, ECO:0000250|UniProtKB:Q9UBL9}.
|
Cavia porcellus (Guinea pig)
|
O70400
|
PDLI1_MOUSE
|
MTTQQIVLQGPGPWGFRLVGGKDFEQPLAISRVTPGSKAAIANLCIGDLITAIDGEDTSSMTHLEAQNKIKGCADNMTLTVSRSEQKIWSPLVTEEGKRHPYKMNLASEPQEVLHIGSAHNRSAMPFTASPAPSTRVITNQYNSPTGLYSSENISNFNNAVESKTSASGEEANSRPVVQPHPSGSLIIDKDSEVYKMLQEKQELNEPPKQSTSFLVLQEILESDGKGDPNKPSGFRSVKAPVTKVAASVGNAQKLPICDKCGTGIVGVFVKLRDHHRHPECYVCTDCGINLKQKGHFFVEDQIYCEKHARERVTPPEGYDVVTVFRE
| null | null |
actin cytoskeleton organization [GO:0030036]; establishment or maintenance of actin cytoskeleton polarity [GO:0030950]; fibroblast migration [GO:0010761]; heart development [GO:0007507]; maintenance of cell polarity [GO:0030011]; muscle structure development [GO:0061061]; regulation of transcription by RNA polymerase II [GO:0006357]; response to hypoxia [GO:0001666]; stress fiber assembly [GO:0043149]
|
actin cytoskeleton [GO:0015629]; adherens junction [GO:0005912]; cytoplasm [GO:0005737]; filamentous actin [GO:0031941]; stress fiber [GO:0001725]; transcription regulator complex [GO:0005667]; Z disc [GO:0030018]
|
actin binding [GO:0003779]; metal ion binding [GO:0046872]; muscle alpha-actinin binding [GO:0051371]; transcription coactivator activity [GO:0003713]
|
PF15936;PF00412;PF00595;
|
2.30.42.10;2.10.110.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11596114}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O00151}. Note=Associates with the actin stress fibers (PubMed:11596114).
| null | null | null | null | null |
FUNCTION: Cytoskeletal protein that may act as an adapter that brings other proteins (like kinases) to the cytoskeleton (By similarity). Involved in assembly, disassembly and directioning of stress fibers in fibroblasts. Required for the localization of ACTN1 and PALLD to stress fibers. Required for cell migration and in maintaining cell polarity of fibroblasts (By similarity). {ECO:0000250|UniProtKB:O00151, ECO:0000250|UniProtKB:P52944}.
|
Mus musculus (Mouse)
|
O70404
|
VAMP8_MOUSE
|
MEEASGSAGNDRVRNLQSEVEGVKNIMTQNVERILSRGENLDHLRNKTEDLEATSEHFKTTSQKVARKFWWKNVKMIVIICVIVLIIVILIILFATGTIPT
| null | null |
autophagosome maturation [GO:0097352]; cellular response to type II interferon [GO:0071346]; defense response to virus [GO:0051607]; establishment of localization in cell [GO:0051649]; membrane fusion [GO:0061025]; mucus secretion [GO:0070254]; positive regulation of pancreatic amylase secretion [GO:1902278]; protein transport [GO:0015031]; protein-containing complex assembly [GO:0065003]; regulation of endocytosis [GO:0030100]; SNARE complex assembly [GO:0035493]; symbiont entry into host cell [GO:0046718]; vesicle fusion [GO:0006906]; vesicle-mediated transport [GO:0016192]; zymogen granule exocytosis [GO:0070625]
|
basal part of cell [GO:0045178]; basolateral part of cell [GO:1990794]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; midbody [GO:0030496]; mitochondrion [GO:0005739]; mucin granule [GO:0098594]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; secretory granule [GO:0030141]; SNARE complex [GO:0031201]; zymogen granule [GO:0042588]; zymogen granule membrane [GO:0042589]
|
SNAP receptor activity [GO:0005484]; syntaxin binding [GO:0019905]
|
PF00957;
|
1.20.5.110;
|
Synaptobrevin family
| null |
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:27628032}; Single-pass type IV membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:Q9WUF4}; Single-pass type IV membrane protein {ECO:0000305}. Early endosome membrane {ECO:0000250|UniProtKB:Q9WUF4}; Single-pass type IV membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:22118466}; Single-pass type IV membrane protein {ECO:0000305}. Zymogen granule membrane {ECO:0000269|PubMed:15363411}; Single-pass type IV membrane protein {ECO:0000305}. Note=Perinuclear vesicular structures of the early and late endosomes, coated pits, and trans-Golgi (By similarity). Sub-tight junctional domain in retinal pigment epithelium cells (By similarity). Midbody region during cytokinesis (By similarity). Lumenal oriented, apical membranes of nephric tubular cell (By similarity). Cycles through the apical but not through the basolateral plasma membrane (By similarity). Apical region of acinar cells; in zymogen granule membranes (PubMed:15363411). {ECO:0000250|UniProtKB:Q9WUF4, ECO:0000269|PubMed:15363411, ECO:0000269|PubMed:9614193}.
| null | null | null | null | null |
FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane via its interaction with the STX17-SNAP29 binary t-SNARE complex (By similarity). Also required for dense-granule secretion in platelets (By similarity). Also plays a role in regulated enzyme secretion in pancreatic acinar cells (PubMed:15363411). Involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells (By similarity). Involved in the homotypic fusion of early and late endosomes (By similarity). Participates also in the activation of type I interferon antiviral response through a TRIM6-dependent mechanism (By similarity). {ECO:0000250|UniProtKB:Q9BV40, ECO:0000269|PubMed:15363411, ECO:0000269|PubMed:22118466}.
|
Mus musculus (Mouse)
|
O70405
|
ULK1_MOUSE
|
MEPGRGGVETVGKFEFSRKDLIGHGAFAVVFKGRHREKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEMANSVYLVMEYCNGGDLADYLHTMRTLSEDTVRLFLQQIAGAMRLLHSKGIIHRDLKPQNILLSNPGGRRANPSNIRVKIADFGFARYLQSNMMAATLCGSPMYMAPEVIMSQHYDGKADLWSIGTIVYQCLTGKAPFQASSPQDLRLFYEKNKTLVPAIPRETSAPLRQLLLALLQRNHKDRMDFDEFFHHPFLDASTPIKKSPPVPVPSYPSSGSGSSSSSSSASHLASPPSLGEMPQLQKTLTSPADAAGFLQGSRDSGGSSKDSCDTDDFVMVPAQFPGDLVAEAASAKPPPDSLLCSGSSLVASAGLESHGRTPSPSPTCSSSPSPSGRPGPFSSNRYGASVPIPVPTQVHNYQRIEQNLQSPTQQQTARSSAIRRSGSTTPLGFGRASPSPPSHTDGAMLARKLSLGGGRPYTPSPQVGTIPERPSWSRVPSPQGADVRVGRSPRPGSSVPEHSPRTTGLGCRLHSAPNLSDFHVVRPKLPKPPTDPLGATFSPPQTSAPQPCPGLQSCRPLRGSPKLPDFLQRSPLPPILGSPTKAGPSFDFPKTPSSQNLLTLLARQGVVMTPPRNRTLPDLSEASPFHGQQLGSGLRPAEDTRGPFGRSFSTSRITDLLLKAAFGTQASDSGSTDSLQEKPMEIAPSAGFGGTLHPGARGGGASSPAPVVFTVGSPPSGATPPQSTRTRMFSVGSSSSLGSTGSSSARHLVPGACGEAPELSAPGHCCSLADPLAANLEGAVTFEAPDLPEETLMEQEHTETLHSLRFTLAFAQQVLEIAALKGSASEAAGGPEYQLQESVVADQISQLSREWGFAEQLVLYLKVAELLSSGLQTAIDQIRAGKLCLSSTVKQVVRRLNELYKASVVSCQGLSLRLQRFFLDKQRLLDGIHGVTAERLILSHAVQMVQSAALDEMFQHREGCVPRYHKALLLLEGLQHTLTDQADIENIAKCKLCIERRLSALLSGVYA
|
2.7.11.1
| null |
autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; axon extension [GO:0048675]; axonogenesis [GO:0007409]; cellular response to amino acid starvation [GO:0034198]; cellular response to nutrient levels [GO:0031669]; cerebellar granule cell differentiation [GO:0021707]; collateral sprouting [GO:0048668]; establishment of localization in cell [GO:0051649]; macroautophagy [GO:0016236]; mitophagy [GO:0000423]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of collateral sprouting [GO:0048671]; neuron migration [GO:0001764]; neuron projection development [GO:0031175]; neuron projection regeneration [GO:0031102]; peptidyl-serine phosphorylation [GO:0018105]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of autophagosome assembly [GO:2000786]; positive regulation of autophagy [GO:0010508]; protein localization [GO:0008104]; radial glia guided migration of cerebellar granule cell [GO:0021933]; Ras protein signal transduction [GO:0007265]; receptor internalization [GO:0031623]; regulation of gene expression [GO:0010468]; regulation of neurotrophin TRK receptor signaling pathway [GO:0051386]; regulation of protein lipidation [GO:1903059]; response to mitochondrial depolarisation [GO:0098780]; response to starvation [GO:0042594]; reticulophagy [GO:0061709]
|
Atg1/ULK1 kinase complex [GO:1990316]; autophagosome [GO:0005776]; axon [GO:0030424]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; membrane [GO:0016020]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045]
|
ATP binding [GO:0005524]; Hsp90 protein binding [GO:0051879]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF12063;PF21127;PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily
|
PTM: Autophosphorylated. Phosphorylated under nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. In response to nutrient limitation, phosphorylated and activated by AMPK, leading to activate autophagy. Under nutrient sufficiency, phosphorylated by MTOR/mTOR, disrupting the interaction with AMPK and preventing activation of ULK1. {ECO:0000269|PubMed:19258318, ECO:0000269|PubMed:21205641, ECO:0000269|PubMed:21258367}.; PTM: Ubiquitinated via 'Lys-63'-linkage by a complex composed of AMBRA1 and TRAF6 following autophagy induction, promoting ULK1 stability and kinase activity. Deubiquitinated by USP20; leading to ULK1 stability and autophagy initiation. {ECO:0000250|UniProtKB:O75385}.; PTM: Acetylated by KAT5/TIP60 under autophagy induction, promoting protein kinase activity. {ECO:0000269|PubMed:22539723}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19258318}. Preautophagosomal structure {ECO:0000269|PubMed:19258318}. Note=Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome.
|
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:0000305|PubMed:22539723, ECO:0000305|PubMed:25723488}; 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:0000305|PubMed:22539723};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase involved in autophagy in response to starvation (PubMed:10624947, PubMed:19258318, PubMed:21205641, PubMed:21258367, PubMed:21460634, PubMed:25040165, PubMed:25723488). Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes (PubMed:10624947, PubMed:19258318, PubMed:21205641, PubMed:21258367, PubMed:21460634, PubMed:25040165). Part of regulatory feedback loops in autophagy: acts both as a downstream effector and negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR (PubMed:21205641, PubMed:21258367). Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity (PubMed:21460634). May phosphorylate ATG13/KIAA0652 and RPTOR; however such data need additional evidences (PubMed:19258318). Plays a role early in neuronal differentiation and is required for granule cell axon formation (By similarity). Also phosphorylates SESN2 and SQSTM1 to regulate autophagy (PubMed:25040165, PubMed:25723488). Phosphorylates FLCN, promoting autophagy (By similarity). Phosphorylates AMBRA1 in response to autophagy induction, releasing AMBRA1 from the cytoskeletal docking site to induce autophagosome nucleation (By similarity). Phosphorylates ATG4B, leading to inhibit autophagy by decreasing both proteolytic activation and delipidation activities of ATG4B (By similarity). {ECO:0000250|UniProtKB:O75385, ECO:0000269|PubMed:10624947, ECO:0000269|PubMed:19258318, ECO:0000269|PubMed:21205641, ECO:0000269|PubMed:21258367, ECO:0000269|PubMed:21460634, ECO:0000269|PubMed:25040165, ECO:0000269|PubMed:25723488}.
