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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O35089
|
CNIH2_MOUSE
|
MAFTFAAFCYMLTLVLCASLIFFVIWHIIAFDELRTDFKNPIDQGNPARARERLKNIERICCLLRKLVVPEYSIHGLFCLMFLCAAEWVTLGLNIPLLFYHLWRYFHRPADGSEVMYDAVSIMNADILNYCQKESWCKLAFYLLSFFYYLYSMVYTLVSF
| null | null |
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; localization within membrane [GO:0051668]; negative regulation of anterograde synaptic vesicle transport [GO:1903743]; negative regulation of receptor localization to synapse [GO:1902684]; regulation of AMPA receptor activity [GO:2000311]; regulation of membrane potential [GO:0042391]; synaptic transmission, glutamatergic [GO:0035249]
|
AMPA glutamate receptor complex [GO:0032281]; COPII-coated ER to Golgi transport vesicle [GO:0030134]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; endoplasmic reticulum membrane [GO:0005789]; glutamatergic synapse [GO:0098978]; postsynaptic density [GO:0014069]; postsynaptic density membrane [GO:0098839]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]
|
channel regulator activity [GO:0016247]
|
PF03311;
| null |
Cornichon family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Postsynaptic density {ECO:0000269|PubMed:21172611}. Cell projection, dendrite {ECO:0000269|PubMed:21172611}. Cell projection, dendritic spine {ECO:0000269|PubMed:21172611}. Postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Also localizes to the cell membrane of extrasynaptic sites (dendritic shafts, spines of pyramidal cells). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by regulating their rates of activation, deactivation and desensitization. Blocks CACNG8-mediated resensitization of AMPA receptors. {ECO:0000269|PubMed:20805473, ECO:0000269|PubMed:21172611}.
|
Mus musculus (Mouse)
|
O35095
|
NCDN_RAT
|
MSCCDLAAAGQLGKAGIMASDCEPALNQAESRNPTLERYLGALREAKNDSEQFAALLLVTKAVKAGDIDAKTRRRIFDAVGFTFPNRLLTTKEAPDGCPDHVLRALGVALLACFCSDPELASHPQVLNKIPILCTFLTARGDPDDAARRSMIDDTYQCLTAVAGTPRGPRHLIAGGTVSALCQAYLGHGYGFDQALALLVGLLAAAETQCWKEAEPDLLAVLRGLSEDFQRAEDASKFELCQLLPLFLPPTTVPPECHRDLQAGLARILGSKLSSWQRNPALKLAARLAHACGSDWIPVGSSGSKFLALLVNLACVEVRLALEETGTEVKEDVVTACYALMELGIQECTRCEQSLLKEPQKVQLVSIMKEAIGAVIHYLLRVGPEKQKEPFVFASVRILGAWLAEETSSLRKEVCQLLPFLVRYAKTLYEEAEEASDISQQVANLAISPTTPGPAWPGDALRLLLPGWCHLTVEDGPREILIKEGAPSLLCKYFLQQWELTSPGHDTSVLPDSVEIGLQTCCHIFLNLVVTAPGLIKRDACFTSLMNTLMTSLPSLVQQQGRLLLAANVATLGLLMARLLSTSPALQGTPASRGFFAAAILFLSQSHVARATPGSDQAVLALSPDYEGIWADLQELWFLGMQAFTGCVPLLPWLAPAALRSRWPQELLQLLGSVSPNSVKPEMVAAYQGVLVELARANRLCREAMRLQAGEETASHYRMAALEQCLSEP
| null | null |
bone resorption [GO:0045453]; neuron projection development [GO:0031175]; regulation of neuronal synaptic plasticity [GO:0048168]
|
cytosol [GO:0005829]; dendrite [GO:0030425]; endosome membrane [GO:0010008]; membrane [GO:0016020]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; postsynapse [GO:0098794]
| null |
PF05536;
| null |
Neurochondrin family
|
PTM: Palmitoylated (PubMed:23687301). Palmitoylation by ZDHHC1, ZDHHC3 and ZDHHC11 regulates the association of NCDN with endosome membranes (PubMed:23687301). May also be palmitoylated by ZDHHC7 (PubMed:23687301). {ECO:0000269|PubMed:23687301}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10521593}. Endosome membrane {ECO:0000269|PubMed:23687301}; Lipid-anchor {ECO:0000305|PubMed:23687301}. Cell projection, dendrite {ECO:0000269|PubMed:10521593, ECO:0000269|PubMed:23687301}. Postsynapse {ECO:0000269|PubMed:23687301}. Note=Localizes to somatic regions of neurons (PubMed:10521593, PubMed:23687301). Localization to endosome membrane requires palmitoylation (PubMed:23687301). {ECO:0000269|PubMed:10521593, ECO:0000269|PubMed:23687301}.
| null | null | null | null | null |
FUNCTION: Probably involved in signal transduction, in the nervous system, via increasing cell surface localization of GRM5 and positively regulating its signaling. Required for the spatial learning process. Acts as a negative regulator of Ca(2+)-calmodulin-dependent protein kinase 2 (CaMK2) phosphorylation. May play a role in modulating melanin-concentrating hormone-mediated functions via its interaction with MCHR1 that interferes with G protein-coupled signal transduction. May be involved in bone metabolism. May also be involved in neurite outgrowth. {ECO:0000269|PubMed:9398642}.
|
Rattus norvegicus (Rat)
|
O35099
|
M3K5_MOUSE
|
MGTEAGEGITFSVPPFASVGFCTIPEGGSCRRGGGAATAAEGEPSLQPLLVPPPPPPPGSFWNVESAAAPGTSCPTTAPGSSATRGRGNSGSGGGRRTTVAYVINEASQGQLVVAESEALQSLREACEAVGATLETLHFGKLDFGETAVLDRFYNADIAVVEMSDAFRQPSLFYHLGVRESFSMANNIILYCDTNSDSLQSLKEIICQKNTVCTGNYTFIPYMVTPHNKVYCCDSSFMKGLTELMQPNFELLLGPICLPLVDRFVQLLKVAQASSSQYFRESILSDIRKARNLYTGKELAAELARIRQRVDNIEVLTADIVINLLLSYRDIQDYDSIVKLVETLEKLPTFDLASHHHVKFHYAFALNRRNLPGDRAKALDIMIPMVQSEEQVASDMYCLVGRIYKDMFLDSNFTDTESRDHGASWFKKAFESEPTLQSGINYAVLLLAAGHQFESSFELRKVGVKLSSLLGKKGNLEKLQSYWEVGFFLGASVLANDHLRVIQASEKLFRLKTPAWYLKSIVETILIYKHFVKLTTEQPSAKQELVDFWMDFLVEATKTDVTVVRFPVLILEPTKIYQPSYLSINNEVEEKTISIWHVLPDDKKGIHEWNFGASSVRGVSISKFEERCCFLYVLHNSDDFQIYFCTELHCKRFFEMVNTITEEKGRGAEDGDCEGDSLEYDYEYDENGDRVVLGKGTYGIVYAGRDLSNQVRIAIKEIPERDSRYSQPLHEEIALHKHLKHKNIVQYLGSFSENGFIKIFMEQVPGGSLSALLRSKWGPLKDNEQTIGFYTKQILEGLKYLHDNQIVHRDIKGDNVLINTYSGVLKISDFGTSKRLAGINPCTETFTGTLQYMAPEIIDKGPRGYGKAADIWSLGCTIIEMATGKPPFYELGEPQAAMFKVGMFKVHPEIPESMSAEAKAFILKCFEPDPDKRACANDLLIDEFLKVSSKKKKTQPKLSALSTGSNEYLRSISLPVPVLVEDTSSSSEYGSVSPDTELKADPFSFKARAKSCGEKDGKGIRTLFLGIPDENFEDHSAPPSPEEKDSGFFMLRKDSERRATLHRILTEDQDKVVRNLMESLAQGAEEPKLKWEHITTLISSLREFVRSTDRKIIATTLSKLKLELDFDSHGISQVQVVLFGFQDAVNKVLRNHNIKPHWMFALDSIIRKAVQTAITILVPELRPHFSLASESDTADPEDLDVEDEHEELSSNQTVRRPQAITEDAVATSGVSTLSSTVSHDSQNAHRSLNVQLGRMKIETNRLLEELVRKERELQALLHQAIEEKDQEIRHLKLKSQPIDIPGFPVCHLNSPGTTTEDSELPGWLRENGADEDTISRFLAEDYTLVDVLYYVTRDDLKCLRLRGGMLCTLWKAIIDFRNKC
|
2.7.11.25
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
cellular response to amino acid starvation [GO:0034198]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to reactive nitrogen species [GO:1902170]; cellular response to tumor necrosis factor [GO:0071356]; endothelial cell apoptotic process [GO:0072577]; innate immune response [GO:0045087]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; JNK cascade [GO:0007254]; MAPK cascade [GO:0000165]; neuron apoptotic process [GO:0051402]; neuron intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0036480]; p38MAPK cascade [GO:0038066]; phosphorylation [GO:0016310]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of JNK cascade [GO:0046330]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of p38MAPK cascade [GO:1900745]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; programmed necrotic cell death [GO:0097300]; regulation of programmed cell death [GO:0043067]; response to endoplasmic reticulum stress [GO:0034976]; response to ischemia [GO:0002931]; stress-activated MAPK cascade [GO:0051403]
|
external side of plasma membrane [GO:0009897]; IRE1-TRAF2-ASK1 complex [GO:1990604]; protein kinase complex [GO:1902911]
|
ATP binding [GO:0005524]; JUN kinase kinase kinase activity [GO:0004706]; magnesium ion binding [GO:0000287]; MAP kinase kinase kinase activity [GO:0004709]; protein domain specific binding [GO:0019904]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein phosphatase binding [GO:0019903]; protein serine kinase activity [GO:0106310]
|
PF19039;PF20309;PF20302;PF13281;PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily
|
PTM: Ser-90 and Ser-1040 are inactivating phosphorylation sites, the former of which is phosphorylated by AKT1 (By similarity). Phosphorylated at Ser-973 which induces association of MAP3K5/ASK1 with the 14-3-3 family proteins and suppresses MAP3K5/ASK1 activity (PubMed:16648474). Calcineurin (CN) dephosphorylates this site. Also dephosphorylated and activated by PGAM5 (By similarity). Phosphorylated at Thr-845 through autophosphorylation and by MAP3K6/ASK2 which leads to activation (PubMed:11920685, PubMed:18948261, PubMed:22399290). Thr-845 is dephosphorylated by PPP5C (PubMed:22399290). Phosphorylation at Ser-973 in response to oxidative stress is negatively regulated by PPIA/CYPA (By similarity). {ECO:0000250|UniProtKB:Q99683, ECO:0000269|PubMed:11920685, ECO:0000269|PubMed:16648474, ECO:0000269|PubMed:18948261, ECO:0000269|PubMed:22399290}.; PTM: Ubiquitinated. Tumor necrosis factor (TNF) induces TNFR2-dependent ubiquitination, leading to proteasomal degradation. Ubiquitinated by RC3H2 in a TRIM48-dependent manner. {ECO:0000250|UniProtKB:Q99683}.; PTM: Methylation at Arg-85 and Arg-87 by PRMT1 promotes association of MAP3K5 with thioredoxin and negatively regulates MAP3K5 association with TRAF2, inhibiting MAP3K5 activation. Methylation is blocked by ubiquitination of PRMT1 by TRIM48. {ECO:0000250|UniProtKB:Q99683}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99683}. Endoplasmic reticulum {ECO:0000250}. Note=Interaction with 14-3-3 proteins alters the distribution of MAP3K5/ASK1 and restricts it to the perinuclear endoplasmic reticulum region. {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=2.7.11.25; Evidence={ECO:0000269|PubMed:16648474}; 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=2.7.11.25; Evidence={ECO:0000269|PubMed:16648474};
| null | null | null | null |
FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signaling for determination of cell fate such as differentiation and survival. Plays a crucial role in the apoptosis signal transduction pathway through mitochondria-dependent caspase activation. MAP3K5/ASK1 is required for the innate immune response, which is essential for host defense against a wide range of pathogens. Mediates signal transduction of various stressors like oxidative stress as well as by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF) or lipopolysaccharide (LPS). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K4/SEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs). Both p38 MAPK and JNKs control the transcription factors activator protein-1 (AP-1). {ECO:0000269|PubMed:11266364, ECO:0000269|PubMed:14749717, ECO:0000269|PubMed:15864310, ECO:0000269|PubMed:16527894, ECO:0000269|PubMed:16648474}.
|
Mus musculus (Mouse)
|
O35111
|
KCNK3_MOUSE
|
MKRQNVRTLALIVCTFTYLLVGAAVFDALESEPEMIERQRLELRQLELRARYNLSEGGYEELERVVLRLKPHKAGVQWRFAGSFYFAITVITTIGYGHAAPSTDGGKVFCMFYALLGIPLTLVMFQSLGERINTFVRYLLHRAKRGLGMRHAEVSMANMVLIGFVSCISTLCIGAAAFSYYERWTFFQAYYYCFITLTTIGFGDYVALQKDQALQTQPQYVAFSFVYILTGLTVIGAFLNLVVLRFMTMNAEDEKRDAEHRALLTHNGQAVGLGGLSCLSGSLGDGVRPRDPVTCAAAAGGVGVGVGGSGFRNVYAEVLHFQSMCSCLWYKSREKLQYSIPMIIPRDLSTSDTCVEHSHSSPGGGGRYSDTPSHPCLCSGTQRSAISSVSTGLHSLAAFRGLMKRRSSV
| null | null |
cellular response to hypoxia [GO:0071456]; cellular response to zinc ion [GO:0071294]; cochlea development [GO:0090102]; negative regulation of cytosolic calcium ion concentration [GO:0051481]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of resting membrane potential [GO:0060075]; response to xenobiotic stimulus [GO:0009410]; stabilization of membrane potential [GO:0030322]
|
plasma membrane [GO:0005886]
|
open rectifier potassium channel activity [GO:0005252]; outward rectifier potassium channel activity [GO:0015271]; potassium ion leak channel activity [GO:0022841]; S100 protein binding [GO:0044548]
|
PF07885;
|
1.10.287.70;
|
Two pore domain potassium channel (TC 1.A.1.8) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14649}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O14649}.
| null | null | null | null | null |
FUNCTION: pH-dependent, voltage-insensitive, background potassium channel protein. Rectification direction results from potassium ion concentration on either side of the membrane. Acts as an outward rectifier when external potassium concentration is low. When external potassium concentration is high, current is inward. {ECO:0000250|UniProtKB:O14649}.