|
Mus musculus (Mouse)
|
O70418
|
RN112_RAT
|
MPRPVLSVTAFCHRLGKRESKRSFMGNSSNSWSHASFPKLELGLGQRPSPPRESPTCSICLERLREPISLDCGHDFCIRCFSTHRIPGCELPCCPECRKICKQKKGLRSLGERMKLLPQRPLPPALQETCAVRAERLLLVRINASGGLILRMGAINRCLKHPLARDTPVCLLAVLGEQHSGKSFLLDHLLRGLPGLESGDSTRPRAEGSLPGIRWGANGLTRGIWMWSHPFLLGKEGKKVAVFLVDTGDVMSPELSRETRVKLCALTMMLSSYQILNTSQELKDTDLGYLEMFVHVAEVMGKHYGMVPIQHLDLLVRDSSHHNKSGQGHVGDILQKLSGKYPKVQELLLGKRARCYLLPAPERQWVNKGQASPGGNTEDDFSHHFRAYISDVLSTAPQHAKSRCQGYWSEGRAMARGDRRLLTGQQLAQEIKNLSGWMGKSGPSFSSPDEMAAQLHDLRKVEAAKKEFEEYVRQQDIATKRIFSALRVLPDTMRNLLSTQKDAILARHGVALLCKEREQTLEALEAELQAEAKAFMDSYTMRFCGHLAAVGGAVGAGLMGLAGGVVGAGMAAAALAAEAGMVAAGAAVGATGAAVVGGGVGAGLAATVGCMEKEEDERVQGGDREPLLQEE
|
2.3.2.27
| null |
embryonic brain development [GO:1990403]; endoplasmic reticulum organization [GO:0007029]; G1 to G0 transition involved in cell differentiation [GO:0070315]; neuron differentiation [GO:0030182]; positive regulation of glial cell differentiation [GO:0045687]; positive regulation of neuron differentiation [GO:0045666]; protein autoubiquitination [GO:0051865]; protein homooligomerization [GO:0051260]; regulation of cell cycle [GO:0051726]; response to hydroperoxide [GO:0033194]
|
cell body [GO:0044297]; cytoplasm [GO:0005737]; endosome [GO:0005768]; membrane [GO:0016020]; neuron projection [GO:0043005]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perikaryon [GO:0043204]; postsynaptic density [GO:0014069]; synaptic vesicle [GO:0008021]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein self-association [GO:0043621]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
|
PF02263;PF00097;
|
3.40.50.300;3.30.40.10;
|
TRAFAC class dynamin-like GTPase superfamily, GB1/RHD3 GTPase family, GB1 subfamily
|
PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q96DY5}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q96DY5}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000250|UniProtKB:Q96DY5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96DY5}. Cytoplasm {ECO:0000250|UniProtKB:Q96DY5}. Nucleus {ECO:0000250|UniProtKB:Q96DY5}. Nucleus, nuclear body {ECO:0000250|UniProtKB:Q96DY5}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q96DY5}. Endosome {ECO:0000250|UniProtKB:Q96DY5}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q96DY5}. Postsynaptic density {ECO:0000250|UniProtKB:Q96DY5}. Perikaryon {ECO:0000250|UniProtKB:Q96DY5}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q96DY5}. Note=Predominantly in the nucleus, but some amounts were also found in the cytoplasm. Oxidative stress stimulates its shuttling from the cytoplasm into the nucleus. Recruited to nuclear bodies via its interaction with ZBTB16. Localizes to the cell soma and neuritis and only slightly to the nucleus in the neurons of most brain areas. {ECO:0000250|UniProtKB:Q96DY5}.
|
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:0000305};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase that plays an important role in neuronal differentiation, including neurogenesis and gliogenesis, during brain development. During embryonic development initiates neuronal differentiation by inducing cell cycle arrest at the G0/G1 phase through up-regulation of cell-cycle regulatory proteins. Plays a role not only in the fetal period during the development of the nervous system, but also in the adult brain, where it is involved in the maintenance of neural functions and protection of the nervous tissue cells from oxidative stress-induced damage. Exhibits GTPase and E3 ubiquitin-protein ligase activities. Regulates dendritic spine density and synaptic neurotransmission; its ability to hydrolyze GTP is involved in the maintenance of dendritic spine density. {ECO:0000250|UniProtKB:Q96DY5}.
|
Rattus norvegicus (Rat)
|
O70421
|
FZD1_MOUSE
|
MAEEAAPSESRAAGRLSLELCAEALPGRREEVGHEDTASHRRPRADPRRWASGLLLLLWLLEAPLLLGVRAQAAGQVSGPGQQAPPPPQPQQSGQQYNGERGISIPDHGYCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVCTVLEQALPPCRSLCERARQGCEALMNKFGFQWPDTLKCEKFPVHGAGELCVGQNTSDKGTPTPSLLPEFWTSNPQHGGGGYRGGYPGGAGTVERGKFSCPRALRVPSYLNYHFLGEKDCGAPCEPTKVYGLMYFGPEELRFSRTWIGIWSVLCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYTAVAVAYIAGFLLEDRVVCNDKFAEDGARTVAQGTKKEGCTILFMMLYFFSMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAIKTITILALGQVDGDVLSGVCFVGLNNVDALRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVLYTVPATIVIACYFYEQAFRDQWERSWVAQSCKSYAIPCPHLQGGGGVPPHPPMSPDFTVFMIKYLMTLIVGITSGFWIWSGKTLNSWRKFYTRLTNSKQGETTV
| null | null |
astrocyte-dopaminergic neuron signaling [GO:0036520]; autocrine signaling [GO:0035425]; canonical Wnt signaling pathway [GO:0060070]; canonical Wnt signaling pathway involved in mesenchymal stem cell differentiation [GO:0044338]; cell-cell signaling [GO:0007267]; endothelial cell differentiation [GO:0045446]; hard palate development [GO:0060022]; membranous septum morphogenesis [GO:0003149]; muscular septum morphogenesis [GO:0003150]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway [GO:1903377]; non-canonical Wnt signaling pathway [GO:0035567]; outflow tract morphogenesis [GO:0003151]; planar cell polarity pathway involved in neural tube closure [GO:0090179]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of neuron projection development [GO:0010976]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of protein phosphorylation [GO:0001934]; regulation of mesenchymal stem cell differentiation [GO:2000739]; regulation of presynapse assembly [GO:1905606]; response to xenobiotic stimulus [GO:0009410]; ventricular septum morphogenesis [GO:0060412]; Wnt signaling pathway [GO:0016055]
|
cell surface [GO:0009986]; plasma membrane [GO:0005886]
|
frizzled binding [GO:0005109]; G protein-coupled receptor activity [GO:0004930]; identical protein binding [GO:0042802]; PDZ domain binding [GO:0030165]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; Wnt receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147]
|
PF01534;PF01392;
|
1.10.2000.10;1.20.1070.10;
|
G-protein coupled receptor Fz/Smo family
|
PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15923619}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Receptor for Wnt proteins (PubMed:15923619). Activated by WNT7B (PubMed:15923619). Activated by WNT3A, WNT3, WNT1 and to a lesser extent WNT2, but apparently not by WNT4, WNT5A, WNT5B, WNT6, WNT7A or WNT7B (By similarity). Contradictory results showing activation by WNT7B have been described for mouse (PubMed:15923619). Functions in the canonical Wnt/beta-catenin signaling pathway (PubMed:15923619). The canonical Wnt/beta-catenin signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (PubMed:15923619). A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (Probable). {ECO:0000250|UniProtKB:Q9UP38, ECO:0000269|PubMed:15923619, ECO:0000305}.
|
Mus musculus (Mouse)
|
O70423
|
AOC3_MOUSE
|
MTQKTTLVLLALAVITIFALVCVLLAGRSGDGGGLSQPLHCPSVLPSVQPRTHPSQSQPFADLSPEELTAVMSFLTKHLGPGLVDAAQARPSDNCVFSVELQLPAKAAALAHLDRGGPPPVREALAIIFFGGQPKPNVSELVVGPLPHPSYMRDVTVERHGGPLPYYRRPVLDREYQDIEEMIFHRELPQASGLLHHCCFYKHQGQNLLTMTTAPRGLQSGDRATWFGLYYNLSGAGFYPHPIGLELLIDHKALDPALWTIQKVFYQGRYYESLTQLEDQFEAGLVNVVLVPNNGTGGSWSLKSSVPPGPAPPLQFHPQGPRFSVQGSQVSSSLWAFSFGLGAFSGPRIFDIRFQGERVAYEISVQEAIALYGGNSPASMSTCYVDGSFGIGKYSTPLIRGVDCPYLATYVDWHFLLESQAPKTLRDAFCVFEQNQGLPLRRHHSDFYSHYFGGVVGTVLVVRSVSTLLNYDYIWDMVFHPNGAIEVKFHATGYISSAFFFGAGEKFGNRVGAHTLGTVHTHSAHFKVDLDVAGLKNWAWAEDMAFVPTIVPWQPEYQMQRLQVTRKLLETEEEAAFPLGGATPRYLYLASNHSNKWGHRRGYRIQILSFAGKPLPQESPIEKAFTWGRYHLAVTQRKEEEPSSSSIFNQNDPWTPTVNFTDFISNETIAGEDLVAWVTAGFLHIPHAEDIPNTVTAGNSVGFFLRPYNFFDEDPSFHSADSIYFREGQDATACEVNPLACLSQTATCAPEIPAFSHGGFAYRDN
|
1.4.3.21
|
COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q16853}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q16853}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q16853}; Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:Q16853}; COFACTOR: Name=L-topaquinone; Xref=ChEBI:CHEBI:79027; Evidence={ECO:0000250|UniProtKB:Q16853}; Note=Contains 1 topaquinone per subunit. {ECO:0000250|UniProtKB:Q16853};
|
amine metabolic process [GO:0009308]; cell adhesion [GO:0007155]; eating behavior [GO:0042755]; leukocyte migration involved in inflammatory response [GO:0002523]; positive regulation of acute inflammatory response [GO:0002675]; positive regulation of glucose transmembrane transport [GO:0010828]; positive regulation of leukocyte migration [GO:0002687]; regulation of blood pressure [GO:0008217]; response to antibiotic [GO:0046677]; response to immobilization stress [GO:0035902]
|
cell surface [GO:0009986]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; microvillus [GO:0005902]; plasma membrane [GO:0005886]
|
aliphatic amine oxidase activity [GO:0052595]; calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; primary amine oxidase activity [GO:0008131]; protein heterodimerization activity [GO:0046982]; quinone binding [GO:0048038]
|
PF01179;PF02727;PF02728;
|
3.10.450.40;2.70.98.20;
|
Copper/topaquinone oxidase family
|
PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000250|UniProtKB:Q16853}.; PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:Q16853}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q16853}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q16853}.
|
CATALYTIC ACTIVITY: Reaction=H2O + methylamine + O2 = formaldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:59420, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16842, ChEBI:CHEBI:28938, ChEBI:CHEBI:59338; Evidence={ECO:0000250|UniProtKB:Q16853}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59421; Evidence={ECO:0000250|UniProtKB:Q16853}; CATALYTIC ACTIVITY: Reaction=benzylamine + H2O + O2 = benzaldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:59424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17169, ChEBI:CHEBI:28938, ChEBI:CHEBI:225238; Evidence={ECO:0000250|UniProtKB:Q16853}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59425; Evidence={ECO:0000250|UniProtKB:Q16853}; CATALYTIC ACTIVITY: Reaction=2-phenylethylamine + H2O + O2 = 2-phenylacetaldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:25265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16424, ChEBI:CHEBI:28938, ChEBI:CHEBI:225237; EC=1.4.3.21; Evidence={ECO:0000250|UniProtKB:Q16853}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25266; Evidence={ECO:0000250|UniProtKB:Q16853};
| null | null | null | null |
FUNCTION: Catalyzes the oxidative deamination of primary amines to the corresponding aldehydes with the concomitant production of hydrogen peroxide and ammonia. Has a preference for the primary monoamines methylamine and benzylamine. Could also act on 2-phenylethylamine but much less efficiently. At endothelial cells surface can also function as a cell adhesion protein that participates in lymphocyte extravasation and recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. {ECO:0000250|UniProtKB:Q16853}.
|
Mus musculus (Mouse)
|
O70433
|
FHL2_MOUSE
|
MTERFDCHHCNESLYGKKYILKEENPHCVACFEELYANTCEECGTPIGCDCKDLSYKDRHWHEGCFHCSRCGSSLVDKPFAAKEEQLLCTDCYSNEYSSKCQECKKTIMPGTRKMEYKGSSWHETCFTCQRCQQPIGTKSFIPKENQNFCVPCYEKQYALQCVQCKKPITTGGVTYREQPWHKECFVCTACKKQLSGQRFTARDEFPYCLTCFCDLYAKKCAGCTNPISGLGGTKYISFEERQWHNDCFNCKKCSLSLVGRGFLTERDDILCPDCGKDI
| null | null |
atrial cardiac muscle cell development [GO:0055014]; heart trabecula formation [GO:0060347]; negative regulation of apoptotic process [GO:0043066]; negative regulation of calcineurin-NFAT signaling cascade [GO:0070885]; negative regulation of transcription by RNA polymerase II [GO:0000122]; osteoblast differentiation [GO:0001649]; regulation of transcription by RNA polymerase II [GO:0006357]; response to hormone [GO:0009725]; ventricular cardiac muscle cell development [GO:0055015]
|
M band [GO:0031430]; nucleus [GO:0005634]; Z disc [GO:0030018]
|
bHLH transcription factor binding [GO:0043425]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; transcription coregulator activity [GO:0003712]; transcription corepressor activity [GO:0003714]; transcription factor binding [GO:0008134]
|
PF00412;
|
2.10.110.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14192}. Nucleus {ECO:0000269|PubMed:20013826}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:22851699}.
| null | null | null | null | null |
FUNCTION: May function as a molecular transmitter linking various signaling pathways to transcriptional regulation. Negatively regulates the transcriptional repressor E4F1 and may function in cell growth. Inhibits the transcriptional activity of FOXO1 and its apoptotic function by enhancing the interaction of FOXO1 with SIRT1 and FOXO1 deacetylation (By similarity). Negatively regulates the calcineurin/NFAT signaling pathway in cardiomyocytes (PubMed:22851699). {ECO:0000250|UniProtKB:Q14192, ECO:0000269|PubMed:22851699}.
|
Mus musculus (Mouse)
|
O70435
|
PSA3_MOUSE
|
MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSANDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDVVKEVAKIIYIVHDEVKDKAFELELSWVGELTKGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM
| null | null |
proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]
|
cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome core complex [GO:0005839]; proteasome core complex, alpha-subunit complex [GO:0019773]; synapse [GO:0045202]
|
ubiquitin protein ligase binding [GO:0031625]
|
PF00227;PF10584;
|
3.60.20.10;
|
Peptidase T1A family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25788}. Nucleus {ECO:0000250|UniProtKB:P25788}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000250|UniProtKB:P25788}.
| null | null | null | null | null |
FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2. {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:22341445}.
|
Mus musculus (Mouse)
|
O70436
|
SMAD2_RAT
|
MSSILPFTPPVVKRLLGWKKSAGGSGGAGGGEQNGQEEKWCEKAVKSLVKKLKKTGRLDELEKAITTQNCNTKCVTIPSTCSEIWGLSTANTVDQWDTTGLYSFSEQTRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELKAIENCEYAFSLKKDEVCVNPYHYQRVETPVLPPVLVPRHTEILTELPPLDDYTHSIPENTNFPAGIEPQSNYIPETPPPGYISEDGETSDQQLNQSMDTGSPAELSPTTLSPVNHSLDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNVNRNATVEMTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSVRCSSMS
| null | null |
activin receptor signaling pathway [GO:0032924]; adrenal gland development [GO:0030325]; anatomical structure morphogenesis [GO:0009653]; anterior/posterior pattern specification [GO:0009952]; aortic valve morphogenesis [GO:0003180]; cell differentiation [GO:0030154]; cell fate commitment [GO:0045165]; cell population proliferation [GO:0008283]; cellular response to glucose stimulus [GO:0071333]; cellular response to transforming growth factor beta stimulus [GO:0071560]; determination of left/right asymmetry in lateral mesoderm [GO:0003140]; developmental growth [GO:0048589]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic foregut morphogenesis [GO:0048617]; embryonic pattern specification [GO:0009880]; endocardial cushion morphogenesis [GO:0003203]; endoderm development [GO:0007492]; endoderm formation [GO:0001706]; gastrulation [GO:0007369]; heart development [GO:0007507]; in utero embryonic development [GO:0001701]; insulin secretion [GO:0030073]; intracellular signal transduction [GO:0035556]; lung development [GO:0030324]; mesoderm formation [GO:0001707]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; nodal signaling pathway [GO:0038092]; odontoblast differentiation [GO:0071895]; organ growth [GO:0035265]; pancreas development [GO:0031016]; paraxial mesoderm morphogenesis [GO:0048340]; pattern specification process [GO:0007389]; pericardium development [GO:0060039]; positive regulation of BMP signaling pathway [GO:0030513]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; post-embryonic development [GO:0009791]; pulmonary valve morphogenesis [GO:0003184]; regulation of binding [GO:0051098]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; response to cholesterol [GO:0070723]; response to glucose [GO:0009749]; response to transforming growth factor beta [GO:0071559]; secondary palate development [GO:0062009]; signal transduction involved in regulation of gene expression [GO:0023019]; SMAD protein signal transduction [GO:0060395]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ureteric bud development [GO:0001657]; zygotic specification of dorsal/ventral axis [GO:0007352]
|
activin responsive factor complex [GO:0032444]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; heteromeric SMAD protein complex [GO:0071144]; homomeric SMAD protein complex [GO:0071142]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; SMAD protein complex [GO:0071141]; transcription regulator complex [GO:0005667]
|
chromatin binding [GO:0003682]; co-SMAD binding [GO:0070410]; disordered domain specific binding [GO:0097718]; 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]; DNA-binding transcription factor binding [GO:0140297]; double-stranded DNA binding [GO:0003690]; I-SMAD binding [GO:0070411]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; phosphatase binding [GO:0019902]; R-SMAD binding [GO:0070412]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; SMAD binding [GO:0046332]; tau protein binding [GO:0048156]; transforming growth factor beta receptor binding [GO:0005160]; type I transforming growth factor beta receptor binding [GO:0034713]; ubiquitin protein ligase binding [GO:0031625]
|
PF03165;PF03166;
|
2.60.200.10;3.90.520.10;
|
Dwarfin/SMAD family
|
PTM: In response to TGF-beta, phosphorylated on the C-terminal SXS motif by TGF-beta and activin type 1 receptor kinases, phosphorylation declines progressively in a KMT5A-dependent manner. Phosphorylation in this motif is required for interaction with a number of proteins including SMURF2, SNON and SMAD4 in response to TGF-beta. Dephosphorylated in this motif by PPM1A leading to disruption of the SMAD2/3-SMAD4 complex, nuclear export and termination of the TGF-beta signaling. In response to decorin, the naturally occurring inhibitor of TGF-beta signaling, phosphorylated on Ser-240 by CaMK2. Phosphorylated by MAPK3 upon EGF stimulation; which increases transcriptional activity and stability, and is blocked by calmodulin. Phosphorylated by PDPK1 (By similarity). {ECO:0000250|UniProtKB:Q15796}.; PTM: Acetylated on Lys-19 by coactivators in response to TGF-beta signaling, which increases transcriptional activity. {ECO:0000250|UniProtKB:Q15796}.; PTM: In response to TGF-beta, ubiquitinated by NEDD4L; which promotes its degradation. Monoubiquitinated, leading to prevent DNA-binding (By similarity). Deubiquitination by USP15 alleviates inhibition and promotes activation of TGF-beta target genes (By similarity). Ubiquitinated by RNF111, leading to its degradation: only SMAD2 proteins that are 'in use' are targeted by RNF111, RNF111 playing a key role in activating SMAD2 and regulating its turnover (By similarity). {ECO:0000250|UniProtKB:Q15796, ECO:0000250|UniProtKB:Q62432}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15796}. Nucleus {ECO:0000250|UniProtKB:Q15796}. Note=Cytoplasmic and nuclear in the absence of TGF-beta (By similarity). On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4 or with IPO7 (By similarity). On dephosphorylation by phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out of the nucleus by interaction with RANBP1 (By similarity). Localized mainly to the nucleus in the early stages of embryo development with expression becoming evident in the cytoplasm at the blastocyst and epiblast stages (By similarity). {ECO:0000250|UniProtKB:Q15796, ECO:0000250|UniProtKB:Q62432}.
| null | null | null | null | null |
FUNCTION: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. Promotes TGFB1-mediated transcription of odontoblastic differentiation genes in dental papilla cells (By similarity). Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator (By similarity). {ECO:0000250|UniProtKB:Q15796, ECO:0000250|UniProtKB:Q62432}.
|
Rattus norvegicus (Rat)
|
O70437
|
SMAD4_RAT
|
MDNMSITNTPTSNDACLSIVHSLMCHRQGGESETFAKRAIESLVKKLKEKKDELDSLITAITTNGAHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARLWRWPDLHKNELKHVKYCQYAFDLKCDSVCVNPYHYERVVSPGIDLSGLTLQSNAPPSMLVKDEYVHDFEGQPSLPTEGHSIQTIQHPPSNRASTETYSAPALLAPSESNATSTTNFPNIPVASTSQPASILAGSHSEGLLQIASGPQPGQQQNGFTAQPATYHHNSTTTWTGSRTAPYTPNLPHHQNGHLQHHPPMPPHPGHYWPVHNELAFQPPISNHPAPEYWCSIAYFEMDVQVGETFKVPSSCPIVTVDGYVDPSGGDRFCLGQLSNVHRTEAIERARLHIGKGVQLECKGEGDVWVRCLSDHAVFVQSYYLDREAGRAPGDAVHKIYPSAYIKVFDLRQCHRQMQQQAATAQAAAAAQAAAVAGNIPGPGSVGGIAPAISLSAAAGIGVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVLHTMPIADPQPLD
| null | null |
adrenal gland development [GO:0030325]; anatomical structure morphogenesis [GO:0009653]; anterior/posterior pattern specification [GO:0009952]; atrioventricular canal development [GO:0036302]; atrioventricular valve formation [GO:0003190]; axon guidance [GO:0007411]; BMP signaling pathway [GO:0030509]; brainstem development [GO:0003360]; branching involved in ureteric bud morphogenesis [GO:0001658]; cardiac muscle hypertrophy in response to stress [GO:0014898]; cardiac septum development [GO:0003279]; cell differentiation [GO:0030154]; cell population proliferation [GO:0008283]; cellular response to glucose stimulus [GO:0071333]; cellular response to transforming growth factor beta stimulus [GO:0071560]; developmental growth [GO:0048589]; DNA-templated transcription [GO:0006351]; embryonic digit morphogenesis [GO:0042733]; endocardial cell differentiation [GO:0060956]; endoderm development [GO:0007492]; endothelial cell activation [GO:0042118]; epithelial cell migration [GO:0010631]; epithelial to mesenchymal transition [GO:0001837]; epithelial to mesenchymal transition involved in endocardial cushion formation [GO:0003198]; ERK1 and ERK2 cascade [GO:0070371]; extrinsic apoptotic signaling pathway [GO:0097191]; female gonad development [GO:0008585]; female gonad morphogenesis [GO:0061040]; formation of anatomical boundary [GO:0048859]; gastrulation [GO:0007369]; gastrulation with mouth forming second [GO:0001702]; in utero embryonic development [GO:0001701]; interleukin-6-mediated signaling pathway [GO:0070102]; intracellular iron ion homeostasis [GO:0006879]; intracellular signal transduction [GO:0035556]; kidney development [GO:0001822]; left ventricular cardiac muscle tissue morphogenesis [GO:0003220]; male gonad development [GO:0008584]; mesendoderm development [GO:0048382]; mesoderm development [GO:0007498]; metanephric mesenchyme morphogenesis [GO:0072133]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cardiac muscle hypertrophy [GO:0010614]; negative regulation of cardiac myofibril assembly [GO:1905305]; negative regulation of cell growth [GO:0030308]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nephrogenic mesenchyme morphogenesis [GO:0072134]; neural crest cell differentiation [GO:0014033]; neuron fate commitment [GO:0048663]; neuron fate specification [GO:0048665]; osteoblast differentiation [GO:0001649]; outflow tract septum morphogenesis [GO:0003148]; ovarian follicle development [GO:0001541]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; positive regulation of cell proliferation involved in heart valve morphogenesis [GO:0003251]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of extracellular matrix assembly [GO:1901203]; positive regulation of follicle-stimulating hormone secretion [GO:0046881]; positive regulation of gene expression [GO:0010628]; positive regulation of luteinizing hormone secretion [GO:0033686]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of SMAD protein signal transduction [GO:0060391]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; regulation of cell population proliferation [GO:0042127]; regulation of hair follicle development [GO:0051797]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; regulation of transforming growth factor beta2 production [GO:0032909]; response to hypoxia [GO:0001666]; response to transforming growth factor beta [GO:0071559]; sebaceous gland development [GO:0048733]; secondary palate development [GO:0062009]; seminiferous tubule development [GO:0072520]; single fertilization [GO:0007338]; SMAD protein signal transduction [GO:0060395]; somite rostral/caudal axis specification [GO:0032525]; spermatogenesis [GO:0007283]; tissue morphogenesis [GO:0048729]; transcription by RNA polymerase II [GO:0006366]; transforming growth factor beta receptor signaling pathway [GO:0007179]; uterus development [GO:0060065]; ventricular septum morphogenesis [GO:0060412]
|
activin responsive factor complex [GO:0032444]; centrosome [GO:0005813]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; heteromeric SMAD protein complex [GO:0071144]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; RNA polymerase II transcription regulator complex [GO:0090575]; SMAD protein complex [GO:0071141]; transcription regulator complex [GO:0005667]
|
chromatin binding [GO:0003682]; collagen binding [GO:0005518]; 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]; filamin binding [GO:0031005]; I-SMAD binding [GO:0070411]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; R-SMAD binding [GO:0070412]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565]; SMAD binding [GO:0046332]; sulfate binding [GO:0043199]; transcription cis-regulatory region binding [GO:0000976]; transcription coactivator binding [GO:0001223]; transcription corepressor binding [GO:0001222]
|
PF03165;PF03166;
|
2.60.200.10;3.90.520.10;
|
Dwarfin/SMAD family
|
PTM: Phosphorylated by PDPK1. {ECO:0000250}.; PTM: Monoubiquitinated on Lys-519 by E3 ubiquitin-protein ligase TRIM33. Monoubiquitination hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade. Deubiquitination by USP9X restores its competence to mediate TGF-beta signaling (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13485}. Nucleus {ECO:0000250|UniProtKB:Q13485}. Note=In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with R-SMAD. PDPK1 prevents its nuclear translocation. {ECO:0000250|UniProtKB:Q13485}.