|
Mus musculus (Mouse)
|
O35112
|
CD166_RAT
|
MASKGSPSCRLVFCLLISAAVLRPGLGWYTVNSAYGDTIVMPCRLDVPQNLMFGKWKYEKPDGSPVFIAFRSSTKKSVQYDDVPEYKDRLSLSENYTLSINNAKISDEKRFVCMLVTEDNVFEAPTLVKVFKQPSKPEIVNRAAFLETEQLKKLGDCISRDSYPDGNITWYRNGKVLQPVDGEVSILFKKEIDPGTQLYTMTSSLEYKTTKSDIQMPFTCSVTYYGPSGQKTIYSEQAIFDIYYPTEQVTIQVLPPKNAIKEGDNITLQCLGNGNPPPEEFMFYLPGQAEGIRSSNTYTLTDVRRNATGDYKCSLIDQRNMAASTTITVHYLDLSLNPSGEVTKQIGDTLPVSCTISASRNATVVWMKDNIRLRSSPSFSSLHYQDAGNYVCETALQEVEGLKKRESLTLIVEGKPQIKMTKKTDPSGLSKTIICHVEGFPKPAIQWTITGSGSVINQTEESPYINGRYYSKIIISPEENVTLTCTAENQLERTVNSLNVSAISIPEHDEADDISDENREKVNDQAKLIVGIVVGLLLAALVAGVVYWLYMKKSKTASKHVNKDLGNMEENKKLEENNHKTEA
| null | null |
adaptive immune response [GO:0002250]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; cell adhesion [GO:0007155]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; motor neuron axon guidance [GO:0008045]; neuron projection extension [GO:1990138]; retinal ganglion cell axon guidance [GO:0031290]
|
axon [GO:0030424]; dendrite [GO:0030425]; external side of plasma membrane [GO:0009897]; immunological synapse [GO:0001772]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; T cell receptor complex [GO:0042101]
|
identical protein binding [GO:0042802]
|
PF08205;PF13927;
|
2.60.40.10;
| null |
PTM: The N-terminus is blocked.; PTM: Glycosylated. {ECO:0000250|UniProtKB:Q13740}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q61490}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q61490}. Cell projection, axon {ECO:0000250|UniProtKB:Q61490}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q61490}. Note=Detected at the immunological synapse, i.e, at the contact zone between antigen-presenting dendritic cells and T-cells. Colocalizes with CD6 and the TCR/CD3 complex at the immunological synapse. {ECO:0000250|UniProtKB:Q13740}.
| null | null | null | null | null |
FUNCTION: Cell adhesion molecule that mediates both heterotypic cell-cell contacts via its interaction with CD6, as well as homotypic cell-cell contacts. Promotes T-cell activation and proliferation via its interactions with CD6 (By similarity). Contributes to the formation and maturation of the immunological synapse via its interactions with CD6 (By similarity). Mediates homotypic interactions with cells that express ALCAM. Mediates attachment of dendritic cells onto endothelial cells via homotypic interaction. Inhibits endothelial cell migration and promotes endothelial tube formation via homotypic interactions. Required for normal organization of the lymph vessel network. Required for normal hematopoietic stem cell engraftment in the bone marrow. Plays a role in hematopoiesis; required for normal numbers of hematopoietic stem cells in bone marrow. Promotes in vitro osteoblast proliferation and differentiation (By similarity). Promotes neurite extension, axon growth and axon guidance; axons grow preferentially on surfaces that contain ALCAM (By similarity). Mediates outgrowth and pathfinding for retinal ganglion cell axons (By similarity). {ECO:0000250|UniProtKB:P42292, ECO:0000250|UniProtKB:Q13740, ECO:0000250|UniProtKB:Q61490}.
|
Rattus norvegicus (Rat)
|
O35114
|
SCRB2_MOUSE
|
MGRCCFYTAGTLSLLLLVTSVTLLVARVFQKAVDQTIEKNMVLQNGTKVFNSWEKPPLPVYIQFYFFNVTNPEEILQGEIPLLEEVGPYTYRELRNKANIQFGENGTTISAVTNKAYVFERNQSVGDPNVDLIRTINIPLLTVVDLAQLTLLRELIEAMLKAYQQKLFVIHTVHELLWGYKDEILSLVHIFKPDVSPNFGLFYERNGTNDGEYVFLTGEDNYLNFSKIVEWNGKTSLDWWTTDTCNMINGTDGDSFHPLISKDEVLYLFPSDLCRSVHITFSSFENVEGLPAFRYKVPAEILANTSENAGFCIPEGNCMDSGVLNISICKNGAPIIMSFPHFYQADEKFVSAIKGMHPNKEEHESFVDINPLTGIILRGAKRFQINTYVRKLDDFVETGDIRTMVFPVMYLNESVLIDKETANQLKSVINTTLVVTNIPYIIMALGVFFGLVFTWLACRGQGSMDEGTADERAPLIRT
| null | null |
aminophospholipid transport [GO:0015917]; endosome to plasma membrane protein transport [GO:0099638]; positive regulation of neuron projection development [GO:0010976]; protein targeting to lysosome [GO:0006622]; receptor-mediated endocytosis [GO:0006898]; regulation of carbohydrate catabolic process [GO:0043470]; regulation of glucosylceramidase activity [GO:1905123]; sensory perception of sound [GO:0007605]
|
cytoplasm [GO:0005737]; endocytic vesicle membrane [GO:0030666]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]
|
cargo receptor activity [GO:0038024]; cholesterol binding [GO:0015485]; enzyme binding [GO:0019899]; phosphatidylcholine binding [GO:0031210]; phosphatidylserine binding [GO:0001786]; protein homodimerization activity [GO:0042803]; protein-folding chaperone binding [GO:0051087]; scavenger receptor activity [GO:0005044]
|
PF01130;
| null |
CD36 family
|
PTM: Acylated by palmitic acid group(s). {ECO:0000250}.; PTM: Heavily glycosylated. {ECO:0000269|PubMed:19349973}.
|
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:24162852, ECO:0000269|PubMed:9399579}; Multi-pass membrane protein {ECO:0000269|PubMed:24162852, ECO:0000269|PubMed:9399579}.
| null | null | null | null | null |
FUNCTION: Acts as a lysosomal receptor for glucosylceramidase (GBA1) targeting. {ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:24162852}.
|
Mus musculus (Mouse)
|
O35115
|
FHL2_RAT
|
MTERFDCHHCNESLYGKKYILKEENPHCVACFEELYANTCEECGTPIGCDCKDLSYKDRHWHEGCFHCSRCGSSLVDKPFAAKEEQLLCTDCYSNEYSSKCQECKKTIMPGTRKMEYKGSSWHETCFTCQRCQQPIGTKSFIPKENQNFCVPCYEKQYALQCVQCKKPITTGGVTYRDQPWHRECFVCTACKKQLSGQRFTARDEFPYCLTCFCDLYAKKCAGCTNPISGLGGTKYISFEERQWHNDCFNCKKCSLSLVGRGFLTERDDILCPDCGKDI
| 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:0000250|UniProtKB:Q14192}. 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}.
|
Rattus norvegicus (Rat)
|
O35116
|
CTND2_RAT
|
FPSVQSNAAAYLQHLCFGDNKIKAEIRRQGGIQLLVDLLDHRMTEVHRSACGALRNLVYGKANDDNKIALKNCGGIPALVRLLRKTTDLEIRELVTGVLWNLSSCDALKMPIIQDALAVLTNAVIIPHSGWENSPLQDDRKIQLHSSQVLRNATGCLRNVSSAGEEARRRMRECDGLTDALLYVIQSALGSSEIDSKTVENCVCILRNLSYRLAAETSQGQHMGTDELDGLLCGEANGKDAESSGCWGKKKKKKKSQDQWDGVG
| null | null |
cell-cell adhesion [GO:0098609]; cell-cell junction assembly [GO:0007043]; dendritic spine morphogenesis [GO:0060997]; learning [GO:0007612]; morphogenesis of a branching structure [GO:0001763]; regulation of canonical Wnt signaling pathway [GO:0060828]; regulation of postsynaptic membrane neurotransmitter receptor levels [GO:0099072]; regulation of synaptic plasticity [GO:0048167]; synapse organization [GO:0050808]
|
adherens junction [GO:0005912]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; nucleus [GO:0005634]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]
|
beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; structural constituent of postsynaptic density [GO:0098919]
|
PF00514;
|
1.25.10.10;
|
Beta-catenin family
|
PTM: O-glycosylated. {ECO:0000250}.; PTM: Phosphorylated by CDK5 (PubMed:17009320). Phosphorylated by GSK3B (By similarity). {ECO:0000250|UniProtKB:O35927, ECO:0000269|PubMed:17009320}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O35927}. Cell junction, adherens junction {ECO:0000250|UniProtKB:O35927}. Cell projection, dendrite {ECO:0000269|PubMed:17009320, ECO:0000269|PubMed:20623542}. Perikaryon {ECO:0000269|PubMed:17009320, ECO:0000269|PubMed:20623542}.
| null | null | null | null | null |
FUNCTION: Has a critical role in neuronal development, particularly in the formation and/or maintenance of dendritic spines and synapses (PubMed:25807484). Involved in the regulation of canonical Wnt signaling (By similarity). It probably acts on beta-catenin turnover, facilitating beta-catenin interaction with GSK3B, phosphorylation, ubiquitination and degradation (PubMed:20623542). May be involved in neuronal cell adhesion and tissue morphogenesis and integrity by regulating adhesion molecules. Functions as a transcriptional activator when bound to ZBTB33 (By similarity). {ECO:0000250|UniProtKB:O35927, ECO:0000250|UniProtKB:Q9UQB3, ECO:0000269|PubMed:20623542, ECO:0000269|PubMed:25807484}.
|
Rattus norvegicus (Rat)
|
O35118
|
GFRA3_MOUSE
|
MGLSWSPRPPLLMILLLVLSLWLPLGAGNSLATENRFVNSCTQARKKCEANPACKAAYQHLGSCTSSLSRPLPLEESAMSADCLEAAEQLRNSSLIDCRCHRRMKHQATCLDIYWTVHPARSLGDYELDVSPYEDTVTSKPWKMNLSKLNMLKPDSDLCLKFAMLCTLHDKCDRLRKAYGEACSGIRCQRHLCLAQLRSFFEKAAESHAQGLLLCPCAPEDAGCGERRRNTIAPSCALPSVTPNCLDLRSFCRADPLCRSRLMDFQTHCHPMDILGTCATEQSRCLRAYLGLIGTAMTPNFISKVNTTVALSCTCRGSGNLQDECEQLERSFSQNPCLVEAIAAKMRFHRQLFSQDWADSTFSVVQQQNSNPALRLQPRLPILSFSILPLILLQTLW
| null | null |
axon guidance [GO:0007411]; glial cell-derived neurotrophic factor receptor signaling pathway [GO:0035860]; nervous system development [GO:0007399]; neuron development [GO:0048666]; neuron migration [GO:0001764]; sympathetic nervous system development [GO:0048485]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; receptor complex [GO:0043235]
|
axon guidance receptor activity [GO:0008046]; coreceptor activity [GO:0015026]; glial cell-derived neurotrophic factor receptor activity [GO:0016167]; signaling receptor activity [GO:0038023]
|
PF02351;
|
1.10.220.110;
|
GDNFR family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O60609}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:O60609}.
| null | null | null | null | null |
FUNCTION: Receptor for artemin (ARTN), a growth factor that supports the survival of sensory and sympathetic peripheral neurons. ARTN-binding leads to autophosphorylation and activation of the RET receptor. {ECO:0000250|UniProtKB:O60609}.
|
Mus musculus (Mouse)
|
O35119
|
TRPC4_RAT
|
MAQFYYKRNVNAPYRDRIPLRIVRAESELSPSEKAYLNAVEKGDYASVKKSLEEAEIYFKININCIDPLGRTALLIAIENENLELIELLLSFNVYVGDALLHAIRKEVVGAVELLLNHKKPSGEKQVPPILLDKQFSEFTPDITPIILAAHTNNYEIIKLLVQKGVSVPRPHEVRCNCVECVSSSDVDSLRHSRSRLNIYKALASPSLIALSSEDPFLTAFQLSWELQELSKVENEFKSEYEELSRQCKQFAKDLLDQTRSSRELEIILNYRDDNSLIEEQSGNDLARLKLAIKYRQKEFVAQPNCQQLLASRWYDEFPGWRRRHWAVKMVTCFIIGLLFPVFSVCYLIAPKSPLGLFIRKPFIKFICHTASYLTFLFLLLLASQHIDRSDLNRQGPPPTIVEWMILPWVLGFIWGEIKQMWDGGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKYSALNPRESWDMWHPTLVAEALFAIANIFSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYEETKGLSCKGIRCEKQNNAFSTLFETLQSLFWSIFGLINLYVTNVKAQHEFTDFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKLWMSYFEEGGTLPTPFNVIPSPKSLWYLVKWIWTHLCKKKMRRKPESFGTIGRRAADNLRRHHQYQEVMRNLVKRYVAAMIREAKTEEGLTEENVKELKQDISSFRFEVLGLLRGSKLSTIQSANAASSASSADSDEKSHSEGNGKDKRKNLSLFDLTTLIHPRSAVIASERHNLSNGSALVVQEPPREKQRKVNFVADIKNFGLFHRRSKQNAAEQNANQIFSVSEEITRQQAAGALERNIQLESKGLASRGDRSIPGLNEQCVLVDHRERNTDTLGLQVGKRVCSSFKSEKVVVEDTVPIIPKEKHAQEEDSSIDYDLSPTDTVAHEDYVTTRL
| null | null |
calcium ion import [GO:0070509]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; gamma-aminobutyric acid secretion [GO:0014051]; oligodendrocyte differentiation [GO:0048709]; positive regulation of store-operated calcium entry [GO:0106129]; regulation of action potential firing rate [GO:0099605]; regulation of calcium ion transport [GO:0051924]; regulation of cytosolic calcium ion concentration [GO:0051480]
|
basolateral plasma membrane [GO:0016323]; calcium channel complex [GO:0034704]; cation channel complex [GO:0034703]; caveola [GO:0005901]; cell surface [GO:0009986]; cortical cytoskeleton [GO:0030863]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; calcium channel activity [GO:0005262]; inositol 1,4,5 trisphosphate binding [GO:0070679]; store-operated calcium channel activity [GO:0015279]
|
PF00023;PF12796;PF00520;PF08344;
|
1.25.40.20;
|
Transient receptor (TC 1.A.4) family, STrpC subfamily, TRPC4 sub-subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Thought to form non-selective a receptor-activated calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Acts as a cell-cell contact-dependent endothelial calcium entry channel. Has also been shown to be calcium-selective (By similarity). May also be activated by intracellular calcium store depletion. {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O35126
|
ATN1_MOUSE
|
MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARIEEPSAPKASKQGRSEEISESESEETSAPKKTKTEQELPRPQSPSDLDSLDGRSINDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYHPPPLFPPSPPPPDSTPRQPESGFEPHPSVPPTGYHAPMEPPTSRLFQGPPPGAPPTHPQLYPGNASGGVLSGPPMGPKGGAAASSVGAPSGGKQHPPPTTPIPISSSGASGAPPAKPPSAPVGGGSLPSAPPPASFPHVTPNLPPPPALRPLNNASASPPGMGAQPIPGHLPSPHAMGQGMSGLPPGPEKGPTLAPSPHPLPPASSSAPGPPMRYPYSSSSSSAAASSSSSSSSASQYPASQALPSYPHSFPPPTSMSVSNQPPKYTQPSLPSQAVWSQGPPPPPPYGRLLANNNTHPGPFPPTGGQSTAHPAAPTHHHHQQQPQQQHHHGNSGPPPPGAYPHPLESSNSHHAHPYNMSPSLGSLRPYPPGPAHLPPPHGQVSYNQAGPNGPPVSSSNSSGSSSQASYSCSHPSSSQGPQGASYPFPPVPPVTTSSATLSTVIATVASSPAGYKTASPPGPPQYSKRAPSPGSYKTATPPGYKPGSPPSFRTGTPPGYRGTSPPAGPGTFKPGSPTVGPGPLPPAGPSSLSSLPPPPAAPTTGPPLTATQIKQEPAEEYEPPESPVPPARSPSPPPKVVDVPSHASQSARFNKHLDRGFNSCARSDLYFVPLEGSKLAKKRADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLGPVPHRPPFEPGSAVATVPPYLGPDTPALRTLSEYARPHVMSPGNRNHPFYVPLGAVDPGLLGYNVPALYSSDPAAREREREARERDLRDRLKPGFEVKPSELEPLHGVPGPGLDPFPRHGGLALQPGPPGLHPFPFHPSLGPLERERLALAAGPALRPDMSYAERLAAERQHAERVAALGNDPLARLQMLNVTPHHHQHSHIHSHLHLHQQDAIHAASASVHPLIDPLASGSHLTRIPYPAGTLPNPLLPHPLHENEVLRHQLFAAPYRDLPASLSAPMSAAHQLQAMHAQSAELQRLALEQQQWLHAHHPLHSVPLPAQEDYYSHLKKESDKPL
| null | null |
cell killing [GO:0001906]; cell migration [GO:0016477]; determination of adult lifespan [GO:0008340]; maintenance of cell polarity [GO:0030011]; male gonad development [GO:0008584]; multicellular organism growth [GO:0035264]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron apoptotic process [GO:0051402]; post-embryonic development [GO:0009791]; regulation of neuron differentiation [GO:0045664]; response to food [GO:0032094]; spermatogenesis [GO:0007283]
|
anchoring junction [GO:0070161]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
JUN kinase binding [GO:0008432]; protein domain specific binding [GO:0019904]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]
|
PF03154;
| null | null |
PTM: Phosphorylated in vitro by MAPK8/JNK1 on Ser-724. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P54258}. Cell junction {ECO:0000250|UniProtKB:P54258}. Nucleus {ECO:0000250|UniProtKB:P54258}. Note=Shuttles between nucleus and cytoplasm. Colocalizes with FAT1 in the perinuclear area, at cell-cell junctions and leading edges of cells. Colocalizes with MTG8 in discrete nuclear dots (By similarity). {ECO:0000250|UniProtKB:P54258}.