| null | null | null | null | null |
FUNCTION: Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling. Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta. Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8 (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O70439
|
STX7_MOUSE
|
MSYTPGIGGDSAQLAQRISSNIQKITQCSVEIQRTLNQLGTPQDSPELRQLLQQKQQYTNQLAKETDKYIKEFGSLPTTPSEQRQRKIQKDRLVAEFTTSLTNFQKAQRQAAEREKEFVARVRASSRVSGGFPEDSSKEKNLVSWESQTQPQVQVQDEEITEDDLRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQLSRAADYQRKSRKTLCIIIFILVVRIVIICLIVWGLKG
| null | null |
endosome to lysosome transport [GO:0008333]; intracellular protein transport [GO:0006886]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906]; vesicle-mediated transport [GO:0016192]
|
early endosome membrane [GO:0031901]; endomembrane system [GO:0012505]; endosome [GO:0005768]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; perinuclear region of cytoplasm [GO:0048471]; SNARE complex [GO:0031201]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]
|
protein-containing complex binding [GO:0044877]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]
|
PF05739;PF14523;
|
1.20.5.110;1.20.58.70;
|
Syntaxin family
| null |
SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O70441
|
SYN3_RAT
|
MNFLRRRLSDSSFVANLPNGYMPDLQRPESSSSSPASPATERRHPQPLAASFSSPGSSLFSSFSSAMKQTPQAPTGLMEPPTPVTPVVQRPRILLVIDDAHTDWSKYFHGKKVNGDIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKIVRSFKPDFILVRQHAYSMALAEDYRSLVIGLQYGGLPAVNSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMLTAPNFPVVIKLGHAHAGMGKIKVENQHDYQDITSVVAMAKTYATTEAFIDSKYDIRIQKIGSNYKAYMRTSISGNWKANTGSAMLEQVAMTERYRLWVDSCSEMFGGLDICAVKAVHSKNGRDYIIEVMDSSMPLIGEHVEEDKQLMADLVVSKMSQLLVPGASVPSPLRPWGPQTKSAKSPGQGQLGPLLGQPQPRPPPQGGPRQAQSPQPPRSRSPSQQRLSPQGQQPVSPQSGSPQQQRSPGSPQLSRASGGSSPNQASKPTASLSSHTRPPVQGRSTSQQGEEPQKTASPHPHLNKSQSLTNSLSTSDTSHRGTPSEDEAKAETIRNLRKSFASLFSD
| null | null |
neurotransmitter secretion [GO:0007269]; synaptic vesicle clustering [GO:0097091]; synaptic vesicle cycle [GO:0099504]
|
extrinsic component of synaptic vesicle membrane [GO:0098850]; glutamatergic synapse [GO:0098978]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]
|
ATP binding [GO:0005524]
|
PF02078;PF02750;PF10581;
|
3.40.50.20;3.30.1490.20;3.30.470.20;
|
Synapsin family
|
PTM: Phosphorylation at Ser-9 dissociates synapsins from synaptic vesicles. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Peripheral membrane protein localized to the cytoplasmic surface of synaptic vesicles.
| null | null | null | null | null |
FUNCTION: May be involved in the regulation of neurotransmitter release and synaptogenesis. Binds ATP with high affinity and ADP with a lower affinity. This is consistent with a catalytic role of the C-domain in which ADP would be dissociated by cellular ATP after bound ATP was hydrolyzed.
|
Rattus norvegicus (Rat)
|
O70443
|
GNAZ_MOUSE
|
MGCRQSSEEKEAARRSRRIDRHLRSESQRQRREIKLLLLGTSNSGKSTIVKQMKIIHSGGFNLDACKEYKPLIIYNAIDSLTRIIRALAALKIDFHNPDRAYDAVQLFALTGPAESKGEITPELLGVMRRLWADPGAQACFGRSSEYHLEDNAAYYLNDLERIAAPDYIPTVEDILRSRDMTTGIVENKFTFKELTFKMVDVGGQRSERKKWIHCFEGVTAIIFCVELSGYDLKLYEDNQTSRMAESLRLFDSICNNNWFINTSLILFLNKKDLLAEKIRRIPLSVCFPEYKGQNTYEEAAVYIQRQFEDLNRNKETKEIYSHFTCATDTSNIQFVFDAVTDVIIQNNLKYIGLC
| null | null |
adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; G protein-coupled receptor signaling pathway [GO:0007186]; G protein-coupled serotonin receptor signaling pathway [GO:0098664]; negative regulation of insulin secretion [GO:0046676]
|
cell body [GO:0044297]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; heterotrimeric G-protein complex [GO:0005834]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
adenylate cyclase inhibitor activity [GO:0010855]; G protein-coupled receptor binding [GO:0001664]; G protein-coupled serotonin receptor binding [GO:0031821]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]
|
PF00503;
|
1.10.400.10;3.40.50.300;
|
G-alpha family, G(i/o/t/z) subfamily
| null |
SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
| null | null | null | null | null |
FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
|
Mus musculus (Mouse)
|
O70444
|
PIM3_RAT
|
MLLSKFGSLAHLCGPGGVDHLPVKILQPAKADKESFEKVYQVGAVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGSLGGMAVPLEVVLLRKVGAAGGARGVIRLLDWFERPDGFLLVLERPEPAQDLFDFITERGALDEPLARRFFAQVLAAVRHCHNCGVVHRDIKDENLLVDLRSGELKLIDFGSGAVLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEEILRGRLFFRRRVSPECQQLIEWCLSLRPSERPSLDQIAAHPWMLGTEGSVPENCDLRLCALDTDDGASTTSSSESL
|
2.7.11.1
| null |
apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cellular response to forskolin [GO:1904322]; negative regulation of apoptotic process [GO:0043066]; negative regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061179]; protein phosphorylation [GO:0006468]; regulation of mitotic cell cycle [GO:0007346]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; 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, PIM subfamily
|
PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000250}.; PTM: Phosphorylated. Interaction with PPP2CA promotes dephosphorylation (By similarity). Autophosphorylated (in vitro). {ECO:0000250}.
|
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: Proto-oncogene with serine/threonine kinase activity that can prevent apoptosis and promote cell survival and protein translation. May contribute to tumorigenesis through: the delivery of survival signaling through phosphorylation of BAD which induces release of the anti-apoptotic protein Bcl-X(L), the regulation of cell cycle progression and protein synthesis and by regulation of MYC transcriptional activity. Additionally to this role on tumorigenesis, can also negatively regulate insulin secretion by inhibiting the activation of MAPK1/3 (ERK1/2), through SOCS6. Involved also in the control of energy metabolism and regulation of AMPK activity in modulating MYC and PPARGC1A protein levels and cell growth (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O70445
|
BARD1_MOUSE
|
MPRRPPRVCSGNQPAPVPAMEPATDGLWAHSRAALARLEKLLRCSRCANILKEPVCLGGCEHIFCSGCISDCVGSGCPVCYTPAWILDLKINRQLDSMIQLSSKLQNLLHDNKDSKDNTSRASLFGDAERKKNSIKMWFSPRSKKVRYVVTKVSVQTQPQKAKDDKAQEASMYEFVSATPPVAVPKSAKTASRTSAKKHPKKSVAKINREENLRPETKDSRFDSKEELKEEKVVSCSQIPVMERPRVNGEIDLLASGSVVEPECSGSLTEVSLPLAEHIVSPDTVSKNEETPEKKVCVKDLRSGGSNGNRKGCHRPTTSTSDSCGSNIPSTSRGIGEPALLAENVVLVDCSSLPSGQLQVDVTLRRKSNASDDPLSLSPGTPPPLLNNSTHRQMMSSPSTVKLSSGMPARKRNHRGETLLHIASIKGDIPSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKVVELLLQHNALVNTPGYQNDSPLHDAVKSGHIDIVKVLLSHGASRNAVNIFGVRPVDYTDNENIRSLLLLPEENESFSTSQCSIVNTGQRKNGPLVFIGSGLSSQQQKMLSKLETVLKAKKCMEFDSTVTHVIVPDEEAQSTLKCMLGILSGCWILKFDWVKACLDSKVREQEEKYEVPGGPQRSRLNREQLLPKLFDGCYFFLGGNFKHHPRDDLLKLIAAAGGKVLSRKPKPDSDVTQTINTVAYHAKPESDQRFCTQYIVYEDLFNCHPERVRQGKVWMAPSTWLISCIMAFELLPLDS
|
2.3.2.27
| null |
cellular response to ionizing radiation [GO:0071479]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA strand resection involved in replication fork processing [GO:0110025]; homologous recombination [GO:0035825]; mitotic G2/M transition checkpoint [GO:0044818]; negative regulation of apoptotic process [GO:0043066]; negative regulation of protein export from nucleus [GO:0046826]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell cycle [GO:0045787]; protein K6-linked ubiquitination [GO:0085020]; regulation of DNA damage checkpoint [GO:2000001]; regulation of DNA repair [GO:0006282]; regulation of phosphorylation [GO:0042325]
|
BRCA1-A complex [GO:0070531]; BRCA1-B complex [GO:0070532]; BRCA1-BARD1 complex [GO:0031436]; BRCA1-C complex [GO:0070533]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; nuclear speck [GO:0016607]; nuclear ubiquitin ligase complex [GO:0000152]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; ubiquitin-protein transferase activity [GO:0004842]
|
PF12796;PF14835;
|
1.25.40.20;3.40.50.10190;3.30.40.10;
| null |
PTM: Processed during apoptosis. The homodimer is more susceptible to proteolytic cleavage than the BARD1/BRCA1 heterodimer. {ECO:0000250|UniProtKB:Q99728}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15077185}. Cytoplasm {ECO:0000269|PubMed:15077185}. Note=Can translocate to the cytoplasm. Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex. {ECO:0000250|UniProtKB:Q99728}.
|
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:0000250|UniProtKB:Q99728};
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage. {ECO:0000250|UniProtKB:Q99728}.
|
Mus musculus (Mouse)
|
O70451
|
MOT2_MOUSE
|
MPSEPSAPLPQPLPPDGGWGWVVVCASFISIGFSYAFPKAVTVFFKDIQEIFNTTSSQIAWISSIMLAVMYAGGPISSVLVNNYGSRPVVIVGGLLCCIGMILASYSNSVIELYLTVGFIGGLGLAFNLQPALTIIGKYFYRRRPLANGCAMAGSPVFLSTLAPFNQYLFNNYGWKGSFLILGGIFLHSCVAGCLMRPVGPSPNTKKSKSKVGSRHDSTLKKASKVSTAQKVNRFLDFSLFMHRGFLIYLSGNVILFLGIFAPIIFLAQYAKHIGVDDYNSAFLLSVMAFIDMFARPSVGLIANTSLIRPRIQYLFSSAIIFTGICHLLCPLATTYSALVVYVVFFGLGFGSISSLLFECLMDIVGATRFSSAVGLTTIVECCPVLFGPPLAGKLLDITGEYKYLYIASGTVVLVSGTYLLIGNAINYRLLDKERKREKAKKKKSASHASREMEALNRSKQDEVTVKASNAHNPPSDRDKESNI
| null | null |
lactate transmembrane transport [GO:0035873]; plasma membrane lactate transport [GO:0035879]; pyruvate transmembrane transport [GO:1901475]
|
basolateral plasma membrane [GO:0016323]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; nucleoplasm [GO:0005654]; parallel fiber to Purkinje cell synapse [GO:0098688]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; Schaffer collateral - CA1 synapse [GO:0098685]
|
identical protein binding [GO:0042802]; lactate transmembrane transporter activity [GO:0015129]; pyruvate transmembrane transporter activity [GO:0050833]; symporter activity [GO:0015293]
|
PF07690;
|
1.20.1250.20;
|
Major facilitator superfamily, Monocarboxylate porter (TC 2.A.1.13) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O60669}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O60669}. Cytoplasm {ECO:0000269|PubMed:21792931}. Basolateral cell membrane {ECO:0000250|UniProtKB:P53988}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O60669}. Note=Requires the ancillary protein, EMB for plasma membrane localization (By similarity). Colocalizes with BSG in spermatozoa. Detected in the cytoplasm of Sertoli cells (PubMed:21792931). {ECO:0000250|UniProtKB:Q63344, ECO:0000269|PubMed:21792931}.
|
CATALYTIC ACTIVITY: Reaction=(S)-lactate(in) + H(+)(in) = (S)-lactate(out) + H(+)(out); Xref=Rhea:RHEA:29415, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651; Evidence={ECO:0000269|PubMed:21792931}; CATALYTIC ACTIVITY: Reaction=3-methyl-2-oxobutanoate(out) + H(+)(out) = 3-methyl-2-oxobutanoate(in) + H(+)(in); Xref=Rhea:RHEA:71783, ChEBI:CHEBI:11851, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q63344}; CATALYTIC ACTIVITY: Reaction=acetoacetate(out) + H(+)(out) = acetoacetate(in) + H(+)(in); Xref=Rhea:RHEA:71775, ChEBI:CHEBI:13705, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q63344}; CATALYTIC ACTIVITY: Reaction=(R)-3-hydroxybutanoate(out) + H(+)(out) = (R)-3-hydroxybutanoate(in) + H(+)(in); Xref=Rhea:RHEA:71795, ChEBI:CHEBI:10983, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q63344}; CATALYTIC ACTIVITY: Reaction=4-methyl-2-oxopentanoate(out) + H(+)(out) = 4-methyl-2-oxopentanoate(in) + H(+)(in); Xref=Rhea:RHEA:71779, ChEBI:CHEBI:15378, ChEBI:CHEBI:17865; Evidence={ECO:0000250|UniProtKB:Q63344}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + pyruvate(out) = H(+)(in) + pyruvate(in); Xref=Rhea:RHEA:64720, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q63344}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64721; Evidence={ECO:0000250|UniProtKB:O60669}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64722; Evidence={ECO:0000250|UniProtKB:O60669}; CATALYTIC ACTIVITY: Reaction=(S)-3-hydroxybutanoate(out) + H(+)(out) = (S)-3-hydroxybutanoate(in) + H(+)(in); Xref=Rhea:RHEA:71871, ChEBI:CHEBI:11047, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q63344};
| null | null | null | null |
FUNCTION: Proton-coupled monocarboxylate symporter (PubMed:21792931). Catalyzes the rapid transport across the plasma membrane of monocarboxylates such as L-lactate, pyruvate and ketone bodies, acetoacetate, beta-hydroxybutyrate and acetate. Dimerization is functionally required and both subunits work cooperatively in transporting substrate (By similarity). {ECO:0000250|UniProtKB:O60669, ECO:0000269|PubMed:21792931}.
|
Mus musculus (Mouse)
|
O70456
|
1433S_MOUSE
|
MERASLIQKAKLAEQAERYEDMAAFMKSAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSEEKGPEVKEYREKVETELRGVCDTVLGLLDSHLIKGAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADSAGEEGGEAPEEPQS
| null | null |
establishment of skin barrier [GO:0061436]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; keratinization [GO:0031424]; keratinocyte development [GO:0003334]; keratinocyte differentiation [GO:0030216]; keratinocyte proliferation [GO:0043616]; negative regulation of innate immune response [GO:0045824]; negative regulation of keratinocyte proliferation [GO:0010839]; negative regulation of stem cell proliferation [GO:2000647]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of cell growth [GO:0030307]; positive regulation of epidermal cell differentiation [GO:0045606]; positive regulation of protein export from nucleus [GO:0046827]; protein export from nucleus [GO:0006611]; protein kinase A signaling [GO:0010737]; regulation of cell cycle [GO:0051726]; regulation of epidermal cell division [GO:0010482]; release of cytochrome c from mitochondria [GO:0001836]; signal transduction [GO:0007165]; skin development [GO:0043588]; stem cell proliferation [GO:0072089]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleus [GO:0005634]
|
identical protein binding [GO:0042802]; phosphoprotein binding [GO:0051219]; phosphoserine residue binding [GO:0050815]; protein kinase binding [GO:0019901]; protein sequestering activity [GO:0140311]
|
PF00244;
|
1.20.190.20;
|
14-3-3 family
|
PTM: Ubiquitinated. Ubiquitination by RFFL induces proteasomal degradation and indirectly regulates p53/TP53 activation. {ECO:0000250|UniProtKB:P31947}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16710422}. Nucleus {ECO:0000269|PubMed:16710422}. Secreted {ECO:0000250|UniProtKB:P31947}. Note=May be secreted by a non-classical secretory pathway. {ECO:0000250|UniProtKB:P31947}.
| null | null | null | null | null |
FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways (By similarity). Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (By similarity). Binding generally results in the modulation of the activity of the binding partner (By similarity). Promotes cytosolic retention of GBP1 GTPase by binding to phosphorylated GBP1, thereby inhibiting the innate immune response (By similarity). Also acts as a TP53/p53-regulated inhibitor of G2/M progression (By similarity). When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (PubMed:16710422). May also regulate MDM2 autoubiquitination and degradation and thereby activate p53/TP53 (By similarity). {ECO:0000250|UniProtKB:P31947, ECO:0000269|PubMed:16710422}.
|
Mus musculus (Mouse)
|
O70458
|
OSMR_MOUSE
|
MAFSVVLHPAFLLAVLSLRASRSEVLEEPLPLTPEIHKVSFQLKLQEVNLEWTVPALTHEELNMIFQIEISRLNISNTIWVENYSTTVKREEAVRWNWTSDIPLECVKHFIRIRALVDDTKSLPQSSWGNWSSWKEVNAKVSVEPDKSLIFPKDKVLEEGSNVTICLMYGQNVYNVSCKLQDEPIHGEQLDSHVSLLKLNNVVFLSDTGTNINCQATKGPKRIFGTVLFVSKVLEEPKNVSCETRDFKTLDCSWEPGVDTTLTWRKQRFQNYTLCESFSKRCEVSNYRNSYTWQITEGSQEMYNFTLTAENQLRKRSVNINFNLTHRVHPKAPQDVTLKIIGATKANMTWKVHSHGNNYTLLCQVKLQYGEVIHEHNVSVHMSANYLFSDLDPDTKYKAFVRCASANHFWKWSDWTQKEFSTPETAPSQALDVWRQVWSENGRRIVTLFWKPLLKSQANGKIISYNIVVENEAKPTESEHYCVWAPALSTNLSLDLQPYKIRITTNNSMGASPESLMVLSNDSGHEEVKEKTIKGIKDAFNISWEPVSGDTMGYVVDWCAHSQDQRCDLQWKNLGPNTTSTTITSDDFKPGVRYNFRIFERSVEHKARLVEKQRGYTQELAPLVNPKVEIPYSTPNSFVLRWPDYDSDFQAGFIKGYLVYVKSKEMQCNQPWERTLLPDNSVLCKYDINGSETKTLTVENLQPESLYEFFVTPYTSAGPGPNETFTKVTTPDARSHMLLQIILPMTLCVLLSIIVCYWKSQWVKEKCYPDIPNPYKSSILSLIKSKKNPHLIMNVKDCIPDVLEVINKAEGSKTQCVGSGKLHIEDVPTKPPIVPTEKDSSGPVPCIFFENFTYDQSAFDSGSHGLIPGPLKDTAHQLGLLAPPNKFQNVLKNDYMKPLVESPTEETSLIYVSQLASPMCGDKDTLATEPPVPVHGSEYKRQMVVPGSLASPSLKEDNSLTSTVLLGQGEQ
| null | null |
cell surface receptor signaling pathway [GO:0007166]; cytokine-mediated signaling pathway [GO:0019221]; positive regulation of cell population proliferation [GO:0008284]
|
external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
ciliary neurotrophic factor receptor binding [GO:0005127]; cytokine binding [GO:0019955]; cytokine receptor activity [GO:0004896]; oncostatin-M receptor activity [GO:0004924]
|
PF00041;PF21177;PF17971;
|
2.60.40.10;
|
Type I cytokine receptor family, Type 2 subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Associates with IL31RA to form the IL31 receptor (PubMed:9920829). Binds IL31 to activate STAT3 and possibly STAT1 and STAT5 (By similarity). Capable of transducing OSM-specific signaling events (By similarity). {ECO:0000250|UniProtKB:Q99650, ECO:0000269|PubMed:9920829}.
|
Mus musculus (Mouse)
|
O70460
|
CCL19_MOUSE
|
MAPRVTPLLAFSLLVLWTFPAPTLGGANDAEDCCLSVTQRPIPGNIVKAFRYLLNEDGCRVPAVVFTTLRGYQLCAPPDQPWVDRIIRRLKKSSAKNKGNSTRRSPVS
| null | null |
cell maturation [GO:0048469]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; chemokine-mediated signaling pathway [GO:0070098]; dendritic cell chemotaxis [GO:0002407]; establishment of T cell polarity [GO:0001768]; G protein-coupled receptor signaling pathway [GO:0007186]; immunological synapse formation [GO:0001771]; inflammatory response [GO:0006954]; lymphocyte chemotaxis [GO:0048247]; mature conventional dendritic cell differentiation [GO:0097029]; monocyte chemotaxis [GO:0002548]; myeloid dendritic cell chemotaxis [GO:0002408]; negative regulation of dendritic cell apoptotic process [GO:2000669]; neutrophil chemotaxis [GO:0030593]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell motility [GO:2000147]; positive regulation of chemotaxis [GO:0050921]; positive regulation of dendritic cell antigen processing and presentation [GO:0002606]; positive regulation of dendritic cell dendrite assembly [GO:2000549]; positive regulation of endocytosis [GO:0045807]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of glycoprotein biosynthetic process [GO:0010560]; positive regulation of GTPase activity [GO:0043547]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of JNK cascade [GO:0046330]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of neutrophil chemotaxis [GO:0090023]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of T-helper 1 cell differentiation [GO:0045627]; positive regulation of tumor necrosis factor production [GO:0032760]; regulation of cell projection assembly [GO:0060491]; release of sequestered calcium ion into cytosol [GO:0051209]; response to nitric oxide [GO:0071731]; response to prostaglandin E [GO:0034695]; T cell costimulation [GO:0031295]
|
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]
|
CCR chemokine receptor binding [GO:0048020]; CCR7 chemokine receptor binding [GO:0031732]; chemokine activity [GO:0008009]; chemokine receptor binding [GO:0042379]
|
PF00048;
|
2.40.50.40;
|
Intercrine beta (chemokine CC) family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Strongly chemotactic for naive (L-selectinhi) CD4 T-cells and for CD8 T-cells and weakly attractive for resting B-cells and memory (L-selectinlo) CD4 T-cells. May play a role in promoting encounters between recirculating T-cells and dendritic cells and in the migration of activated B-cells into the T-zone of secondary lymphoid tissues. Binds to chemokine receptor CCR7. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4.