| null | null | null | null | null |
FUNCTION: Transcriptional corepressor. Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of the poly-Q repeats (By similarity). Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation. {ECO:0000250|UniProtKB:P54259, ECO:0000269|PubMed:16702404, ECO:0000269|PubMed:19131340}.
|
Mus musculus (Mouse)
|
O35129
|
PHB2_MOUSE
|
MAQNLKDLAGRLPAGPRGMGTALKLLLGAGAVAYGVRESVFTVEGGHRAIFFNRIGGVQQDTILAEGLHFRIPWFQYPIIYDIRARPRKISSPTGSKDLQMVNISLRVLSRPNAQELPSMYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEAKQVAQQEAQRAQFLVEKAKQEQRQKIVQAEGEAEAAKMLGEALSKNPGYIKLRKIRAAQNISKTIATSQNRIYLTADNLVLNLQDESFTRGSDSLIKGKK
| null | null |
activation of phospholipase C activity [GO:0007202]; activation of protein kinase C activity [GO:1990051]; antiviral innate immune response [GO:0140374]; B cell activation [GO:0042113]; CD40 signaling pathway [GO:0023035]; cell migration [GO:0016477]; cellular response to hypoxia [GO:0071456]; cellular response to retinoic acid [GO:0071300]; intracellular estrogen receptor signaling pathway [GO:0030520]; mammary gland alveolus development [GO:0060749]; mammary gland branching involved in thelarche [GO:0060744]; mammary gland epithelial cell proliferation [GO:0033598]; mitochondrion organization [GO:0007005]; mitophagy [GO:0000423]; negative regulation of apoptotic process [GO:0043066]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of intracellular estrogen receptor signaling pathway [GO:0033147]; negative regulation of mammary gland epithelial cell proliferation [GO:0033600]; positive regulation of cell cycle G1/S phase transition [GO:1902808]; positive regulation of exit from mitosis [GO:0031536]; positive regulation of immunoglobulin production [GO:0002639]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; protein import into nucleus [GO:0006606]; protein stabilization [GO:0050821]; regulation of branching involved in mammary gland duct morphogenesis [GO:0060762]; regulation of cardiolipin metabolic process [GO:1900208]; regulation of cytochrome-c oxidase activity [GO:1904959]; RIG-I signaling pathway [GO:0039529]; sister chromatid cohesion [GO:0007062]
|
axon [GO:0030424]; cell surface [GO:0009986]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; inner mitochondrial membrane protein complex [GO:0098800]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrial prohibitin complex [GO:0035632]; mitochondrion [GO:0005739]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; presynaptic active zone [GO:0048786]; protein-containing complex [GO:0032991]
|
amide binding [GO:0033218]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; sphingolipid binding [GO:0046625]
|
PF01145;
|
3.30.479.30;
|
Prohibitin family
|
PTM: Phosphorylated. Tyrosine phosphorylation is indirectly stimulated by IGFBP6. {ECO:0000250|UniProtKB:Q99623}.
|
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:20959514, ECO:0000269|PubMed:24856930}. Cytoplasm {ECO:0000269|PubMed:15140878}. Nucleus {ECO:0000269|PubMed:15140878, ECO:0000269|PubMed:20959514}. Cell membrane {ECO:0000250|UniProtKB:Q99623}.
| null | null | null | null | null |
FUNCTION: Protein with pleiotropic attributes mediated in a cell-compartment- and tissue-specific manner, which include the plasma membrane-associated cell signaling functions, mitochondrial chaperone, and transcriptional co-regulator of transcription factors and sex steroid hormones in the nucleus. {ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:12878603, ECO:0000269|PubMed:15140878, ECO:0000269|PubMed:20959514, ECO:0000269|PubMed:23241883, ECO:0000269|PubMed:24856930, ECO:0000269|PubMed:28017329, ECO:0000269|PubMed:31522117}.; FUNCTION: In the mitochondria, together with PHB, forms large ring complexes (prohibitin complexes) in the inner mitochondrial membrane (IMM) and functions as a chaperone protein that stabilizes mitochondrial respiratory enzymes and maintains mitochondrial integrity in the IMM, which is required for mitochondrial morphogenesis, neuronal survival, and normal lifespan (Probable). The prohibitin complex, with DNAJC19, regulates cardiolipin remodeling and the protein turnover of OMA1 in a cardiolipin-binding manner (PubMed:31819158). Also regulates cytochrome-c oxidase assembly (COX) and mitochondrial respiration. Binding to sphingoid 1-phosphate (SPP) modulates its regulator activity (PubMed:11302691, PubMed:20959514). Has a key role of mitophagy receptor involved in targeting mitochondria for autophagic degradation (PubMed:28017329). Involved in mitochondrial-mediated antiviral innate immunity, activates RIG-I-mediated signal transduction and production of IFNB1 and pro-inflammatory cytokine IL6 (PubMed:31522117). {ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:20959514, ECO:0000269|PubMed:28017329, ECO:0000269|PubMed:31522117, ECO:0000269|PubMed:31819158, ECO:0000305}.; FUNCTION: In the nucleus, serves as transcriptional co-regulator (Probable). Acts as a mediator of transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases. Functions as an estrogen receptor (ER)-selective coregulator that potentiates the inhibitory activities of antiestrogens and represses the activity of estrogens. Competes with NCOA1 for modulation of ER transcriptional activity (PubMed:12878603, PubMed:15140878). {ECO:0000269|PubMed:12878603, ECO:0000269|PubMed:15140878, ECO:0000305}.; FUNCTION: In the plasma membrane, is involved in IGFBP6-induced cell migration (By similarity). Cooperates with CD86 to mediate CD86-signaling in B lymphocytes that regulates the level of IgG1 produced through the activation of distal signaling intermediates. Upon CD40 engagement, required to activate NF-kappa-B signaling pathway via phospholipase C and protein kinase C activation (PubMed:23241883). {ECO:0000250|UniProtKB:Q99623, ECO:0000269|PubMed:23241883}.
|
Mus musculus (Mouse)
|
O35130
|
NEP1_MOUSE
|
MSAASGGFQPRERRFSVQEQDWETTPPKKLRLGAGSKCGGRRLIVVLEGASLETVKVGKTYELLNCDRHKSMLLKNGRDPGEVRPDITHQSLLMLMDSPLNRAGLLQVYIHTQKNVLIEVNPQTRIPRTFDRFCGLMVQLLHKLSVRAADGPQKLLKVIKNPVSDHFPVGCMKIGTSFSVEDISDIRELVPSSDPVVFVVGAFAHGKVSVEYTEKMVSISNYPLSAALTCAKVTTAFEEVWGVI
|
2.1.1.-
| null |
blastocyst development [GO:0001824]; nucleologenesis [GO:0017126]; ribosomal small subunit biogenesis [GO:0042274]; rRNA base methylation [GO:0070475]
|
chromosome [GO:0005694]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; small-subunit processome [GO:0032040]
|
identical protein binding [GO:0042802]; rRNA (pseudouridine) methyltransferase activity [GO:0070037]; rRNA binding [GO:0019843]
|
PF03587;
|
3.40.1280.10;
|
Class IV-like SAM-binding methyltransferase superfamily, RNA methyltransferase NEP1 family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q92979}.
|
CATALYTIC ACTIVITY: Reaction=pseudouridine(1248) in human 18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylpseudouridine(1248) in human 18S rRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:46712, Rhea:RHEA-COMP:11638, Rhea:RHEA-COMP:11639, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65314, ChEBI:CHEBI:74890; Evidence={ECO:0000250|UniProtKB:Q92979};
| null | null | null | null |
FUNCTION: S-adenosyl-L-methionine-dependent pseudouridine N(1)-methyltransferase that methylates pseudouridine at position in 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Is not able to methylate uridine at this position (By similarity). Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 during the formation of pre-ribosomes (By similarity). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (By similarity). {ECO:0000250|UniProtKB:Q06287, ECO:0000250|UniProtKB:Q92979}.
|
Mus musculus (Mouse)
|
O35132
|
CP27B_RAT
|
MTQAVKLASRVFHRVQLPSQLGSDSVLRSLSDIPGPSTPSFLAELFCKGGLSRLHELQVHGAARYGPIWSGSFGTLRTVYVADPALVEQLLRQESHCPERCSFSSWSEHRRRHQRACGLLTADGEEWQRLRSLLAPLLLRPQAAAGYAGTLDSVVSDLVRRLRRQRGRGSGLPDLVLDVAGEFYKFGLEGIGAVLLGSRLGCLEAEVPPDTETFIEAVGSVFVSTLLTMAMPSWLHRLIPGPWARLCRDWDQMFAFAQKHVEQREGEAAVRNQGKPEEDLPTGHHLTHFLFREKVSVQSIVGNVTELLLAGVDTVSNTLSWALYELSRHPEVQSALHSEITGAVNPGSYAHLQATALSQLPLLKAVIKEVLRLYPVVPGNSRVPDRDICVGNYVIPQDTLVSLCHYATSRDPAQFREPNSFNPARWLGEGPAPHPFASLPFGFGKRSCIGRRLAELELQMALAQILTHFEVLPEPGALPVKPMTRTVLVPERSIHLQFVDR
|
1.14.15.18
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
|
bone mineralization [GO:0030282]; C21-steroid hormone biosynthetic process [GO:0006700]; calcitriol biosynthetic process from calciol [GO:0036378]; calcium ion homeostasis [GO:0055074]; calcium ion transport [GO:0006816]; cellular response to peptide hormone stimulus [GO:0071375]; cholesterol metabolic process [GO:0008203]; cortisol metabolic process [GO:0034650]; decidualization [GO:0046697]; G1 to G0 transition [GO:0070314]; glucocorticoid biosynthetic process [GO:0006704]; lactation [GO:0007595]; negative regulation of bone trabecula formation [GO:1900155]; negative regulation of cell growth [GO:0030308]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of ossification [GO:0030279]; positive regulation of keratinocyte differentiation [GO:0045618]; positive regulation of parathyroid hormone secretion [GO:2000830]; positive regulation of vitamin D receptor signaling pathway [GO:0070564]; regulation of bone mineralization [GO:0030500]; response to calcium ion [GO:0051592]; response to cAMP [GO:0051591]; response to copper ion [GO:0046688]; response to estrogen [GO:0043627]; response to insulin [GO:0032868]; response to lipopolysaccharide [GO:0032496]; response to peptide hormone [GO:0043434]; response to prostaglandin E [GO:0034695]; response to type II interferon [GO:0034341]; response to vitamin D [GO:0033280]; response to xenobiotic stimulus [GO:0009410]; vitamin D catabolic process [GO:0042369]; vitamin D metabolic process [GO:0042359]
|
cytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]
|
calcidiol 1-monooxygenase activity [GO:0004498]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; secalciferol 1-monooxygenase activity [GO:0062185]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Mitochondrion membrane.
|
CATALYTIC ACTIVITY: Reaction=calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = calcitriol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:20573, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17823, ChEBI:CHEBI:17933, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.14.15.18; Evidence={ECO:0000250|UniProtKB:O35084}; CATALYTIC ACTIVITY: Reaction=2 H(+) + O2 + 2 reduced [adrenodoxin] + secalciferol = calcitetrol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:49064, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28818, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:47799; EC=1.14.15.18; Evidence={ECO:0000250|UniProtKB:O35084};
| null |
PATHWAY: Hormone biosynthesis; cholecalciferol biosynthesis.
| null | null |
FUNCTION: Catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D3) to 1-alpha,25-dihydroxyvitamin D3 (1alpha,25(OH)(2)D3), and of 24,25-dihydroxyvitamin D3 (24,25(OH)(2)D3) to 1-alpha,24,25-trihydroxyvitamin D3 (1alpha,24,25(OH)(3)D3). Is also active with 25-hydroxy-24-oxo-vitamin D3. Plays an important role in normal bone growth, calcium metabolism, and tissue differentiation. {ECO:0000250|UniProtKB:O35084}.