|
Mus musculus (Mouse)
|
O70467
|
ANM3_RAT
|
MCSLAAGNGQGAELGPEPLELSDSGDDAGWEDEDADAEPAQGRQHTPCLFCDRLFRSAEETFSHCKLEHQFNIDGMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWDKDEYLKPVLEDDLLLQFDVEDLYEPVSAPFTYPNGLSENTSAVEKLKLMEARALSAEAALARAREDLQKMKQFAQDFVMNVDVRTCSSTTTIADLQEDEDGVYFSSYGHYGIHEEMLKDKVRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVIAVDQSEILYQAMDIIRLNKLEDTIVLIKGKIEEVSLPVEKVDVIISEWMGYFLLFESMLDSVLYAKSKYLAKGGSVYPDICTISLVAVSDVSKHADRIAFWDDVYGFNMSCMKKAVIPEAVVEVVDHKTLISDPCDIKHIDCHTTSISDLEFSSDFTLRTTKTAMCTAVAGYFDIYFEKNCHNRVVFSTGPQSTKTHWKQTIFLLEKPFPVKAGEALKGKITVHKNKKDPRSLIVTLTLNSSTQTYSLQ
|
2.1.1.319
| null |
dendritic spine morphogenesis [GO:0060997]; methylation [GO:0032259]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of retinoic acid biosynthetic process [GO:1900053]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]; modified amino acid binding [GO:0072341]; protein-arginine N-methyltransferase activity [GO:0016274]; protein-arginine omega-N asymmetric methyltransferase activity [GO:0035242]; protein-arginine omega-N monomethyltransferase activity [GO:0035241]; ribosome binding [GO:0043022]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]
|
PF21137;PF21336;PF06325;
|
2.70.160.11;3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, Protein arginine N-methyltransferase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9642256}.
|
CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) + N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48100, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11990, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65280; Evidence={ECO:0000269|PubMed:9642256}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48101; Evidence={ECO:0000305|PubMed:9642256}; CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319; Evidence={ECO:0000269|PubMed:9642256}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48097; Evidence={ECO:0000305|PubMed:9642256};
| null | null | null | null |
FUNCTION: Protein-arginine N-methyltransferase that catalyzes both the monomethylation and asymmetric dimethylation of the guanidino nitrogens of arginine residues in target proteins, and therefore falls into the group of type I methyltransferases (PubMed:10899106, PubMed:15334060, PubMed:9642256). May regulate retinoic acid synthesis and signaling by inhibiting ALDH1A1 retinal dehydrogenase activity (By similarity). {ECO:0000250|UniProtKB:O60678, ECO:0000269|PubMed:10899106, ECO:0000269|PubMed:15334060, ECO:0000269|PubMed:9642256}.
|
Rattus norvegicus (Rat)
|
O70468
|
MYPC3_MOUSE
|
MPEPGKKPVSAFNKKPRSAEVTAGSAAVFEAETERSGVMVRWQRDGSDITANDKYGLAAEGKRHTLTVRDASPDDQGSYAVIAGSSKVKFDLKVTEPAPPEKAESEVAPGAPEEVPAPATELEESVSSPEGSVSVTQDGSAAEHQGAPDDPIGLFLMRPQDGEVTVGGSIVFSARVAGASLLKPPVVKWFKGKWVDLSSKVGQHLQLHDSYDRASKVYLFELHITDAQTTSAGGYRCEVSTKDKFDSCNFNLTVHEAIGSGDLDLRSAFRRTSLAGAGRRTSDSHEDAGTPDFSSLLKKRDSFRRDSKLEAPAEEDVWEILRQAPPSEYERIAFQHGVEACHRPLKRLKGMKQDEKKSTAFQKKLEPAYQVNKGHKIRLTVELADPDAEVKWLKNGQEIQMSGSKYIFESVGAKRTLTISQCSLADDAAYQCVVGGEKCSTELFVKEPPVLITRSLEDQLVMVGQRVEFECEVSEEGAQVKWLKDGVELTREETFKYRFKKDGRKHHLIINEATLEDAGHYAVRTSGGQSLAELIVQEKKLEVYQSIADLAVGAKDQAVFKCEVSDENVRGVWLKNGKELVPDNRIKVSHIGRVHKLTIDDVTPADEADYSFVPEGFACNLSAKLHFMEVKIDFVPRQEPPKIHLDCPGSTPDTIVVVTGNKLRLDVPISGDPAPTVVWQKTVTQGKKASAGPHPDAPEDAGADEEWVFDKKLLCETEGRVRVETTKDRSVFTVEGAEKEDEGVYTVTVKNPVGEDQVNLTVKVIDVPDAPAAPKISNVGEDSCTVQWEPPAYDGGQPVLGYILERKKKKSYRWMRLNFDLLRELSHEARRMIEGVAYEMRVYAVNAVGMSRPSPASQPFMPIGPPGEPTHLAVEDVSDTTVSLKWRPPERVGAGGLDGYSVEYCQEGCSEWTPALQGLTERRSMLVKDLPTGARLLFRVRAHNVAGPGGPIVTKEPVTVQEILQRPRLQLPRHLRQTIQKKVGEPVNLLIPFQGKPRPQVTWTKEGQPLAGEEVSIRNSPTDTILFIRAARRTHSGTYQVTVRIENMEDKATLILQIVDKPSPPQDIRIVETWGFNVALEWKPPQDDGNTEIWGYTVQKADKKTMEWFTVLEHYRRTHCVVSELIIGNGYYFRVFSHNMVGSSDKAAATKEPVFIPRPGITYEPPKYKALDFSEAPSFTQPLANRSIIAGYNAILCCAVRGSPKPKISWFKNGLDLGEDARFRMFCKQGVLTLEIRKPCPYDGGVYVCRATNLQGEAQCECRLEVRVPQ
| null | null |
cardiac muscle contraction [GO:0060048]; cell adhesion [GO:0007155]; heart morphogenesis [GO:0003007]; muscle contraction [GO:0006936]; myosin filament assembly [GO:0031034]; regulation of heart contraction [GO:0008016]; regulation of heart rate [GO:0002027]; sarcomere organization [GO:0045214]; ventricular cardiac muscle tissue morphogenesis [GO:0055010]
|
A band [GO:0031672]; cytoskeleton [GO:0005856]; myofibril [GO:0030016]; sarcomere [GO:0030017]; striated muscle myosin thick filament [GO:0005863]
|
actin binding [GO:0003779]; metal ion binding [GO:0046872]; myosin heavy chain binding [GO:0032036]; structural constituent of cytoskeleton [GO:0005200]
|
PF00041;PF07679;PF18362;
|
2.60.40.10;
|
Immunoglobulin superfamily, MyBP family
|
PTM: Substrate for phosphorylation by PKA and PKC. Reversible phosphorylation appears to modulate contraction (By similarity). {ECO:0000250}.; PTM: Polyubiquitinated. {ECO:0000250|UniProtKB:Q14896}.
| null | null | null | null | null | null |
FUNCTION: Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role.
|
Mus musculus (Mouse)
|
O70469
|
DOK2_MOUSE
|
MVRMEEPAVKQGFLHLQQQQTFGKKWRRFAAVLYGESGCALARLELQDVPEKTRRGEATRKVVRLSDCLRVAEVGSEASSPRDTSAFILETKERLYLLAAPSAERSDWIQAICLLAFPGQRKGSPGLEEKSGSPCMEENELYSSSTTGLCKEYMVTIRPTEASERCRLRGSYTLRTGVSALELWGGPEPGTQLYDWPYRFLRRFGRDKATFSFEAGRRCLSGEGNFEFETRHGNEIFQALEKVIAVQKNATPSGPPSLPATGPMMPTVLPRPESPYSRPHDSLPSPSPGTLVPGMRPGAPEGEYAVPFDTVAHSLRKSFRGLLTGPPPHLPDPLYDSIQEDPGAPLPDHIYDEPEGVAALSLYDRTQRPSGETWREQATADGGPSSLQQDSSVPDWPQATEYDNVILKKGPK
| null | null |
negative regulation of MAPK cascade [GO:0043409]; positive regulation of MAPK cascade [GO:0043410]; Ras protein signal transduction [GO:0007265]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
cytoplasm [GO:0005737]
|
transmembrane receptor protein tyrosine kinase adaptor activity [GO:0005068]
|
PF02174;PF00169;
|
2.30.29.30;
|
DOK family, Type A subfamily
|
PTM: On immunoreceptor stimulation, phosphorylated on C-terminal tyrosine residues. Phosphorylation on Tyr-351 is required for binding to the SH2 domain of NCK. Phosphorylation on both Tyr-276 and Tyr-304 is required for interaction with RASGAP. Phosphorylated on tyrosine residues by TEK/TIE2. {ECO:0000269|PubMed:10508618, ECO:0000269|PubMed:11470823, ECO:0000269|PubMed:12665569, ECO:0000269|PubMed:9697832}.
| null | null | null | null | null | null |
FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK2 may modulate the cellular proliferation induced by IL-4, as well as IL-2 and IL-3. May be involved in modulating Bcr-Abl signaling. Attenuates EGF-stimulated MAP kinase activation.
|
Mus musculus (Mouse)
|
O70473
|
AK1A1_CRIGR
|
MASCVLLHTGQKMPLIGLGTWKSNPGQVKAAIKYALSVGYRHIDCAAVYGNEIEIGEALKENVGPGKAVPREELFVTSKLWNTKHHPEDVEAALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNDDGTIRYDSTHYKETWKALEALVAKGLVKALGLSNFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRHPDEPVLLEEPVVLALAEKHGRSPAQILLRWQVQRKVVCIPKSITPSRILQNIQVFDFTFSPEEMKQLDALNKHWRYIVPMITVDGKSVPRDAGHPLYPFNDPY
|
1.1.1.19; 1.1.1.2; 1.1.1.20; 1.1.1.372; 1.1.1.54; 1.6.-.-
| null |
aldehyde catabolic process [GO:0046185]; cellular detoxification of aldehyde [GO:0110095]; D-glucuronate catabolic process [GO:0042840]; daunorubicin metabolic process [GO:0044597]; doxorubicin metabolic process [GO:0044598]; glucuronate catabolic process to xylulose 5-phosphate [GO:0019640]; L-ascorbic acid biosynthetic process [GO:0019853]; lipid metabolic process [GO:0006629]
|
apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; synapse [GO:0045202]
|
alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; allyl-alcohol dehydrogenase activity [GO:0047655]; glucuronolactone reductase activity [GO:0047941]; glycerol dehydrogenase [NADP+] activity [GO:0047956]; L-glucuronate reductase activity [GO:0047939]; methylglyoxal reductase (NADPH-dependent, acetol producing) [GO:1990002]; S-nitrosoglutathione reductase activity [GO:0080007]
|
PF00248;
|
3.20.20.100;
|
Aldo/keto reductase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JII6}. Apical cell membrane {ECO:0000250|UniProtKB:Q9JII6}.