|
Rattus norvegicus (Rat)
|
O35134
|
RPA1_MOUSE
|
MLASKHTPWRRLQGISFGMYSAEELKKLSVKSITNPRYVDYLGNPSANGLYDLALGPADSKEVCATCVQDFNNCSGHLGHIDLPLTVYNPFLFDKLYLLLRGSCLSCHMLTCPRAAIYLLISQLRVLEVGALQAVYELERILSRFLEETGDPSAFEIQEELEEYTSKILQNNLLGSQGTHVKNVCESRSKLVAQFWKTHMAAKQCPHCKTGRSVVRKEHNSKLIITYPATVHKKSDQEGTELPEGVPEAPGIDKAQMGKRGYLTPSSAQEHLFAIWKNEGFFLNYLFSGLDDIGPESSFNPSMFFLDFIVVPPSRYRPVNRLGDQMFTNGQTVNLQAVMKDAVLIRKLLALMAQEQKLPCEMTELTIDKENDSSVAIDRSFLGLLPGPSLTDKLYNIWIRLQSHVNIVFDSEMDKLMLEKYPGIRQILEKKEGLFRKHMMGKRVDYAARSVICPDMYINTNEIGIPMVFATKLTYPQPVTPWNVQELRQAVINGPNVHPGASMVINEDGSRTALSSVDAAQREAVAKQLLTPATGAPKPQGTKVVCRHVKNGDILLLNRQPTLHRPSIQAHRARILPEEKVLRLHYANCKAYNADFDGDEMNAHFPQSELGRAEAYVLACTDQQYLVPKDGQPLAGLIQDHMVSGANMTIRGCFFTREQYMELVYRGLTDKVGRVKLFPPAILKPFPLWTGKQVVSTLLINIIPEDYAPLNLSGKAKIGSKAWVKEKPRPIPDFDPDSMCESQVIIREGELLCGVLDKAHYGSSAYGLVHCCYEIYGGETSGRVLTCLARLFTAYLQLYRGFTLGVEDILVKPNADVVRQRIIEESTQCGPQAVKAALSLPETASCDEIQGKWQDAHLSKDQRDFNMIDMKFKEEVNHYSNEINKACMPLGLHRQFPENNLQMMVQSGAKGSTVNTMQISCLLGQIELEGRRPPLMASGKSLPCFEPYEFTPRAGGFVTGRFLTGIRPPEFFFHCMAGREGLVDTAVKTSRSGYLQRCIIKHLEGLVIQYDLTVRDSDGSVVQFLYGEDGLDIPKTQFLQPKQFPFLAGNYEVIMKSKHLHEVLSRADPQKVLGHIKAIKKWHHKHSGALLRKGAFLSFSQKIQAAVKALNLKGSIQNGRSPETQQMLQMWYDLDEESRWKYQKRAAPCPDPSLSVWRPDIYFASVSETFEKKIDDFSQEWAAQAERSYKKSELSLDRLRTLLQLKWQRSLCDPGEAVGLLAAQSIGEPSTQMTLNTFHFAGRGEMNVTLGIPRLREILMVASANIKTPMMSVPVFDTKKALKKVKSLKKRLTRVCLGEVLQKVDIQESFCMGEKRNKFQVYELRFQFLPHAYYQQEKCLRPEDILHFMETRFFKLLMEAIKKKKNKASAFRNVNSRRATQKDLNDTEDSGRSQREEERDEEEEGNIVDAEAEEGDADASDTKRKEKQEEEVDYESEEEGEEEEEEEVQEEGNIKGDGVHQGHEPDEEEHLGLEEEESSQKPPRRHSRPQGAEAIKRRIQAVRESYSFIEDYQYDTEESLWCQVTVKLPLMKINFDMSSLVVSLAHKAIVYTTKGITRCLLNETTNSKNEKELVLNTEGINLPELFKYSEILDLRRLYSNDIHAMANTYGIEAALRVIEKEIKDVFAVYGIAVDPRHLSLVADYMCFEGVYKPLNRFGIQSSSSPLQQMTFETSFQFLKQATMMGSHDELKSPSACLVVGKVVKGGTGLFELKQPLR
|
2.7.7.6
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O95602}; Note=Two Mg(2+) ions are coordinated by both the catalytic residues and the nucleic acid substrate to enhance substrate recognition and catalytic efficiency. {ECO:0000250|UniProtKB:O95602};
|
negative regulation of protein localization to nucleolus [GO:1904750]; rRNA transcription [GO:0009303]
|
chromosome [GO:0005694]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase I complex [GO:0005736]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; DNA/RNA hybrid binding [GO:0071667]; magnesium ion binding [GO:0000287]; RNA polymerase I activity [GO:0001054]; zinc ion binding [GO:0008270]
|
PF04997;PF00623;PF04983;PF05000;PF04998;
|
1.10.132.30;1.10.357.120;2.40.40.20;3.30.70.2850;6.10.250.2940;3.30.1490.180;4.10.860.120;1.10.274.100;
|
RNA polymerase beta' chain family
|
PTM: Phosphorylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:O95602}. Chromosome {ECO:0000269|PubMed:30272023, ECO:0000269|PubMed:30746471}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000250|UniProtKB:O95602, ECO:0000269|PubMed:10589839}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249; Evidence={ECO:0000250|UniProtKB:O95602, ECO:0000269|PubMed:10589839};
| null | null | null | null |
FUNCTION: Catalytic core component of RNA polymerase I (Pol I), a DNA-dependent RNA polymerase which synthesizes ribosomal RNA precursors using the four ribonucleoside triphosphates as substrates. Transcribes 47S pre-rRNAs from multicopy rRNA gene clusters, giving rise to 5.8S, 18S and 28S ribosomal RNAs (By similarity). Pol I-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol I pre-initiation complex (PIC) is recruited by the selectivity factor 1 (SL1/TIF-IB) complex bound to the core promoter that precedes an rDNA repeat unit. The PIC assembly bends the promoter favoring the formation of the transcription bubble and promoter escape. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Highly processive, assembles in structures referred to as 'Miller trees' where many elongating Pol I complexes queue and transcribe the same rDNA coding regions. At terminator sequences downstream of the rDNA gene, PTRF interacts with Pol I and halts Pol I transcription leading to the release of the RNA transcript and polymerase from the DNA (By similarity). Forms Pol I active center together with the second largest subunit POLR1B/RPA2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR1A/RPA1 contributing a Mg(2+)-coordinating DxDGD motif, and POLR1B/RPA2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and the template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. Has proofreading activity: Pauses and backtracks to allow the cleavage of a missincorporated nucleotide via POLR1H/RPA12. High Pol I processivity is associated with decreased transcription fidelity (By similarity) (PubMed:10589839). {ECO:0000250|UniProtKB:O95602, ECO:0000250|UniProtKB:P10964, ECO:0000269|PubMed:10589839}.
|
Mus musculus (Mouse)
|
O35136
|
NCAM2_MOUSE
|
MSLLLSFYLLGLLVRSGQALLQVTISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKGQTQEATVVLEIYQKLTFREVVSPQEFKQGEDAEVVCRVSSSPAPAVSWLYHNEEVTTIPDNRFAVLANNNLQILNINKSDEGIYRCEGRVEARGEIDFRDIIVIVNVPPAIMMPQKSFNATAERGEEMTLTCKASGSPDPTISWFRNGKLIEENEKYILKGSNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFLQVFVQPHILQLKNETTSENGHVTLVCEAEGEPVPEITWKRAIDGVMFSEGDKSPDGRIEVKGQHGRSSLHIRDVKLSDSGRYDCEAASRIGGHQRSMHLDIEYAPKFVSNQTMYYSWEGNPINISCDVTANPPASIHWRREKLLLPAKNTTHLKTHSVGRKMILEIAPTSDNDFGRYNCTATNRIGTRFQEYILELADVPSSPHGVKIIELSQTTAKISFNKPESHGGVPIHHYQVDVKEVASETWKIVRSHGVQTMVVLSSLEPNTTYEIRVAAVNGKGQGDYSKIEIFQTLPVREPSPPSIHGQPSSGKSFKISITKQDDGGAPILEYIVKYRSKDKEDQWLEKKVQGNKDHIILEHLQWTMGYEVQITAANRLGYSEPTVYEFSMPPKPNIIKDTLFNGLGLGAIIGLGVAALLLILVVTDVSCFFIRQCGLLMCITRRMCGKKSGSSGKSKELEEGKAAYLKDGSKEPIVEMRTEDERITNHEDGSPVNEPNETTPLTEPEKLPLKEENGKEVLNAETIEIKVSNDIIQSKEDDIKA
| null | null |
axonal fasciculation [GO:0007413]; cell adhesion [GO:0007155]
|
axon [GO:0030424]; nuclear body [GO:0016604]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
|
identical protein binding [GO:0042802]
|
PF00041;PF07679;PF13927;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform Short]: Cell membrane; Lipid-anchor, GPI-anchor.
| null | null | null | null | null |
FUNCTION: May play important roles in selective fasciculation and zone-to-zone projection of the primary olfactory axons.
|
Mus musculus (Mouse)
|
O35137
|
ALX4_MOUSE
|
MNAETCVSYCESPAAAMDAYYSPVSQSREGSSPFRGFPGGDKFGTTFLSAGAKGQGFGDAKSRARYGAGQQDLAAPLESSSGARGSFNKFQPQPPTPQPPPAPPAPPAHLYLQRGACKTPPDGSLKLQEGSGGHNAALQVPCYAKESNLGEPELPPDSEPVGMDNSYLSVKETGAKGPQDRASAEIPSPLEKTDSESNKGKKRRNRTTFTSYQLEELEKVFQKTHYPDVYAREQLAMRTDLTEARVQVWFQNRRAKWRKRERFGQMQQVRTHFSTAYELPLLTRAENYAQIQNPSWIGNNGAASPVPACVVPCDPVPACMSPHAHPPGSGASSVSDFLSVSGAGSHVGQTHMGSLFGAAGISPGLNGYEMNGEPDRKTSSIAALRMKAKEHSAAISWAT
| null | null |
anterior/posterior pattern specification [GO:0009952]; digestive tract development [GO:0048565]; embryonic digit morphogenesis [GO:0042733]; embryonic forelimb morphogenesis [GO:0035115]; embryonic hindlimb morphogenesis [GO:0035116]; embryonic skeletal system morphogenesis [GO:0048704]; hair follicle development [GO:0001942]; limb morphogenesis [GO:0035108]; muscle organ development [GO:0007517]; pattern specification process [GO:0007389]; positive regulation of transcription by RNA polymerase II [GO:0045944]; post-embryonic development [GO:0009791]; regulation of apoptotic process [GO:0042981]; regulation of transcription by RNA polymerase II [GO:0006357]; roof of mouth development [GO:0060021]; skeletal system morphogenesis [GO:0048705]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; HMG box domain binding [GO:0071837]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]
|
PF00046;PF03826;
|
1.10.10.60;
|
Paired homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Transcription factor involved in skull and limb development.
|
Mus musculus (Mouse)
|
O35142
|
COPB2_RAT
|
MPLRLDIKRKLTAMSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTPEGHAQNVSCATFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIVKLGREEPAMSMDANGKIIWAKHSEVQQANLKAMGDTEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAHDSSEYAIRESNSVVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWENTELIRRIEIQPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRLNYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAHFLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFSLAQECLHHAQDYGGLLLLATASGNASMVNKLAEGAERDGKNNVAFMSYFLQGKLDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLSKVNQKAAESLADPTEYENLFPGLKEAFVVEEWVKETHADLWPAKQYPLVTPNEERNVMEEAKRFQPSRATAQQEPDGKPASSPVIMASQTTHKEEKSFQELEDDLDTMELEDIDTTDINLDEDILDD
| null | null |
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intra-Golgi vesicle-mediated transport [GO:0006891]; intracellular protein transport [GO:0006886]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]
|
COPI vesicle coat [GO:0030126]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
protein kinase C binding [GO:0005080]; structural molecule activity [GO:0005198]
|
PF04053;PF00400;
|
1.25.40.470;2.130.10.10;
|
WD repeat COPB2 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Golgi apparatus membrane {ECO:0000269|PubMed:17360540}; Peripheral membrane protein {ECO:0000269|PubMed:17360540}; Cytoplasmic side {ECO:0000269|PubMed:17360540}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it (By similarity). Shows only a slight preference for the cis-Golgi apparatus (<55%), compared with the trans-Golgi (>45%). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). {ECO:0000250|UniProtKB:P35606}.; FUNCTION: This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner.
|
Rattus norvegicus (Rat)
|
O35143
|
ATIF1_MOUSE
|
MAGSALAVRARFGVWGMKVLQTRGFVSDSSDSMDTGAGSIREAGGAFGKREKAEEDRYFREKTKEQLAALRKHHEDEIDHHSKEIERLQKQIERHKKKIQQLKNNH
| null | null |
erythrocyte differentiation [GO:0030218]; heme biosynthetic process [GO:0006783]; mitochondrial depolarization [GO:0051882]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of hydrolase activity [GO:0051346]; positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization [GO:1904925]; positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901030]; positive regulation of proteolysis involved in protein catabolic process [GO:1903052]; reactive oxygen species metabolic process [GO:0072593]; regulation of ATP metabolic process [GO:1903578]; regulation of protein targeting to mitochondrion [GO:1903214]
|
cell surface [GO:0009986]; mitochondrion [GO:0005739]; protein-containing complex [GO:0032991]
|
angiostatin binding [GO:0043532]; ATPase binding [GO:0051117]; ATPase inhibitor activity [GO:0042030]; calmodulin binding [GO:0005516]; identical protein binding [GO:0042802]; mitochondrial proton-transporting ATP synthase complex binding [GO:0140260]
|
PF04568;
|
1.20.5.500;
|
ATPase inhibitor family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase (By similarity). Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme (PubMed:23135403). {ECO:0000250|UniProtKB:P01096, ECO:0000269|PubMed:23135403}.
|
Mus musculus (Mouse)
|
O35144
|
TERF2_MOUSE
|
MAAGAGTAGPASGPGVVRDPMASQPRKRPSREGGEGGEGERRSNTMAGGGGSSDSSGRAASRRASRSGGRARRGRHEPGLGGAAERGAGEARLEEAVNRWVLKFYFHEALRAFRSSRYRDFRQIRDIMQALLVRPLGKEHTVSRLLRVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTDSMVESSRKLVKEAAVIICIKNKEFEKASKILKKYMSKDPTTQKLRTDLLNIIREKNLAHPVIQNFSYEVFQQKMLRFLESHLDDTEPYLLTMAKKALKSESAASSTMREEKHPEPVEKPLREPPSRQPQNPPATIGIRTLKAAFKALSTAQDSEAAFAKLDQKDLVLANLASPSSPAHKHKRPRKDEHESAAPAEGEGGSDRQPRNSPMTISRLLLEEDSQSTEPSPGLNSSHKAMSASKPRALNQPHPGEKKPKASKDKWNSPNGLEEKEVWLEEDQLFEVQAPGEDRSSSLTRKQKWTIEESEWVKDGVRKYGEGNWAAISKSYPFVNRTAVMIKDRWRTMKKLGMN
| null | null |
anterograde axonal transport [GO:0008089]; axonal transport of messenger ribonucleoprotein complex [GO:0099088]; cell cycle [GO:0007049]; in utero embryonic development [GO:0001701]; negative regulation of cellular senescence [GO:2000773]; negative regulation of gene expression [GO:0010629]; negative regulation of t-circle formation [GO:1904430]; negative regulation of telomere capping [GO:1904354]; negative regulation of telomere maintenance via recombination [GO:0032208]; negative regulation of telomere maintenance via telomerase [GO:0032211]; negative regulation of telomeric D-loop disassembly [GO:1905839]; positive regulation of gene expression [GO:0010628]; positive regulation of telomere maintenance [GO:0032206]; protection from non-homologous end joining at telomere [GO:0031848]; protein localization to chromosome, telomeric region [GO:0070198]; regulation of telomere maintenance via telomerase [GO:0032210]; telomere capping [GO:0016233]; telomere maintenance [GO:0000723]; telomeric D-loop disassembly [GO:0061820]; telomeric loop formation [GO:0031627]
|
axon cytoplasm [GO:1904115]; chromosome, telomeric region [GO:0000781]; male germ cell nucleus [GO:0001673]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; shelterin complex [GO:0070187]; telomere cap complex [GO:0000782]
|
double-stranded telomeric DNA binding [GO:0003691]; enzyme binding [GO:0019899]; G-rich strand telomeric DNA binding [GO:0098505]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; telomerase activity [GO:0003720]; telomeric DNA binding [GO:0042162]
|
PF00249;PF16772;PF08558;
|
1.10.10.60;1.25.40.210;
| null |
PTM: Phosphorylated upon DNA damage, most probably by ATM. Phosphorylated TERF2 is not bound to telomeric DNA, and rapidly localizes to damage sites (By similarity). {ECO:0000250|UniProtKB:Q15554}.; PTM: Methylated by PRMT1 at multiple arginines within the N-terminal Arg-rich region. Methylation may control association with telomeres (By similarity). {ECO:0000250|UniProtKB:Q15554}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:20339076}. Chromosome, telomere {ECO:0000269|PubMed:20339076}. Note=Colocalizes with telomeric DNA in interphase cells and is located at chromosome ends during metaphase. {ECO:0000269|PubMed:20339076}.
| null | null | null | null | null |
FUNCTION: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes (PubMed:20339076, PubMed:20619712, PubMed:20622870, PubMed:28216226). In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo (By similarity). Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection (By similarity). Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways (By similarity). Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair (By similarity). Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo (PubMed:28216226). Preferentially binds to positive supercoiled DNA (By similarity). Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology (By similarity). Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length (PubMed:20339076, PubMed:20619712, PubMed:20622870). {ECO:0000250|UniProtKB:Q15554, ECO:0000269|PubMed:20339076, ECO:0000269|PubMed:20619712, ECO:0000269|PubMed:20622870, ECO:0000269|PubMed:28216226}.
|
Mus musculus (Mouse)
|
O35147
|
BAD_RAT
|
MGTPKQPSLAPAHALGLRKSDPGIRSLGSDAGGRRWRPAAQSMFQIPEFEPSEQEDASTTDRGLGPSLTEDQPGPYLAPGLLGSIVQQQPGQAANNSHHGGAGTMETRSRHSSYPAGTEEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKGLPRPKSAGTATQMRQSASWTRIIQSWWDRNLGKGGSTPSQ
| null | null |
activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; ADP metabolic process [GO:0046031]; apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; ATP metabolic process [GO:0046034]; cellular response to chromate [GO:0071247]; cellular response to hypoxia [GO:0071456]; cellular response to lipid [GO:0071396]; cellular response to mechanical stimulus [GO:0071260]; cellular response to nicotine [GO:0071316]; cerebral cortex development [GO:0021987]; cytokine-mediated signaling pathway [GO:0019221]; epithelial cell proliferation [GO:0050673]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; glucose catabolic process [GO:0006007]; glucose homeostasis [GO:0042593]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; pore complex assembly [GO:0046931]; positive regulation of apoptotic process [GO:0043065]; positive regulation of B cell differentiation [GO:0045579]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of glucokinase activity [GO:0033133]; positive regulation of granulosa cell apoptotic process [GO:1904710]; positive regulation of insulin secretion [GO:0032024]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of intrinsic apoptotic signaling pathway in response to osmotic stress [GO:1902220]; positive regulation of mitochondrial membrane potential [GO:0010918]; positive regulation of proteolysis [GO:0045862]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; positive regulation of T cell differentiation [GO:0045582]; positive regulation of type B pancreatic cell development [GO:2000078]; regulation of apoptotic process [GO:0042981]; regulation of mitochondrial membrane permeability [GO:0046902]; release of cytochrome c from mitochondria [GO:0001836]; response to amino acid [GO:0043200]; response to benzene [GO:1901423]; response to calcium ion [GO:0051592]; response to estradiol [GO:0032355]; response to ethanol [GO:0045471]; response to glucocorticoid [GO:0051384]; response to glucose [GO:0009749]; response to hormone [GO:0009725]; response to hydrogen peroxide [GO:0042542]; response to hypoxia [GO:0001666]; response to oleic acid [GO:0034201]; response to organic cyclic compound [GO:0014070]; response to organic substance [GO:0010033]; response to progesterone [GO:0032570]; response to testosterone [GO:0033574]; response to xenobiotic stimulus [GO:0009410]; spermatogenesis [GO:0007283]; type B pancreatic cell proliferation [GO:0044342]
|
BAD-BCL-2 complex [GO:0097138]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]
|
14-3-3 protein binding [GO:0071889]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; lipid binding [GO:0008289]; phospholipid binding [GO:0005543]; protein kinase B binding [GO:0043422]; protein kinase binding [GO:0019901]; protein phosphatase 2B binding [GO:0030346]; protein phosphatase binding [GO:0019903]
|
PF10514;
| null |
Bcl-2 family
|
PTM: Phosphorylated at one or more of Ser-113, Ser-137, Ser-156 and Ser-171 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-137 or Ser-113 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-156, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-137 is the major site of AKT/PKB phosphorylation, Ser-156 the major site of protein kinase A (CAPK) phosphorylation.; PTM: Methylation at Arg-132 and Arg-134 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-137. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Mitochondrion outer membrane. Cytoplasm {ECO:0000250|UniProtKB:Q61337}. Note=Colocalizes with HIF3A in the cytoplasm. Upon phosphorylation, locates to the cytoplasm. {ECO:0000250|UniProtKB:Q61337}.
| null | null | null | null | null |
FUNCTION: Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity). Appears to act as a link between growth factor receptor signaling and the apoptotic pathways. {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O35149
|
ZNT4_MOUSE
|
MAGPGAWKRLKSLLRKDDTPLFLNDTSAFDFSDEVSDEGLSRFNKLRVVVADDDSEAPERPVNGAHPALQADDDSLLDQDLPLTNSQLSLKMDPCDNCSKRRELLKQRKVKTRLTIAAVLYLLFMIGELVGGYMANSLAIMTDALHMLTDLSAIILTLLALWLSSKSPTRRFTFGFHRLEVLSAMISVMLVYVLMGFLLYEAVQRTIHMNYEINGDVMLITAAVGVAVNVIMGFLLNQSGHHHSHAHSHSLPSNSPSMVSSGHNHGQDSLAVRAAFVHALGDLVQSVGVLIAAYIIRFKPEYKIADPICTYIFSLLVAFTTFRIIWDTVVIILEGVPSHLNVDYIKESLMKIEDVYSVEDLNIWSLTSGKSTAIVHMQLIPGSSSKWEEVQSKAKHLLLNTFGMYKCTIQLQSYRQEVIRTCANCHSSST
| null | null |
response to toxic substance [GO:0009636]; response to zinc ion [GO:0010043]; zinc export across plasma membrane [GO:0140882]; zinc ion import into lysosome [GO:0140916]; zinc ion transmembrane transport [GO:0071577]
|
endosome membrane [GO:0010008]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]
|
antiporter activity [GO:0015297]; metal ion binding [GO:0046872]; zinc ion transmembrane transporter activity [GO:0005385]
|
PF01545;
|
1.20.1510.10;
|
Cation diffusion facilitator (CDF) transporter (TC 2.A.4) family, SLC30A subfamily
| null |
SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:O55174}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:O14863}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:O14863}; Multi-pass membrane protein {ECO:0000255}. Note=Enriched in vesicles within the basal region of epithelial cells. {ECO:0000250|UniProtKB:O55174}.
|
CATALYTIC ACTIVITY: Reaction=2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out); Xref=Rhea:RHEA:72627, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:9354792};
| null | null | null | null |
FUNCTION: Probable proton-coupled zinc ion antiporter mediating zinc import from cytoplasm potentially into the endocytic compartment (PubMed:9354792). Controls zinc deposition in milk (PubMed:9354792). {ECO:0000269|PubMed:9354792}.
|
Mus musculus (Mouse)
|
O35152
|
BET1L_RAT
|
MADWTRAQSSGAVEEIVDRENKRMADSLASKVTRLKSLALDIDRDTEDQNRYLDGMDSDFTSVTGLLTGSVKRFSTVARSGRDTRKLLCGMAVVLIVAFFILSYLFSRTRT
| null | null |
protein transport [GO:0015031]; regulation of retrograde vesicle-mediated transport, Golgi to ER [GO:2000156]; retrograde transport, endosome to Golgi [GO:0042147]
|
cytosol [GO:0005829]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; Golgi-associated vesicle [GO:0005798]; SNARE complex [GO:0031201]; trans-Golgi network [GO:0005802]
|
SNAP receptor activity [GO:0005484]
| null |
1.20.5.110;
| null | null |
SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type IV membrane protein. Golgi apparatus, trans-Golgi network membrane. Note=Present throughout the Golgi apparatus, with strongly increasing concentration from cis-Golgi to the trans-Golgi face of the stacks.
| null | null | null | null | null |
FUNCTION: Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex. {ECO:0000269|PubMed:12388752, ECO:0000269|PubMed:14742712}.
|
Rattus norvegicus (Rat)
|
O35158
|
CDON_RAT
|
MHPDLGPLWKLLYVLVILCSSVSSDLATYFISEPLSAVQKLGRPVVLHCSAKPVTARISWLHNGKRLDRNTEQIKIHRGTLTILSLNPSLSGCYQCVANNSVGAVVSGPATVSADALADFDSSTMHVITAEKKNTGFIGCRVPESNPKAEVRYKIRGKWLMYSTGNYIILPSGNLQILNVSSKDKGSYKCAAYNPVTSELKVEPAGRKLLVSRPSSDGFHILHPALSQALAVLPHSPVTLECVVSGVPASQVYWLKDGQDCLSGSNWRRLYSHLATASIDPADSGNYSCVVGNNSSGDVKHVTYTVNVLEHASISKGLHDQKVSLGATVRFTCEVHGNPAPNRTWFHNAQPIRPSSRHLTEGSVLKITGVIMEDSGLYQCMADNGIGFMQSTGRLQIEQDSGQRPVIVTAPANVEVTDGDFVTLSCNATGEPVPVIHWYGRHGLITSHPSQVLRSKSRKSHLFRPGDLDPEPVYLIMSQAGSSSLSIQAVTREHAGKYTCEAVNKHGSTQSEAFLTVVPFETNTKAEPVTPSEASQNDERDPRDGSESGLLNLFPVKVHSGGVELPAEKNASVPDAPNILSPPQTHMPDTYTLVWRTGRDGGMPINAYFVKYRKLDDGSGAVGSWHTVRVPGSESELHLTELEPSSLYEVLMVARSAVGEGQPAMLTFRTSKEKMASSKNTQASFPPVGIPKRPVTSEASNSNFGVVLTDSSRHSGVPEAPDRPTISMASETSVYVTWIPRANGGSPITAFKVEYKRMKSSDWLVAAEDIPPSKLSVEVRSLEPGSIYKFRVIVINHYGESFRSSASRPYQVAGFPNRFSNRPITGPHIAYTEAVSDTQIMLKWTYIPSSNNNTPIQGFYIYYRPTDSDNDSDYKRDVVEGSKQWHTIGHLQPETSYDIKMQCFNEGGESEFSNVMICETKVKRVPGASEYPMKELSTPPSSSGNGGNVGPATSPARSSDMLYLIVGCVLGVMVLILLVFIALCLWKSRQQSAIQKYDPPGYLYQGSEINGQMVEYTTLSGTARINGSVHGGFLSKGSLSNGCSHLHHKGPNGVNGILNGTINGGLYSAHTSSLTRTCVEFEHPHHLVNGGAVYTAVPQMDPLECINCRNCRNNNRCFTKTNSPLPVVPVVASYPQDGLEMKPLGVMKFPVCPVSTVPDGGQIPEECLKDSVAPAPTQRTCRQDNTSDINSDSTEDTAEFNRGDSSGHSEAEDKVFSWSPLILSPVLEDCSEKTAWSPPGPPLDGLSVVLQQAQET
| null | null |
anterior/posterior pattern specification [GO:0009952]; axon guidance [GO:0007411]; cell adhesion [GO:0007155]; cell fate specification [GO:0001708]; cell-cell adhesion [GO:0098609]; cerebral cortex development [GO:0021987]; embryonic body morphogenesis [GO:0010172]; embryonic morphogenesis [GO:0048598]; embryonic retina morphogenesis in camera-type eye [GO:0060059]; lens development in camera-type eye [GO:0002088]; myoblast fusion [GO:0007520]; nervous system development [GO:0007399]; neural precursor cell proliferation [GO:0061351]; neuroblast proliferation [GO:0007405]; neuron differentiation [GO:0030182]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of skeletal muscle tissue development [GO:0048643]; positive regulation of small GTPase mediated signal transduction [GO:0051057]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of neuron differentiation [GO:0045664]; skeletal muscle satellite cell differentiation [GO:0014816]; skeletal muscle tissue development [GO:0007519]; smoothened signaling pathway [GO:0007224]; striated muscle cell differentiation [GO:0051146]
|
axon [GO:0030424]; cell surface [GO:0009986]; plasma membrane [GO:0005886]
|
cell-cell adhesion mediator activity [GO:0098632]
|
PF00041;PF07679;PF13927;
|
2.60.40.10;
| null |
PTM: N-glycosylated. {ECO:0000269|PubMed:9214393}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21802063, ECO:0000269|PubMed:9214393}; Single-pass membrane protein {ECO:0000269|PubMed:21802063, ECO:0000269|PubMed:9214393}.
| null | null | null | null | null |
FUNCTION: Component of a cell-surface receptor complex that mediates cell-cell interactions between muscle precursor cells. Promotes differentiation of myogenic cells (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O35160
|
PITX3_MOUSE
|
MEFGLLGEAEARSPALSLSDAGTPHPPLPEHGCKGQEHSDSEKASASLPGGSPEDGSLKKKQRRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRKRERSQQAELCKGGFAAPLGGLVPPYEEVYPGYSYGNWPPKALAPPLAAKTFPFAFNSVNVGPLASQPVFSPPSSIAASMVPSAAAAPGTVPGPGALQGLGGAPPGLAPAAVSSGAVSCPYASAAAAAAAAASSPYVYRDPCNSSLASLRLKAKQHASFSYPAVPGPPPAANLSPCQYAVERPV
| null | null |
anatomical structure morphogenesis [GO:0009653]; cellular response to glial cell derived neurotrophic factor [GO:1990792]; dopaminergic neuron differentiation [GO:0071542]; lens development in camera-type eye [GO:0002088]; lens fiber cell differentiation [GO:0070306]; lens morphogenesis in camera-type eye [GO:0002089]; locomotory behavior [GO:0007626]; midbrain development [GO:0030901]; negative regulation of gliogenesis [GO:0014014]; negative regulation of neurogenesis [GO:0050768]; neuron development [GO:0048666]; positive regulation of cell proliferation in midbrain [GO:1904935]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]; response to cocaine [GO:0042220]; response to immobilization stress [GO:0035902]; response to methamphetamine hydrochloride [GO:1904313]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00046;PF03826;
|
1.10.10.60;
|
Paired homeobox family, Bicoid subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138, ECO:0000269|PubMed:17184956}.
| null | null | null | null | null |
FUNCTION: Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. In addition to its importance during development, it also has roles in the long-term survival and maintenance of the mdDA neurons. Activates NR4A2/NURR1-mediated transcription of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons. Acts by decreasing the interaction of NR4A2/NURR1 with the corepressor NCOR2/SMRT which acts through histone deacetylases (HDACs) to keep promoters of NR4A2/NURR1 target genes in a repressed deacetylated state. Essential for the normal lens development and differentiation. Plays a critical role in the maintenance of mitotic activity of lens epithelial cells, fiber cell differentiation and in the control of the temporal and spatial activation of fiber cell-specific crystallins. Positively regulates FOXE3 expression and negatively regulates PROX1 in the anterior lens epithelium, preventing activation of CDKN1B/P27Kip1 and CDKN1C/P57Kip2 and thus maintains lens epithelial cells in cell cycle. {ECO:0000269|PubMed:15950611, ECO:0000269|PubMed:17184956, ECO:0000269|PubMed:19007884, ECO:0000269|PubMed:19144721, ECO:0000269|PubMed:19334279}.