|
CATALYTIC ACTIVITY: Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH; Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.2; Evidence={ECO:0000250|UniProtKB:P14550}; CATALYTIC ACTIVITY: Reaction=L-gulonate + NADP(+) = aldehydo-D-glucuronate + H(+) + NADPH; Xref=Rhea:RHEA:14909, ChEBI:CHEBI:13115, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142686; EC=1.1.1.19; Evidence={ECO:0000250|UniProtKB:P51635}; CATALYTIC ACTIVITY: Reaction=L-gulono-1,4-lactone + NADP(+) = D-glucurono-3,6-lactone + H(+) + NADPH; Xref=Rhea:RHEA:18925, ChEBI:CHEBI:15378, ChEBI:CHEBI:17587, ChEBI:CHEBI:18268, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.20; Evidence={ECO:0000250|UniProtKB:P51635}; CATALYTIC ACTIVITY: Reaction=allyl alcohol + NADP(+) = acrolein + H(+) + NADPH; Xref=Rhea:RHEA:12168, ChEBI:CHEBI:15368, ChEBI:CHEBI:15378, ChEBI:CHEBI:16605, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.54; Evidence={ECO:0000250|UniProtKB:P51635}; CATALYTIC ACTIVITY: Reaction=glycerol + NADP(+) = D-glyceraldehyde + H(+) + NADPH; Xref=Rhea:RHEA:23592, ChEBI:CHEBI:15378, ChEBI:CHEBI:17378, ChEBI:CHEBI:17754, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.372; Evidence={ECO:0000250|UniProtKB:P51635}; CATALYTIC ACTIVITY: Reaction=glycerol + NADP(+) = H(+) + L-glyceraldehyde + NADPH; Xref=Rhea:RHEA:38111, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:27975, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.372; Evidence={ECO:0000250|UniProtKB:P51635}; CATALYTIC ACTIVITY: Reaction=hydroxyacetone + NADP(+) = H(+) + methylglyoxal + NADPH; Xref=Rhea:RHEA:27986, ChEBI:CHEBI:15378, ChEBI:CHEBI:17158, ChEBI:CHEBI:27957, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:P51635}; CATALYTIC ACTIVITY: Reaction=3-deoxyfructose + NADP(+) = 3-deoxyglucosone + H(+) + NADPH; Xref=Rhea:RHEA:58668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60777, ChEBI:CHEBI:142685; Evidence={ECO:0000250|UniProtKB:P51635}; CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + NADP(+) = (R)-mevaldate + H(+) + NADPH; Xref=Rhea:RHEA:20193, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:195523; Evidence={ECO:0000250|UniProtKB:P51635}; CATALYTIC ACTIVITY: Reaction=H(+) + NADPH + S-nitroso-CoA = NADP(+) + sulfinamide-CoA; Xref=Rhea:RHEA:78375, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145546, ChEBI:CHEBI:145548; Evidence={ECO:0000250|UniProtKB:P14550}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78376; Evidence={ECO:0000250|UniProtKB:P14550}; CATALYTIC ACTIVITY: Reaction=H(+) + NADPH + S-nitrosoglutathione = NADP(+) + sulfinamide glutathione; Xref=Rhea:RHEA:63500, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145544, ChEBI:CHEBI:145547; Evidence={ECO:0000250|UniProtKB:Q9JII6};
| null | null | null | null |
FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids, with a preference for negatively charged substrates, such as glucuronate and succinic semialdehyde (By similarity). Plays an important role by catalyzing the reduction of D-glucuronic acid and D-glucurono-gamma-lactone. Functions as a detoxifiying enzyme by reducing a range of toxic aldehydes. Reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic. Involved also in the detoxification of lipid-derived aldehydes like acrolein (By similarity). Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity). Also acts as an inhibitor of protein S-nitrosylation by mediating degradation of S-nitroso-coenzyme A (S-nitroso-CoA), a cofactor required to S-nitrosylate proteins (By similarity). S-nitroso-CoA reductase activity is involved in reprogramming intermediary metabolism in renal proximal tubules, notably by inhibiting protein S-nitrosylation of isoform 2 of PKM (PKM2) (By similarity). Also acts as a S-nitroso-glutathione reductase by catalyzing the NADPH-dependent reduction of S-nitrosoglutathione (By similarity). Displays no reductase activity towards retinoids (By similarity). {ECO:0000250|UniProtKB:P14550, ECO:0000250|UniProtKB:P50578, ECO:0000250|UniProtKB:P51635}.
|
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
|
O70475
|
UGDH_MOUSE
|
MVEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNEARINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIREADLVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKPNLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDETPEGQKAVRALCAVYEHWVPKEKILTTNTWSSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLFNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSADDQVSRLVTISKDPYEACDGAHALVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDGLHSELQTIGFQIETIGKKVSSKRIPYTPGEIPKFSLQDPPNKKPKV
|
1.1.1.22
| null |
chondroitin sulfate biosynthetic process [GO:0030206]; gastrulation with mouth forming second [GO:0001702]; glycosaminoglycan biosynthetic process [GO:0006024]; heparan sulfate proteoglycan biosynthetic process [GO:0015012]; neuron development [GO:0048666]; protein hexamerization [GO:0034214]; UDP-glucuronate biosynthetic process [GO:0006065]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
identical protein binding [GO:0042802]; NAD binding [GO:0051287]; UDP-glucose 6-dehydrogenase activity [GO:0003979]
|
PF00984;PF03720;PF03721;
|
1.20.5.100;3.40.50.720;
|
UDP-glucose/GDP-mannose dehydrogenase family
| null | null |
CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000269|PubMed:9737970};
| null |
PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1. {ECO:0000269|PubMed:9737970}.
| null | null |
FUNCTION: Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans (PubMed:9737970). Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (PubMed:14505572). Required for proper brain and neuronal development (By similarity). {ECO:0000250|UniProtKB:O60701, ECO:0000269|PubMed:14505572, ECO:0000269|PubMed:9737970}.
|
Mus musculus (Mouse)
|
O70477
|
PKNX1_MOUSE
|
MMATQTLSIDSYQDGQQMQVVTELKTEQDPNCSDPDAEGVSPPPIESQTPMDADKQAIYRHPLFPLLALLFEKCEQSTQGSEGTTSASFDVDIENFVRKQEKDGKPFFCEDPETDNLMVKAIQVLRIHLLELEKVNELCKDFCSRYIACLKTKMNSETLLSGEPGSPYSPVQSQQIQSAITGTLSPQGIVVPASALQQGNVTMATVAGGTVYQPVTVVTPQGQVVTQALSPGTIRIQNSQLQLQLNQDLSILHQEDGSSKNKRGVLPKHATNVMRSWLFQHIGHPYPTEDEKKQIAAQTNLTLLQVNNWFINARRRILQPMLDSSCSETPKTKKKPAQNRPVQRFWPDSLASGVAQATPSELAMSEGAVVTITTPVNMNVDSLQSLSSDGATLAVQQVMMAGQSEDESVDSTEDEGGALAPTHISGLVLENSDSLQ
| null | null |
angiogenesis [GO:0001525]; camera-type eye development [GO:0043010]; erythrocyte differentiation [GO:0030218]; hemopoiesis [GO:0030097]; 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]; T cell differentiation [GO:0030217]
|
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
|
PF05920;PF16493;
|
1.10.10.60;
|
TALE/MEIS homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Activates transcription in the presence of PBX1A and HOXA1. {ECO:0000269|PubMed:29465778}.; FUNCTION: (Microbial infection) In complex with PBX1, binds to the 5'-TGATTGAC-3' consensus sequence in the U5 region of Moloney murine leukemia virus and promotes viral transcription. {ECO:0000269|PubMed:12529389}.
|
Mus musculus (Mouse)
|
O70480
|
VAMP4_MOUSE
|
MPPKFKRHLNDDDVTGSVKSERRNLLEDDSDEEEDFFLRGPSGPRFGPRNDKIKHVQNQVDEVIDVMQENITKVIERGERLDELQDKSESLSDNATAFSNRSKQLRRQMWWRGCKIKAIMALAAAILLLMIIILIVVKFRT
| null | null |
cellular response to type II interferon [GO:0071346]; Golgi ribbon formation [GO:0090161]; Golgi to plasma membrane protein transport [GO:0043001]; regulation of Golgi to plasma membrane protein transport [GO:0042996]; regulation of synaptic vesicle endocytosis [GO:1900242]; SNARE complex assembly [GO:0035493]; synaptic vesicle to endosome fusion [GO:0016189]
|
Golgi apparatus [GO:0005794]; phagocytic vesicle [GO:0045335]; presynaptic endosome membrane [GO:0098954]; SNARE complex [GO:0031201]; trans-Golgi network [GO:0005802]
| null |
PF00957;
|
1.20.5.110;
|
Synaptobrevin family
|
PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type X (BoNT/X) which hydrolyzes the 87-Arg-|-Ser-88 bond and probably inhibits neurotransmitter release (PubMed:28770820). It remains unknown whether BoNT/X is ever produced, or what organisms it targets. {ECO:0000269|PubMed:28770820}.
|
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Note=Associated with trans Golgi network (TGN) and newly formed immature secretory granules (ISG). Not found on the mature secretory organelles (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Involved in the pathway that functions to remove an inhibitor (probably synaptotagmin-4) of calcium-triggered exocytosis during the maturation of secretory granules. May be a marker for this sorting pathway that is critical for remodeling the secretory response of granule (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O70481
|
UBR1_MOUSE
|
MADEEMDGAERMDVSPEPPLAPQRPASWWDQQVDFYTAFLHHLAQLVPEIYFAEMDPDLEKQEESVQMSILTPLEWYLFGEDPDICLEKLKHSGAFQLCGKVFKSGETTYSCRDCAIDPTCVLCMDCFQSSVHKNHRYKMHTSTGGGFCDCGDTEAWKTGPFCVDHEPGRAGTTKESLHCPLNEEVIAQARRIFPSVIKYIVEMTIWEEEKELPPELQIREKNERYYCVLFNDEHHSYDHVIYSLQRALDCELAEAQLHTTAIDKEGRRAVKAGVYATCQEAKEDIKSHSENVSQHPLHVEVLHSVVMAHQKFALRLGSWMNKIMSYSSDFRQIFCQACLVEEPGSENPCLISRLMLWDAKLYKGARKILHELIFSSFFMEMEYKKLFAMEFVKYYKQLQKEYISDDHERSISITALSVQMLTVPTLARHLIEEQNVISVITETLLEVLPEYLDRNNKFNFQGYSQDKLGRVYAVICDLKYILISKPVIWTERLRAQFLEGFRSFLKILTCMQGMEEIRRQVGQHIEVDPDWEAAIAIQMQLKNILLMFQEWCACDEDLLLVAYKECHKAVMRCSTNFMSSTKTVVQLCGHSLETKSYKVSEDLVSIHLPLSRTLAGLHVRLSRLGAISRLHEFVPFDGFQVEVLVEYPLRCLVLVAQVVAEMWRRNGLSLISQVFYYQDVKCREEMYDKDIIMLQIGASIMDPNKFLLLVLQRYELTDAFNKTISTKDQDLIKQYNTLIEEMLQVLIYIVGERYVPGVGNVTREEVIMREITHLLCIEPMPHSAIARNLPENENNETGLENVINKVATFKKPGVSGHGVYELKDESLKDFNMYFYHYSKTQHSKAEHMQKKRRKQENKDEALPPPPPPEFCPAFSKVVNLLSCDVMMYILRTIFERAVDMESNLWTEGMLQMAFHILALGLLEEKQQLQKAPEEEVAFDFYHKASRLGSSAMNAQNIQMLLEKLKGIPQLESQKDMITWILQMFDTVKRLREKSCLVVATTSGLECVKSEEITHDKEKAERKRKAEAARLHRQKIMAQMSALQKNFIETHKLMYDNTSEVTGKEDSIMEEESTSAVSEASRIALGPKRGPAVTEKEVLTCILCQEEQEVKLENNAMVLSACVQKSTALTQHRGKPVDHLGETLDPLFMDPDLAHGTYTGSCGHVMHAVCWQKYFEAVQLSSQQRIHVDLFDLESGEYLCPLCKSLCNTVIPIIPLQPQKINSENAEALAQLLTLARWIQTVLARISGYNIKHAKGEAPAVPVLFNQGMGDSTFEFHSILSFGVQSSVKYSNSIKEMVILFATTIYRIGLKVPPDELDPRVPMMTWSTCAFTIQAIENLLGDEGKPLFGALQNRQHNGLKALMQFAVAQRTTCPQVLIHKHLARLLSVILPNLQSENTPGLLSVDLFHVLVGAVLAFPSLYWDDTVDLQPSPLSSSYNHLYLFHLITMAHMLQILLTTDTDLSSGPPLAEGEEDSEEARCASAFFVEVSQHTDGLAGCGAPGWYLWLSLRNGITPYLRCAALLFHYLLGVAPPEELFANSAEGEFSALCSYLSLPTNLFLLFQEYWDTIRPLLQRWCGDPALLKSLKQKSAVVRYPRKRNSLIELPEDYSCLLNQASHFRCPRSADDERKHPVLCLFCGAILCSQNICCQEIVNGEEVGACVFHALHCGAGVCIFLKIRECRVVLVEGKARGCAYPAPYLDEYGETDPGLKRGNPLHLSRERYRKLHLVWQQHCIIEEIARSQETNQMLFGFNWQLL
|
2.3.2.27
| null |
cellular response to leucine [GO:0071233]; negative regulation of TOR signaling [GO:0032007]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511]; ubiquitin-dependent protein catabolic process via the N-end rule pathway [GO:0071596]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; proteasome complex [GO:0000502]; ubiquitin ligase complex [GO:0000151]
|
leucine binding [GO:0070728]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]
|
PF02617;PF18995;PF02207;
|
2.10.110.30;3.30.1390.10;
|
UBR1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {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;
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. May be involved in pancreatic homeostasis. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth (By similarity). {ECO:0000250, ECO:0000269|PubMed:11689692, ECO:0000269|PubMed:14585983, ECO:0000269|PubMed:16311597}.