|
Mus musculus (Mouse)
|
O35161
|
CELR1_MOUSE
|
MAPSSPRVLPALVLLAAAALPALELGAAAWELRVPGGARAFALGPGWSYRLDTTRTPRELLDVSREGPAAGRRLGLGAGTLGCARLAGRLLPLQVRLVARGAPTAPSLVLRARAYGARCGVRLLRRSARGAELRSPAVRSVPGLGDALCFPAAGGGAASLTSVLEAITNFPACSCPPVAGTGCRRGPICLRPGGSAELRLVCALGRAAGAVWVELVIEATSGTPSESPSVSPSLLNLSQPRAGVVRRSRRGTGSSTSPQFPLPSYQVSVPENEPAGTAVIELRAHDPDEGDAGRLSYQMEALFDERSNGYFLIDAATGAVTTARSLDRETKDTHVLKVSAVDHGSPRRSAATYLTVTVSDTNDHSPVFEQSEYRERIRENLEVGYEVLTIRATDGDAPSNANMRYRLLEGAGGVFEIDARSGVVRTRAVVDREEAAEYQLLVEANDQGRNPGPLSASATVHIVVEDENDNYPQFSEKRYVVQVPEDVAVNTAVLRVQATDRDQGQNAAIHYSIVSGNLKGQFYLHSLSGSLDVINPLDFEAIREYTLRIKAQDGGRPPLINSSGLVSVQVLDVNDNAPIFVSSPFQAAVLENVPLGHSVLHIQAVDADAGENARLQYRLVDTASTIVGGSSVDSENPASAPDFPFQIHNSSGWITVCAELDREEVEHYSFGVEAVDHGSPAMSSSASVSITVLDVNDNDPMFTQPVYELRLNEDAAVGSSVLTLRARDRDANSVITYQLTGGNTRNRFALSSQSGGGLITLALPLDYKQERQYVLAVTASDGTRSHTAQVFINVTDANTHRPVFQSSHYTVSVSEDRPVGTSIATISATDEDTGENARITYVLEDPVPQFRIDPDTGTIYTMTELDYEDQAAYTLAITAQDNGIPQKSDTTSLEILILDANDNAPRFLRDFYQGSVFEDAPPSTSVLQVSATDRDSGPNGRLLYTFQGGDDGDGDFYIEPTSGVIRTQRRLDRENVAVYNLWALAVDRGSPNPLSASVGIQVSVLDINDNPPVFEKDELELFVEENSPVGSVVARIRANDPDEGPNAQIMYQIVEGNVPEVFQLDLLSGDLRALVELDFEVRRDYMLVVQATSAPLVSRATVHIRLLDQNDNPPELPDFQILFNNYVTNKSNSFPSGVIGRIPAHDPDLSDSLNYTFLQGNELSLLLLDPATGELQLSRDLDNNRPLEALMEVSVSDGIHSVTALCTLRVTIITDDMLTNSITVRLENMSQEKFLSPLLSLFVEGVATVLSTTKDDIFVFNIQNDTDVSSNILNVTFSALLPGGTRGRFFPSEDLQEQIYLNRTLLTTISAQRVLPFDDNICLREPCENYMKCVSVLRFDSSAPFISSTTVLFRPIHPITGLRCRCPPGFTGDYCETEIDLCYSNPCGANGRCRSREGGYTCECFEDFTGEHCQVNVRSGRCASGVCKNGGTCVNLLIGGFHCVCPPGEYEHPYCEVSTRSFPPQSFVTFRGLRQRFHFTVSLAFATQDRNALLLYNGRFNEKHDFIALEIVEEQLQLTFSAGETTTTVTPQVPGGVSDGRWHSVLVQYYNKPNIGHLGLPHGPSGEKVAVVTVDDCDAAVAVHFGSYVGNYSCAAQGTQSGSKKSLDLTGPLLLGGVPNLPEDFPVHSRQFVGCMRNLSIDGRIVDMAAFIANNGTRAGCASQRNFCDGTSCQNGGTCVNRWNTYLCECPLRFGGKNCEQAMPHPQRFTGESVVLWSDLDITISVPWYLGLMFRTRKEDGVLMEATAGTSSRLHLQILNSYIRFEVSYGPSDVASMQLSKSRITDGGWHHLLIELRSAKEGKDIKYLAVMTLDYGMDQSTVQIGNQLPGLKMRTIVIGGVTEDKVSVRHGFRGCMQGVRMGETSTNIATLNMNDALKVRVKDGCDVEDPCASSPCPPHSHCRDTWDSYSCICDRGYFGKKCVDACLLNPCKHVAACVRSPNTPRGYSCECGPGHYGQYCENKVDLPCPKGWWGNPVCGPCHCAVSQGFDPDCNKTNGQCQCKENYYKPPAQDACLPCDCFPHGSHSRACDMDTGQCACKPGVIGRQCNRCDNPFAEVTSLGCEVIYNGCPRAFEAGIWWPQTKFGQPAAVPCPKGSVGNAVRHCSGEKGWLPPELFNCTSGSFVDLKALNEKLNRNETRMDGNRSLRLAKALRNATQGNSTLFGNDVRTAYQLLARILQHESRQQGFDLAATREANFHEDVVHTGSALLAPATEASWEQIQRSEAGAAQLLRHFEAYFSNVARNVKRTYLRPFVIVTANMILAVDIFDKLNFTGAQVPRFEDIQEELPRELESSVSFPADTFKPPEKKEGPVVRLTNRRTTPLTAQPEPRAERETSSSRRRRHPDEPGQFAVALVVIYRTLGQLLPEHYDPDHRSLRLPNRPVINTPVVSAMVYSEGTPLPSSLQRPILVEFSLLETEERSKPVCVFWNHSLDTGGTGGWSAKGCELLSRNRTHVTCQCSHSASCAVLMDISRREHGEVLPLKIITYAALSLSLVALLVAFVLLSLVRTLRSNLHSIHKNLITALFFSQLIFMVGINQTENPFLCTVVAILLHYVSMGTFAWTLVENLHVYRMLTEVRNIDTGPMRFYHVVGWGIPAIVTGLAVGLDPQGYGNPDFCWLSLQDTLIWSFAGPVGTVIIINTVIFVLSAKVSCQRKHHYYERKGVVSMLRTAFLLLLLVTATWLLGLLAVNSDTLSFHYLFAAFSCLQGIFVLLFHCVAHREVRKHLRAVLAGKKLQLDDSATTRATLLTRSLNCNNTYSEGPDMLRTALGESTASLDSTTRDEGVQKLSVSSGPARGNHGEPDASFIPRNSKKAHGPDSDSDSELSLDEHSSSYASSHTSDSEDDGGEAEDKWNPAGGPAHSTPKADALANHVPAGWPDESLAGSDSEELDTEPHLKVETKVSVELHRQAQGNHCGDRPSDPESGVLAKPVAVLSSQPQEQRKGILKNKVTYPPPLPEQPLKSRLREKLADCEQSPTSSRTSSLGSGDGVHATDCVITIKTPRREPGREHLNGVAMNVRTGSAQANGSDSEKP
| null | null |
anterior/posterior pattern specification [GO:0009952]; apical protein localization [GO:0045176]; cell-cell adhesion [GO:0098609]; establishment of body hair planar orientation [GO:0048105]; establishment of planar polarity [GO:0001736]; establishment of planar polarity of embryonic epithelium [GO:0042249]; hair follicle development [GO:0001942]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; inner ear morphogenesis [GO:0042472]; lateral sprouting involved in lung morphogenesis [GO:0060490]; locomotory behavior [GO:0007626]; motor neuron migration [GO:0097475]; neural tube closure [GO:0001843]; orthogonal dichotomous subdivision of terminal units involved in lung branching morphogenesis [GO:0060488]; planar cell polarity pathway involved in neural tube closure [GO:0090179]; planar dichotomous subdivision of terminal units involved in lung branching morphogenesis [GO:0060489]; protein localization involved in establishment of planar polarity [GO:0090251]; regulation of actin cytoskeleton organization [GO:0032956]; Rho protein signal transduction [GO:0007266]; wound healing [GO:0042060]
|
membrane [GO:0016020]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; G protein-coupled receptor activity [GO:0004930]
|
PF00002;PF00028;PF00008;PF16489;PF01825;PF02793;PF00053;PF02210;
|
2.60.120.200;2.60.220.50;2.60.40.60;4.10.1240.10;2.10.25.10;1.20.1070.10;2.170.300.10;
|
G-protein coupled receptor 2 family, LN-TM7 subfamily
|
PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor that may have an important role in cell/cell signaling during nervous system formation.
|
Mus musculus (Mouse)
|
O35165
|
GOSR2_RAT
|
MEPLYQQTHKQVHEIQSHMGRLETADKQSVHLVENEIQASIDQIFSHLERLEILSSKEPPNRRQNAKLRVDQLKYDVQHLQTALRNFQHRRQAKEQQERQRDELLSRTFTTNDSDTTIPMDESLQFNSSLQNIHHGMDDLIGGGHSILEGLRAQRLTLKGTQKKILDIANMLGLSNTVMRLIEKRAFQDKYFMIGGMLLTCAVMFLVVQYLT
| null | null |
intra-Golgi vesicle-mediated transport [GO:0006891]; protein transport [GO:0015031]; vesicle fusion [GO:0006906]; vesicle-mediated transport [GO:0016192]
|
cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; nucleoplasm [GO:0005654]; SNARE complex [GO:0031201]
|
SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]
|
PF12352;
|
1.20.58.400;
|
GOSR2 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:14742712}; Single-pass type IV membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:14742712}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:9094723}. Note=Concentrated most in the intermediate compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2. Greatly reduced in concentration at the trans end of the Golgi apparatus. {ECO:0000269|PubMed:14742712}.
| null | null | null | null | null |
FUNCTION: Involved in transport of proteins from the cis/medial-Golgi to the trans-Golgi network. {ECO:0000269|PubMed:9094723}.
|
Rattus norvegicus (Rat)
|
O35166
|
GOSR2_MOUSE
|
MEPLYQQTNKQVQEIQSHMGRLERADKQSVHLVENEIQASIEQIFSHLERLEILSSKEPLNRRQNAKLRVDQLKYDVQHLQTALRNFQHRRQVREQQERQRDELLSRTFTTNDSDTTIPMDESLQFNSSLHNIHHGMDDLIGGGHSILEGLRAQRLTLKGTQKKILDIANMLGLSNTVMRLIEKRAFQDKYFMIGGMLLTCAVMFLVVQYLT
| null | null |
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intra-Golgi vesicle-mediated transport [GO:0006891]; protein transport [GO:0015031]; vesicle fusion [GO:0006906]; vesicle-mediated transport [GO:0016192]
|
cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; nucleoplasm [GO:0005654]; SNARE complex [GO:0031201]
|
SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]
|
PF12352;
| null |
GOSR2 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:O35165}; Single-pass type IV membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O35165}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O35165}. Note=Concentrated most in the intermediate compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2. Greatly reduced in concentration at the trans end of the Golgi apparatus. {ECO:0000250|UniProtKB:O35165}.
| null | null | null | null | null |
FUNCTION: Involved in transport of proteins from the cis/medial-Golgi to the trans-Golgi network. {ECO:0000250|UniProtKB:O35165}.
|
Mus musculus (Mouse)
|
O35167
|
COLQ_RAT
|
MAVLNPMTLGIYLQLFFCSIVSQPTFINSVLPISAALPGLDQKKRGNHKACCLLMPPPPPLFPPPFFRGSRSPLLSPDMKNLLELEASPSPCMQGSLGSPGPPGPQGPPGLPGKAGPKGEKGDLGRPGRKGRPGPPGVPGEPGPVGWPGPEGPRGEKGDVGMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPGMLGQKGEMGPKGESGIAGHRGPTGRPGKRGKQGQKGDSGIMGPPGKPGPSGQPGRQGPPGPPGPPSAGQLVMGLKGERGFPGPPGRCLCGPPANVNNPSYGDPMYGRGSPRVPAIFVVNNQEELEKLNTQNAIAFRRDQRSLYFKDSLGWLPIQLTPFYPVGLHHKAAWHLCGDGVLQPGEECDDGNPDVSDGCIDCHRAYCGDGYRHRGVEDCDGSDFGYLKCETYLPGSYGELRCTQYCSIDSTPCRYFT
| null | null |
establishment of protein localization to membrane [GO:0090150]; extracellular matrix organization [GO:0030198]; regulation of synaptic assembly at neuromuscular junction [GO:0008582]; skeletal muscle acetylcholine-gated channel clustering [GO:0071340]
|
basement membrane [GO:0005604]; collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]
|
extracellular matrix structural constituent conferring tensile strength [GO:0030020]; heparin binding [GO:0008201]; structural molecule activity [GO:0005198]
|
PF01391;
| null |
COLQ family
|
PTM: The triple-helical tail is stabilized by disulfide bonds at each end.
|
SUBCELLULAR LOCATION: Synapse {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina. {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O35173
|
KCNS1_MOUSE
|
MVSEFPGPGSRVPWRPRDEALRVNVGGVRRLLSARALARFPGTRLGRLQAAASEEQARRLCDDYDAAAHEFYFDRHPGFFLGLLHFYRTGHLHVLDELCVFAFGQEADYWGLGENALATCCRARYLERRVARPRAWDEDSDAPSSVDPCPDEISDVQRELARYGAARCGRLRRRLWLTMENPGYSLPSKLFSCVSIGVVLASIAAMCIHSLPEYQAREAAAAVAAVAAGRSAEEVRDDPVLRRLEYFCIAWFSFEVSSRLLLAPSTRNFFCHPLNLIDIVSVLPFYLTLLAGAALGDQRGASGEELGDLGKVVQVFRLMRIFRVLKLARHSTGLRSLGATLKHSYREVGILLLYLAVGVSVFSGVAYTAEEENEGFHTIPACWWWGTVSMTTVGYGDVVPETVGGKLAASGCILGGILVVALPITIIFNKFSHFYRRQKALEAAVRSSGQREFEDLLSSVDGVSDVSLETSRDTSQEGRSTDLETQAPREPAKSHSY
| null | null |
potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; protein homooligomerization [GO:0051260]; regulation of delayed rectifier potassium channel activity [GO:1902259]
|
perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076]
|
delayed rectifier potassium channel activity [GO:0005251]; potassium channel regulator activity [GO:0015459]
|
PF02214;PF00520;
|
1.10.287.70;1.20.120.350;
|
Potassium channel family, S (TC 1.A.1.2) subfamily, Kv9.1/KCNS1 sub-subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9305895}; Multi-pass membrane protein {ECO:0000305}. Note=May not reach the plasma membrane but remain in an intracellular compartment in the absence of KCNB1 or KCNB2 (PubMed:9305895). {ECO:0000269|PubMed:9305895}.
| null | null | null | null | null |
FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2 (PubMed:9305895). {ECO:0000269|PubMed:9305895}.
|
Mus musculus (Mouse)
|
O35174
|
KCNS2_MOUSE
|
MTRQSLWDVSDTDVEDGEIRINVGGFKRRLRSHTLLRFPETRLGRLLLCHSREAILELCDDYDDVQREFYFDRNPELFPYVLHFYHTGKLHVMAELCVFSFSQEIEYWGINEFFIDSCCSYSYHGRKVEPEQEKWDEQSDQESTTSSFDEILAFYNDASKFDGQPLGNFRRQLWLALDNPGYSVLSRVFSVLSILVVLGSIITMCLNSLPDFQIPDSQGNPGEDPRFEIVEHFGIAWFTFELVARFAVAPDFLKFFKNALNLIDLMSIVPFYITLVVNLVVESSPTLANLGRVAQVLRLMRIFRILKLARHSTGLRSLGATLKYSYKEVGLLLLYLSVGISIFSVVAYTIEKEENEGLATIPACWWWATVSMTTVGYGDVVPGTTAGKLTASACILAGILVVVLPITLIFNKFSHFYRRQKQLESAMRSCDFGDGMKEVPSVNLRDYYAHKVKSLMASLTNMSRSSPSELSLDDSLH
| null | null |
potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; protein homooligomerization [GO:0051260]; regulation of delayed rectifier potassium channel activity [GO:1902259]
|
perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076]
|
voltage-gated potassium channel activity [GO:0005249]
|
PF02214;PF00520;
|
1.10.287.70;1.20.120.350;
|
Potassium channel family, S (TC 1.A.1.2) subfamily, Kv9.2/KCNS2 sub-subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9305895}; Multi-pass membrane protein {ECO:0000305}. Note=May not reach the plasma membrane but remain in an intracellular compartment in the absence of KCNB1 or KCNB2 (PubMed:9305895). {ECO:0000269|PubMed:9305895}.
| null | null | null | null | null |
FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2 (PubMed:9305895). {ECO:0000269|PubMed:9305895}.
|
Mus musculus (Mouse)
|
O35177
|
CASL_MOUSE
|
MWARNLMARALYDNVPECAEELAFRKGDILTVIEQNTGGLEGWWLCSLHGRQGIVPGNRVKLLIGPVQETPGHEQPTPGPMHQTFGQQKLYQVPNSQAASRDTIYQVPPSYQNQGIYQVPTGHGTPEQDVYQVPPSVQRNIGGTNGPLLSKKVITPVRTGHGYVYEYPSRYQKDVYDVPPSHSTQGVYDIPPSSVKGPVFSVPVGEIKPQGVYDIPPTQGVYAIPPSACRDEAGLREKEYDFPPPMKQDGKPDTRPEGVYDIPPTSTKTAGKDLHIKFPCDAPGGVEPMARRHQSFSLHHAPSQLGQSGDTQSDAYDVPRGVQFLEVPTETSEKANPEERDGVYDVPLHNPADAKGSRDVVDGINRLSFSSTGSTRSNMSTSSTSSKESSLSASPSQDKRLRLDPDTAIEKLYRLQQTLEMGVCSLMSLVTTDWRCYGYMERHINEIRTAVDKVELFLREYLHFAKGALANASCLPELVLHNKMKRELQRVEDSHQILSQTSHDLNECSWSLNILAINKPQNKCDDLDRFVMVAKTVPDDAKQLTTTISTYAETLFRADPANSHLKNGPNSIMNSSEYTHPGSQMQPLHPGDYKAQVHSKPLPPSLSKDQPPDCGSSDGSERSWMDDYDYVHLQGKEEFERQQKELLEKENIMKQSKAQLEHHQLSQFQLLEQEITKPVENDISKWKPSQSLPTTNNSVGAQDRQLLCFYYDQCETHFISLLNAIDALFSCVSSAQPPRIFVAHSKFVILSAHKLVFIGDTLTRQVAAQDIRNKVRNSSNQLCEQLKTIVMATKMAALHYPSTTALQEMVHQVTDLSRNAQLFKRSLLEMATF
| null | null |
cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell division [GO:0051301]; cell migration [GO:0016477]; cilium disassembly [GO:0061523]; learning or memory [GO:0007611]; lymphocyte migration into lymphoid organs [GO:0097021]; negative regulation of cell migration [GO:0030336]; positive regulation of cell migration [GO:0030335]; positive regulation of dendritic spine maintenance [GO:1902952]; positive regulation of immunological synapse formation [GO:2000522]; positive regulation of lymphocyte chemotaxis [GO:0140131]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of protein localization [GO:1903829]; positive regulation of protein tyrosine kinase activity [GO:0061098]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; regulation of actin cytoskeleton organization [GO:0032956]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
basolateral plasma membrane [GO:0016323]; cell cortex [GO:0005938]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; immunological synapse [GO:0001772]; lamellipodium [GO:0030027]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle pole [GO:0000922]
|
protein tyrosine kinase binding [GO:1990782]
|
PF12026;PF08824;PF14604;
|
1.20.120.230;1.20.120.830;2.30.30.40;
|
CAS family
|
PTM: Polyubiquitinated by ITCH/AIP4, leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q14511}.; PTM: PTK2/FAK1 phosphorylates the protein at the YDYVHL motif (conserved among all cas proteins) following integrin stimulation (By similarity). The SRC family kinases (FYN, SRC, LCK and CRK) are recruited to the phosphorylated sites and can phosphorylate other tyrosine residues (By similarity). Ligation of either integrin beta-1 or B-cell antigen receptor on tonsillar B-cells and B-cell lines promotes tyrosine phosphorylation and both integrin and BCR-mediated tyrosine phosphorylation requires an intact actin network (By similarity). Phosphorylation is required to recruit NEDD9 to T-cell receptor microclusters at the periphery of newly formed immunological synapses (PubMed:27359298). In fibroblasts transformation with oncogene v-ABL results in an increase in tyrosine phosphorylation. Transiently phosphorylated following CD3 cross-linking and this phosphorylated form binds to CRKL and C3G (By similarity). A mutant lacking the SH3 domain is phosphorylated upon CD3 cross-linking but not upon integrin beta-1 cross-linking. Tyrosine phosphorylation occurs upon stimulation of the G-protein coupled C1a calcitonin receptor. Calcitonin-stimulated tyrosine phosphorylation is mediated by calcium- and protein kinase C-dependent mechanisms and requires the integrity of the actin cytoskeleton. Phosphorylation at Ser-368 induces proteasomal degradation (By similarity). Phosphorylated by LYN (By similarity). Phosphorylation at Ser-779 by CSNK1D or CSNK1E, or phosphorylation of Thr-803 by CSNK1E enhances the interaction of NEDD9 with PLK1 (By similarity). {ECO:0000250|UniProtKB:Q14511, ECO:0000269|PubMed:27359298}.
|
SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q14511}. Nucleus {ECO:0000250|UniProtKB:Q14511}. Golgi apparatus {ECO:0000250|UniProtKB:Q14511}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q14511}. Cytoplasm {ECO:0000250|UniProtKB:Q14511}. Cell junction, focal adhesion {ECO:0000269|PubMed:25059660}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14511}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:A0A8I3PDQ1}. Cell projection, cilium {ECO:0000250|UniProtKB:Q14511}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q14511}. Basolateral cell membrane {ECO:0000250|UniProtKB:A0A8I3PDQ1}.
| null | null | null | null | null |
FUNCTION: Scaffolding protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion (By similarity). As a focal adhesion protein, plays a role in embryonic fibroblast migration (PubMed:25059660). May play an important role in integrin beta-1 or B cell antigen receptor (BCR) mediated signaling in B- and T-cells. Integrin beta-1 stimulation leads to recruitment of various proteins including CRKl and SHPTP2 to the tyrosine phosphorylated form (By similarity). Promotes adhesion and migration of lymphocytes; as a result required for the correct migration of lymphocytes to the spleen and other secondary lymphoid organs (PubMed:16148091, PubMed:17174122). Plays a role in the organization of T-cell F-actin cortical cytoskeleton and the centralization of T-cell receptor microclusters at the immunological synapse (PubMed:27359298). Negatively regulates cilia outgrowth in polarized cysts (By similarity). Modulates cilia disassembly via activation of AURKA-mediated phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin (By similarity). Positively regulates RANKL-induced osteoclastogenesis (PubMed:27336669). Required for the maintenance of hippocampal dendritic spines in the dentate gyrus and CA1 regions, thereby involved in spatial learning and memory (PubMed:26683084). {ECO:0000250|UniProtKB:A0A8I3PDQ1, ECO:0000250|UniProtKB:Q14511, ECO:0000269|PubMed:16148091, ECO:0000269|PubMed:17174122, ECO:0000269|PubMed:25059660, ECO:0000269|PubMed:26683084, ECO:0000269|PubMed:27336669, ECO:0000269|PubMed:27359298}.
|
Mus musculus (Mouse)
|
O35179
|
SH3G2_RAT
|
MSVAGLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQASSQPRREYQPKPRMSLEFATGDGTQPNGGLSHTGTPKPAGVQMDQPCCRALYDFEPENEGELGFKEGDIITLTNQIDENWYEGMLHGQSGFFPINYVEILVALPH
| null | null |
cellular response to brain-derived neurotrophic factor stimulus [GO:1990416]; dendrite extension [GO:0097484]; lipid tube assembly [GO:0060988]; membrane bending [GO:0097753]; membrane tubulation [GO:0097749]; negative regulation of blood-brain barrier permeability [GO:1905604]; negative regulation of gene expression [GO:0010629]; negative regulation of protein phosphorylation [GO:0001933]; neuron projection development [GO:0031175]; positive regulation of membrane tubulation [GO:1903527]; postsynaptic actin cytoskeleton organization [GO:0098974]; regulation of clathrin-dependent endocytosis [GO:2000369]; regulation of receptor internalization [GO:0002090]; synaptic vesicle endocytosis [GO:0048488]; synaptic vesicle uncoating [GO:0016191]; vesicle scission [GO:0099050]
|
basal dendrite [GO:0097441]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; photoreceptor ribbon synapse [GO:0098684]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; presynapse [GO:0098793]; presynaptic cytosol [GO:0099523]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202]; synaptic vesicle membrane [GO:0030672]
|
identical protein binding [GO:0042802]; lipid binding [GO:0008289]; protein kinase binding [GO:0019901]; transmembrane transporter binding [GO:0044325]
|
PF03114;PF00018;
|
1.20.1270.60;2.30.30.40;
|
Endophilin family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9238017, ECO:0000269|PubMed:9341169}. Membrane {ECO:0000269|PubMed:9238017}; Peripheral membrane protein {ECO:0000269|PubMed:9238017}. Early endosome {ECO:0000250|UniProtKB:Q62420}. Presynapse {ECO:0000269|PubMed:9341169}.
| null | null | null | null | null |
FUNCTION: Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature. Required for BDNF-dependent dendrite outgrowth. Cooperates with SH3GL2 to mediate BDNF-NTRK2 early endocytic trafficking and signaling from early endosomes (By similarity). {ECO:0000250|UniProtKB:Q62420, ECO:0000269|PubMed:11604418, ECO:0000269|PubMed:16763559}.
|
Rattus norvegicus (Rat)
|
O35180
|
SH3G3_RAT
|
MSVAGLKKQFHKASQLFSEKISGAEGTKLDEEFLDMEKKIDITSKAVAEILSKATEYLQPNPAYRAKLGMLNTMSKLRGQVKATGYPQTEGLLGDCMLKYGRELGEDSAFGNSLVEVGEALKLMAEVKDSLDINVKQTFIDPLQLLQDKDLKEIGHHLRKLEGRRLDYDYKKKRVGKIPEEEIRQAVEKFEESKELAERSMFNFLENDVEQVSQLAVFVEAALDYHRQSTEILQELQNKLELRIALASQVPRRDYMPKPVNTSSTNANGVEPSSSSKLTGTDIPSDQPCCRGLYDFEPENEGELGFKEGDIITLTNQIDENWYEGMLRGESGFFPINYVEVIVPLPR
| null | null |
negative regulation of clathrin-dependent endocytosis [GO:1900186]; positive regulation of neuron differentiation [GO:0045666]; regulation of clathrin-dependent endocytosis [GO:2000369]; synaptic vesicle uncoating [GO:0016191]
|
acrosomal vesicle [GO:0001669]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; glutamatergic synapse [GO:0098978]; postsynaptic density, intracellular component [GO:0099092]; postsynaptic endosome [GO:0098845]; presynapse [GO:0098793]
|
identical protein binding [GO:0042802]; lipid binding [GO:0008289]
|
PF03114;PF00018;
|
1.20.1270.60;2.30.30.40;
|
Endophilin family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17088211, ECO:0000269|PubMed:9238017}. Early endosome membrane {ECO:0000269|PubMed:17088211}; Peripheral membrane protein {ECO:0000305|PubMed:17088211}. Note=Associated with postsynaptic endosomes in hippocampal neurons. Associated with presynaptic endosomes in olfactory neurons. {ECO:0000269|PubMed:17088211}.
| null | null | null | null | null |
FUNCTION: Implicated in endocytosis. May recruit other proteins to membranes with high curvature. {ECO:0000269|PubMed:15066995}.
|
Rattus norvegicus (Rat)
|
O35181
|
NRG3_MOUSE
|
MSEGAAGASPPGAASAAAASAEEGTAAAAAAAAAGGGPDGGGEGAAEPPRELRCSDCIVWNRQQTWLCVVPLFIGFIGLGLSLMLLKWIVVGSVKEYVPTDLVDSKGMGQDPFFLSKPSSFPKAMETTTTTTSTTSPATPSAGGAASSRTPNRISTRLTTITRAPTRFPGHRVPIRASPRSTTARNTAAPPTVLSTTAPFFSSSTPGSRPPMPGAPSTQAMPSWPTAAYATSSYLHDSTPSWTLSPFQDAAAASSSSPSSTSSTTTTPETSTSPKFHTTTYSTERSEHFKPCRDKDLAYCLNDGECFVIETLTGSHKHCRCKEGYQGVRCDQFLPKTDSILSDPTDHLGIEFMESEDVYQRQVLSISCIIFGIVIVGMFCAAFYFKSKKQAKQIQEHLKESQNGKNYSLKASSTKSESLMKSHVHLQNYSKADRHPVTALEKIMESSFSAPQSFPEVTSPDRGSQPIKHHSPGQRSGMLHRNTFRRAPPSPRSRLGGIVGPAYQQLEESRIPDQDTIPCQGIEVRKTISHLPIQLWCVERPLDLKYVSNGLRTQQNASINMQLPSRETNPYFNSLDQKDLVGYLSPRANSVPIIPSMGLEETCMQMPGISDVKSIKWCKNSYSADIVNASMPVSDCLLEEQQEVKILLETVQEQIRILTDARRSEDFELASMETEDSASENTAFLPLSPTAKSEREAQFVLRNEIQRDSVLTK
| null | null |
animal organ development [GO:0048513]; chemorepulsion involved in interneuron migration from the subpallium to the cortex [GO:0021842]; ERBB4 signaling pathway [GO:0038130]; ERBB4-ERBB4 signaling pathway [GO:0038138]; intracellular signal transduction [GO:0035556]; mammary gland development [GO:0030879]; mammary placode formation [GO:0060596]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of neuron migration [GO:2001223]; pattern specification process [GO:0007389]; synapse assembly [GO:0007416]
|
extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; synapse [GO:0045202]
|
chemorepellent activity [GO:0045499]; growth factor activity [GO:0008083]; receptor ligand activity [GO:0048018]
| null |
2.10.25.10;
|
Neuregulin family
|
PTM: Proteolytic cleavage close to the plasma membrane on the external face leads to the release of the soluble growth factor form. {ECO:0000250}.; PTM: Extensive glycosylation precedes the proteolytic cleavage. {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Pro-neuregulin-3, membrane-bound isoform]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Does not seem to be active. {ECO:0000250}.; SUBCELLULAR LOCATION: [Neuregulin-3]: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Direct ligand for the ERBB4 tyrosine kinase receptor. Binding results in ligand-stimulated tyrosine phosphorylation and activation of the receptor. Does not bind to the EGF receptor, ERBB2 or ERBB3 receptors. {ECO:0000269|PubMed:9275162}.