|
Mus musculus (Mouse)
|
O70490
|
ACSM2_RAT
|
MHWLWKIPRLCTFWGTEMFHRTFHMNIKKLMPIQWGHQEVPAKFNFASDVIDHWASLEKAGKRSPGPALWWMNGSGEELKWNFRELSEISKQTANVLTGACGLQRGDRVAVVLPRVPEWWLVTLGCMRSGLVFMPGTTQMKSTDILYRLQSSKARAIVAGDEVVQEVDAVAPDCSFLKIKLLVSEKNREGWLNFKALLKDASPIHQCVETVSQESAAIYFTSGTSGPPKMAEHSHCSLGLKAKMDAGWTGLGPSDTMWTISDTGWILNILGSFLEPWVLGTCIFVHLLPKFDPQTVLKVLSSYPINTLLGAPLIYRMLLQQDLSSYKFPHLHSCFSGGETLLPETLESWKAKTGLEIREIYGQTETGITCRVSRTMKVKPGYLGTAIVPYDVQVIDEQGNVLPPGKEGDMALRVKPIRPIGMFSGYVDNPKKTQANIRGDFWLLGDRGIKDTEGYFHFMGRTDDIINSSGYRIGPSEVENALMEHPAVVETAVISSPDPIRREVVKAFVVLAPEFLSHDQDQLTKVLQEHVKSVTAPYKYPRKVEFVLDLPKTITGKIERAKLRAKEWKTSG
|
6.2.1.2; 6.2.1.25
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q68CK6}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q68CK6};
|
acyl-CoA metabolic process [GO:0006637]; fatty acid biosynthetic process [GO:0006633]; medium-chain fatty-acyl-CoA metabolic process [GO:0036112]
|
mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; benzoate-CoA ligase activity [GO:0018858]; butyrate-CoA ligase activity [GO:0047760]; decanoate-CoA ligase activity [GO:0102391]; fatty acid ligase activity [GO:0015645]; fatty-acyl-CoA synthase activity [GO:0004321]; metal ion binding [GO:0046872]
|
PF00501;PF13193;
|
3.30.300.30;3.40.50.12780;
|
ATP-dependent AMP-binding enzyme family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q68CK6}.
|
CATALYTIC ACTIVITY: Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2; Evidence={ECO:0000250|UniProtKB:Q68CK6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341; Evidence={ECO:0000250|UniProtKB:Q68CK6}; CATALYTIC ACTIVITY: Reaction=ATP + benzoate + CoA = AMP + benzoyl-CoA + diphosphate; Xref=Rhea:RHEA:10132, ChEBI:CHEBI:16150, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57369, ChEBI:CHEBI:456215; EC=6.2.1.25; Evidence={ECO:0000250|UniProtKB:Q68CK6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10133; Evidence={ECO:0000250|UniProtKB:Q68CK6}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA; Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q68CK6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741; Evidence={ECO:0000250|UniProtKB:Q68CK6}; CATALYTIC ACTIVITY: Reaction=ATP + butanoate + CoA = AMP + butanoyl-CoA + diphosphate; Xref=Rhea:RHEA:46172, ChEBI:CHEBI:17968, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q68CK6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173; Evidence={ECO:0000250|UniProtKB:Q68CK6}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA; Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q68CK6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632; Evidence={ECO:0000250|UniProtKB:Q68CK6}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + decanoate = AMP + decanoyl-CoA + diphosphate; Xref=Rhea:RHEA:33627, ChEBI:CHEBI:27689, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q68CK6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33628; Evidence={ECO:0000250|UniProtKB:Q68CK6};
| null | null | null | null |
FUNCTION: Catalyzes the activation of fatty acids by CoA to produce an acyl-CoA, the first step in fatty acid metabolism (By similarity). Capable of activating medium-chain fatty acids (e.g. butyric (C4) to decanoic (C10) acids), and certain carboxylate-containing xenobiotics, e.g. benzoate (By similarity). {ECO:0000250|UniProtKB:Q68CK6}.
|
Rattus norvegicus (Rat)
|
O70491
|
STRA6_MOUSE
|
MESQASENGSQTSSGVTDDYSSWYIEEPLGAEEVQPEGVIPLCQLTAPPALLHACLASLSFLVLLLLALLVRRRRLWPRCGHRGLGLPSPVDFLAGDLSWTVPAAVFVVLFSNLCLLLPDENPLPFLNLTAASSPDGEMETSRGPWKLLALLYYPALYYPLAACASAGHQAAFLLGTVLSWAHFGVQVWQKAECPQDPKIYKHYSLLASLPLLLGLGFLSLWYPVQLVQSLRHRTGAGSQGLQTSYSEKYLRTLLCPKKLDSCSHPASKRSLLSRAWAFSHHSIYTPQPGFRLPLKLVISATLTGTATYQVALLLLVSVVPTVQKVRAGINTDVSYLLAGFGIVLSEDRQEVVELVKHHLWTVEACYISALVLSCASTFLLLIRSLRTHRANLQALHRGAALDLDPPLQSIHPSRQAIVSWMSFCAYQTAFSCLGLLVQQVIFFLGTTSLAFLVFVPLLHGRNLLLLRSLESTWPFWLTVALAVILQNIAANWIFLRTHHGYPELTNRRMLCVATFLLFPINMLVGAIMAVWRVLISSLYNTVHLGQMDLSLLPQRAASLDPGYHTYQNFLRIEASQSHPGVIAFCALLLHAPSPQPRPPLAPQDSLRPAEEEEGMQLLQTKDLMAKGAGHKGSQSRARWGLAYTLLHNPSLQAFRKAALTSAKANGTQP
| null | null |
camera-type eye development [GO:0043010]; establishment of localization in cell [GO:0051649]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; retinol transport [GO:0034633]; vitamin A import into cell [GO:0071939]
|
plasma membrane [GO:0005886]
|
retinal binding [GO:0016918]; retinol binding [GO:0019841]; retinol transmembrane transporter activity [GO:0034632]; signaling receptor activity [GO:0038023]
|
PF14752;
| null | null |
PTM: Phosphorylated on tyrosine residues in response to RBP4 binding (PubMed:21368206). Phosphorylation requires the presence of LRAT, suggesting it may be triggered by the uptake of retinol that is then metabolized within the cell to retinoids that function as signaling molecules (By similarity). {ECO:0000250|UniProtKB:Q9BX79, ECO:0000269|PubMed:21368206}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9203140}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q0V8E7}. Note=In the retinal pigment epithelium localizes to the basolateral membrane (PubMed:22467576, PubMed:24852372). Plasma membrane of the basal pole of Sertoli cells, absent in plasma membrane of neighboring spermatogonia (PubMed:9203140). {ECO:0000250|UniProtKB:Q0V8E7, ECO:0000269|PubMed:22467576, ECO:0000269|PubMed:9203140}.
| null | null | null | null | null |
FUNCTION: Functions as a retinol transporter (PubMed:23839944, PubMed:24852372). Accepts all-trans retinol from the extracellular retinol-binding protein RBP4, facilitates retinol transport across the cell membrane, and then transfers retinol to the cytoplasmic retinol-binding protein RBP1. Retinol uptake is enhanced by LRAT, an enzyme that converts retinol to all-trans retinyl esters, the storage forms of vitamin A (By similarity). Contributes to the activation of a signaling cascade that depends on retinol transport and LRAT-dependent generation of retinol metabolites that then trigger activation of JAK2 and its target STAT5, and ultimately increase the expression of SOCS3 and inhibit cellular responses to insulin (PubMed:21368206, PubMed:23839944). Important for the homeostasis of vitamin A and its derivatives, such as retinoic acid and 11-cis-retinal (PubMed:22467576, PubMed:24852372). STRA6-mediated transport is particularly important in the eye, and under conditions of dietary vitamin A deficiency (PubMed:22467576, PubMed:23839944, PubMed:24852372). Does not transport retinoic acid (By similarity). {ECO:0000250|UniProtKB:Q9BX79, ECO:0000269|PubMed:21368206, ECO:0000269|PubMed:22467576, ECO:0000269|PubMed:23839944, ECO:0000269|PubMed:24852372}.
|
Mus musculus (Mouse)
|
O70492
|
SNX3_MOUSE
|
MAETVADTRRLITKPQNLNDAYGPPSNFLEIDVSNPQTVGVGRGRFTTYEIRVKTNLPIFKLKESTVRRRYSDFEWLRSELERESKVVVPPLPGKAFLRHVPFRGDDGIFDDNFIEERKQGLEQFINKVAGHPLAQNERCLHMFLQDEIIDKSYTPSKIRHA
| null | null |
endocytic recycling [GO:0032456]; heme biosynthetic process [GO:0006783]; hemoglobin biosynthetic process [GO:0042541]; late endosome to Golgi transport [GO:0034499]; negative regulation of phagocytosis [GO:0050765]; positive regulation of neuron projection development [GO:0010976]; protein to membrane docking [GO:0022615]; regulation of intracellular protein transport [GO:0033157]; regulation of protein metabolic process [GO:0051246]; regulation of Wnt signaling pathway [GO:0030111]; transferrin transport [GO:0033572]
|
clathrin-coated vesicle [GO:0030136]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; early phagosome [GO:0032009]; endosome membrane [GO:0010008]; retromer complex [GO:0030904]
|
phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]; retromer complex binding [GO:1905394]
|
PF00787;
|
3.30.1520.10;
|
Sorting nexin family
|
PTM: Ubiquitinated, leading to its proteasomal degradation. Deubiquitinated by USP10. {ECO:0000269|PubMed:18632802}.
|
SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:23416069}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:O60493}. Note=Colocalizes to clathrin-coated endosomal vesicles morphologically distinct from retromer-decorated non-branched endosomal tubule structures. Colocalizes with EEA1 on nascent phagosomes in dendritic cells but competes with EEA1 for binding to phagosomal membrane (By similarity). {ECO:0000250|UniProtKB:O60493, ECO:0000269|PubMed:23416069}.
| null | null | null | null | null |
FUNCTION: Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Can also bind phosphatidylinositol 4-phosphate (PtdIns(P4)), phosphatidylinositol 5-phosphate (PtdIns(P5)) and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2) (PubMed:19576982). Plays a role in protein transport between cellular compartments. Together with RAB7A facilitates endosome membrane association of the retromer cargo-selective subcomplex (CSC). May act in part as component of the SNX3-retromer complex which mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway (By similarity). Promotes stability and cell surface expression of epithelial sodium channel (ENAC) subunits SCNN1A and SCNN1G (PubMed:18632802). Not involved in EGFR degradation. Involved in the regulation of phagocytosis in dendritic cells possibly by regulating EEA1 recruitment to the nascent phagosomes (By similarity). Involved in iron homeostasis through regulation of endocytic recycling of the transferrin receptor Tfrc presuambly by delivering the transferrin:transferrin receptor complex to recycling endosomes; the function may involve the CSC retromer subcomplex (PubMed:23416069). Involved in regulation of neurite outgrowth in primary neurons (PubMed:19576982). {ECO:0000250|UniProtKB:O60493, ECO:0000269|PubMed:18632802, ECO:0000269|PubMed:23416069}.
|
Mus musculus (Mouse)
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.