|
Mus musculus (Mouse)
|
O35182
|
SMAD6_MOUSE
|
MFRSKRSGLVRRLWRSRVVPDREEGSGGGGGVDEDGSLGSRAEPAPRAREGGGCSRSEVRSVAPRRPRDAVGPRGAAIAGRRRRTGGLPRPVSESGAGAGGSPLDVAEPGGPGWLPESDCETVTCCLFSERDAAGAPRDSGDPQARQSPEPEEGGGPRSREARSRLLLLEQELKTVTYSLLKRLKERSLDTLLEAVESRGGVPGGCVLVPRADLRLGGQPAPPQLLLGRLFRWPDLQHAVELKPLCGCHSFTAAADGPTVCCNPYHFSRLCGPESPPPPYSRLSPPDQYKPLDLSDSTLSYTETEATNSLITAPGEFSDASMSPDATKPSHWCSVAYWEHRTRVGRLYAVYDQAVSIFYDLPQGSGFCLGQLNLEQRSESVRRTRSKIGFGILLSKEPDGVWAYNRGEHPIFVNSPTLDAPGGRALVVRKVPPGYSIKVFDFERSGLLQHADAAHGPYDPHSVRISFAKGWGPCYSRQFITSCPCWLEILLNNHR
| null | null |
anatomical structure morphogenesis [GO:0009653]; aorta development [GO:0035904]; aortic valve morphogenesis [GO:0003180]; BMP signaling pathway [GO:0030509]; cardiac vascular smooth muscle cell development [GO:0060948]; cell differentiation [GO:0030154]; cell-substrate adhesion [GO:0031589]; coronary vasculature development [GO:0060976]; coronary vasculature morphogenesis [GO:0060977]; fat cell differentiation [GO:0045444]; heart valve development [GO:0003170]; immune response [GO:0006955]; mitral valve morphogenesis [GO:0003183]; negative regulation of activin receptor signaling pathway [GO:0032926]; negative regulation of apoptotic process [GO:0043066]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of ossification [GO:0030279]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of SMAD protein signal transduction [GO:0060392]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; outflow tract septum morphogenesis [GO:0003148]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of vasoconstriction [GO:0045907]; pulmonary valve morphogenesis [GO:0003184]; regulation of transcription by RNA polymerase II [GO:0006357]; response to estrogen [GO:0043627]; response to laminar fluid shear stress [GO:0034616]; response to lipopolysaccharide [GO:0032496]; SMAD protein signal transduction [GO:0060395]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ureteric bud development [GO:0001657]; vasoconstriction [GO:0042310]; ventricular septum development [GO:0003281]; zygotic specification of dorsal/ventral axis [GO:0007352]
|
cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; heteromeric SMAD protein complex [GO:0071144]; nuclear body [GO:0016604]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
chromatin binding [GO:0003682]; co-SMAD binding [GO:0070410]; I-SMAD binding [GO:0070411]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein sequestering activity [GO:0140311]; R-SMAD binding [GO:0070412]; transcription cis-regulatory region binding [GO:0000976]; transcription regulator inhibitor activity [GO:0140416]; type I activin receptor binding [GO:0070698]; 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: Monoubiquitinated at Lys-174 by the E2/E3 hybrid ubiquitin-protein ligase UBE2O, leading to reduced binding affinity for the activated BMP type I receptor ACVR1/ALK2, thereby enhancing BMP7 and regulating adipocyte differentiation (By similarity). Ubiquitinated by WWP1 (PubMed:15221015). Ubiquitinated by ARK2C, promoting proteasomal degradation, leading to enhance the BMP-Smad signaling (PubMed:23610558). {ECO:0000250|UniProtKB:O43541, ECO:0000269|PubMed:15221015, ECO:0000269|PubMed:23610558}.; PTM: Arginine methylation by PRMT1, which is recruited by BMPR2, initiates BMP-Induced signaling and induces dissociation from the BMPR1B receptor at the cell surface leading to derepress downstream Smad1/Smad5 signaling. {ECO:0000269|PubMed:23747011}.; PTM: Phosphorylated by BMP type 1 receptor kinase and by PRKX. {ECO:0000250|UniProtKB:O43541}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Transforming growth factor-beta superfamily receptors signaling occurs through the Smad family of intracellular mediators. SMAD6 is an inhibitory Smad (i-Smad) that negatively regulates signaling downstream of type I transforming growth factor-beta (By similarity). Acts as a mediator of TGF-beta and BMP anti-inflammatory activities. Suppresses IL1R-TLR signaling through its direct interaction with PEL1, preventing NF-kappa-B activation, nuclear transport and NF-kappa-B-mediated expression of pro-inflammatory genes (PubMed:16951688). Blocks the BMP-SMAD1 signaling pathway by competing with SMAD4 for receptor-activated SMAD1-binding. Binds to regulatory elements in target promoter regions (By similarity). {ECO:0000250|UniProtKB:O43541, ECO:0000269|PubMed:16951688}.
|
Mus musculus (Mouse)
|
O35185
|
BHE40_MOUSE
|
MERIPSAQPPPTCLPKAPGLEHGDLSGMDFAHMYQVYKSRRGIKRSEDSKETYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTNLIDQQQQKIIALQSGLQAGDLSGRNLEAGQEMFCSGFQTCAREVLQYLAKHENTRDLKSSQLVTHLHRVVSELLQGGASRKPLDSAPKAVDLKEKPSFLAKGSEGPGKNCVPVIQRTFAPSGGEQSGSDTDTDSGYGGELEKGDLRSEQPYFKSDHGRRFAVGERVSTIKQESEEPPTKKSRMQLSEEEGHFAGSDLMGSPFLGPHPHQPPFCLPFYLIPPSATAYLPMLEKCWYPTSVPVLYPGLNTSAAALSSFMNPDKIPTPLLLPQRLPSPLAHSSLDSSALLQALKQIPPLNLETKD
| null | null |
anterior/posterior pattern specification [GO:0009952]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; entrainment of circadian clock by photoperiod [GO:0043153]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of circadian rhythm [GO:0042752]; regulation of neurogenesis [GO:0050767]; regulation of transcription by RNA polymerase II [GO:0006357]; response to light stimulus [GO:0009416]
|
cytoplasm [GO:0005737]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; MRF binding [GO:0043426]; protein domain specific binding [GO:0019904]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]
|
PF07527;PF00010;
|
6.10.250.980;4.10.280.10;
| null |
PTM: Ubiquitinated; which may lead to proteasomal degradation. {ECO:0000250}.; PTM: Sumoylation inhibits its ubiquitination and promotes its negative regulation of the CLOCK-BMAL1 heterodimer transcriptional activator activity. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14503}. Nucleus {ECO:0000250|UniProtKB:O14503}. Note=Predominantly localized in the nucleus (By similarity). {ECO:0000250|UniProtKB:O14503}.
| null | null | null | null | null |
FUNCTION: Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes (PubMed:18411297). Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional repressors (PER/CRY loop) (PubMed:14672706). Both these loops are interlocked as it represses the expression of PER1/2 and in turn is repressed by PER1/2 and CRY1/2 (By similarity). Represses the activity of the circadian transcriptional activator: CLOCK-BMAL1|BMAL2 heterodimer by competing for the binding to E-box elements (5'-CACGTG-3') found within the promoters of its target genes (By similarity). Negatively regulates its own expression and the expression of DBP and BHLHE41/DEC2 (PubMed:14672706). Acts as a corepressor of RXR and the RXR-LXR heterodimers and represses the ligand-induced RXRA and NR1H3/LXRA transactivation activity (PubMed:19786558). May function as a transcriptional factor for neuronal differentiation (PubMed:9284045). Represses the transcription of NR0B2 and attentuates the transactivation of NR0B2 by the CLOCK-BMAL1 complex (By similarity). Drives the circadian rhythm of blood pressure through transcriptional repression of ATP1B1 in the cardiovascular system (PubMed:30012868). {ECO:0000250|UniProtKB:O14503, ECO:0000269|PubMed:14672706, ECO:0000269|PubMed:18411297, ECO:0000269|PubMed:19786558, ECO:0000269|PubMed:30012868, ECO:0000269|PubMed:9284045}.
|
Mus musculus (Mouse)
|
O35186
|
CATK_RAT
|
MWVFKFLLLPVVSFALSPEETLDTQWELWKKTHGKQYNSKVDEISRRLIWEKNLKKISVHNLEASLGAHTYELAMNHLGDMTSEEVVQKMTGLRVPPSRSFSNDTLYTPEWEGRVPDSIDYRKKGYVTPVKNQGQCGSCWAFSSAGALEGQLKKKTGKLLALSPQNLVDCVSENYGCGGGYMTTAFQYVQQNGGIDSEDAYPYVGQDESCMYNATAKAAKCRGYREIPVGNEKALKRAVARVGPVSVSIDASLTSFQFYSRGVYYDENCDRDNVNHAVLVVGYGTQKGNKYWIIKNSWGESWGNKGYVLLARNKNNACGITNLASFPKM
|
3.4.22.38
| null |
bone resorption [GO:0045453]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to zinc ion starvation [GO:0034224]; collagen catabolic process [GO:0030574]; immune response [GO:0006955]; intramembranous ossification [GO:0001957]; mononuclear cell differentiation [GO:1903131]; negative regulation of cartilage development [GO:0061037]; positive regulation of apoptotic signaling pathway [GO:2001235]; proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603]; response to ethanol [GO:0045471]; response to insulin [GO:0032868]; response to organic cyclic compound [GO:0014070]; thyroid hormone generation [GO:0006590]
|
apical plasma membrane [GO:0016324]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lysosome [GO:0005764]; nucleoplasm [GO:0005654]
|
collagen binding [GO:0005518]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; fibronectin binding [GO:0001968]; proteoglycan binding [GO:0043394]
|
PF08246;PF00112;
|
3.90.70.10;
|
Peptidase C1 family
| null |
SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P43235}. Secreted {ECO:0000250|UniProtKB:P43235}. Apical cell membrane {ECO:0000250|UniProtKB:P43235}; Peripheral membrane protein {ECO:0000250|UniProtKB:P43235}; Extracellular side {ECO:0000250|UniProtKB:P43235}. Note=Localizes to the lumen of thyroid follicles and to the apical membrane of thyroid epithelial cells. {ECO:0000250|UniProtKB:P43235}.
|
CATALYTIC ACTIVITY: Reaction=Broad proteolytic activity. With small-molecule substrates and inhibitors, the major determinant of specificity is P2, which is preferably Leu, Met > Phe, and not Arg.; EC=3.4.22.38;
| null | null | null | null |
FUNCTION: Thiol protease involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation. Involved in the release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen. {ECO:0000250|UniProtKB:P43235}.
|
Rattus norvegicus (Rat)
|
O35188
|
X3CL1_MOUSE
|
MAPSPLAWLLRLAAFFHLCTLLPGQHLGMTKCEIMCDKMTSRIPVALLIRYQLNQESCGKRAIVLETTQHRRFCADPKEKWVQDAMKHLDHQAAALTKNGGKFEKRVDNVTPGITLATRGLSPSALTKPESATLEDLALELTTISQEARGTMGTSQEPPAAVTGSSLSTSEAQDAGLTAKPQSIGSFEAADISTTVWPSPAVYQSGSSSWAEEKATESPSTTAPSPQVSTTSPSTPEENVGSEGQPPWVQGQDLSPEKSLGSEEINPVHTDNFQERGPGNTVHPSVAPISSEETPSPELVASGSQAPKIEEPIHATADPQKLSVLITPVPDTQAATRRQAVGLLAFLGLLFCLGVAMFAYQSLQGCPRKMAGEMVEGLRYVPRSCGSNSYVLVPV
| null | null |
angiogenesis involved in wound healing [GO:0060055]; autocrine signaling [GO:0035425]; cell-cell adhesion [GO:0098609]; 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]; chemotaxis [GO:0006935]; cytokine-mediated signaling pathway [GO:0019221]; eosinophil chemotaxis [GO:0048245]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; G protein-coupled receptor signaling pathway [GO:0007186]; inflammatory response [GO:0006954]; inhibitory postsynaptic potential [GO:0060080]; integrin activation [GO:0033622]; leukocyte migration involved in inflammatory response [GO:0002523]; lymphocyte chemotaxis [GO:0048247]; microglial cell activation [GO:0001774]; microglial cell proliferation [GO:0061518]; monocyte chemotaxis [GO:0002548]; negative regulation of cell migration [GO:0030336]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of glutamate receptor signaling pathway [GO:1900450]; negative regulation of hippocampal neuron apoptotic process [GO:0110091]; negative regulation of interleukin-1 alpha production [GO:0032690]; negative regulation of tumor necrosis factor production [GO:0032720]; negative regulation of vasoconstriction [GO:0045906]; neuron cellular homeostasis [GO:0070050]; neutrophil chemotaxis [GO:0030593]; positive regulation of actin filament bundle assembly [GO:0032233]; positive regulation of calcium-independent cell-cell adhesion [GO:0051041]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell migration [GO:0030335]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of I-kappaB phosphorylation [GO:1903721]; positive regulation of inflammatory response [GO:0050729]; positive regulation of macrophage chemotaxis [GO:0010759]; positive regulation of microglial cell migration [GO:1904141]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of neuron projection development [GO:0010976]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transforming growth factor beta1 production [GO:0032914]; regulation of lipopolysaccharide-mediated signaling pathway [GO:0031664]; response to ischemia [GO:0002931]; wound healing [GO:0042060]
|
cell body [GO:0044297]; cell projection [GO:0042995]; cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]
|
CCR chemokine receptor binding [GO:0048020]; chemoattractant activity [GO:0042056]; chemokine activity [GO:0008009]; CX3C chemokine receptor binding [GO:0031737]; CXCR1 chemokine receptor binding [GO:0045237]; integrin binding [GO:0005178]
|
PF00048;
|
2.40.50.40;
|
Intercrine delta family
|
PTM: A soluble short 80 kDa form may be released by proteolytic cleavage from the long membrane-anchored form. {ECO:0000269|PubMed:10382755}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9177350}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Processed fractalkine]: Secreted {ECO:0000269|PubMed:10382755}.
| null | null | null | null | null |
FUNCTION: Chemokine that acts as a ligand for both CX3CR1 and integrins ITGAV:ITGB3 and ITGA4:ITGB1 (PubMed:10187784, PubMed:18971423). The CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis (PubMed:10187784, PubMed:10382755, PubMed:18971423, PubMed:9177350). Regulates leukocyte adhesion and migration processes at the endothelium (PubMed:10382755, PubMed:9177350). Can activate integrins in both a CX3CR1-dependent and CX3CR1-independent manner (By similarity). In the presence of CX3CR1, activates integrins by binding to the classical ligand-binding site (site 1) in integrins (By similarity). In the absence of CX3CR1, binds to a second site (site 2) in integrins which is distinct from site 1 and enhances the binding of other integrin ligands to site 1 (By similarity). {ECO:0000250|UniProtKB:P78423, ECO:0000269|PubMed:10187784, ECO:0000269|PubMed:10382755, ECO:0000269|PubMed:18971423, ECO:0000269|PubMed:9177350}.; FUNCTION: [Processed fractalkine]: The soluble form is chemotactic for T-cells and monocytes, but not for neutrophils. {ECO:0000250|UniProtKB:P78423}.; FUNCTION: [Fractalkine]: The membrane-bound form promotes adhesion of those leukocytes to endothelial cells. {ECO:0000250|UniProtKB:P78423}.
|
Mus musculus (Mouse)
|
O35206
|
COFA1_MOUSE
|
MTHRRTAQGRRPRWLLSIISALLSAVLQTRAATGSASQVHLDLTVLIGVPLPSSVSFTTGYGGFPAYSFGPGANVGRPARTLIPPTFFRDFAIGVAVKPNSAQGGVLFAITDAFQKVIYLGLRLSSVEDGRQRVILYYTEPGSHVSREAAVFSVPVMTNRWNRFAVTVQGEEVALFMDCEEQSQVRFQRSSWPLTFEPSAGIFVGNAGAMGLERFTGSIQQLTIYSDPRTPEELCEAQESSASGEASGFQEMDEVAEIMEAVTYTQAPPKESHVDPISVPPTSSSPAEDSELSGEPVPEGTPETNLSIIGHSSPEQGSGEILNDTLEVHAMDGDPGTDDGSGDGALLNVTDGQGLSATATGEASVPVTTVLEAENGSMPTGSPTLAMFTQSIREVDTPDPENLTTTASGDGEVPTSTDGDTEADSSPTGGPTLKPREEATLGSHGEEWLTPAVSKMPLKAFEEEEASGTAIDSLDVIFTPTVVLEQVSRRPTDIQATFTPTVVLEETSGAPTDTQDALTPTVAPEQMFTAEPTDGGDLVASTEEAEEEGSGSMPPSGPPLPTPTVTPKRQVTLVGVEAEGSGPVGGLDEGSGSGDIVGNEDLLRGPPGPPGPPGSPGIPGKPGTDVFMGPPGSPGEDGAPGEPGPQGPEGQPGLDGASGQQGMKGEKGARGPNGSAGEKGDPGNRGLPGPPGKNGEVGTPGVMGPPGPPGPPGPPGPGCTTELGFEIEGSGDVRLLSKPTISGPTSPSGPKGEKGEQGAKGERGADGTSTMGPPGPRGPPGHVEVLSSSLINITNGSMNFSDIPELMGPPGPDGVPGLPGFPGPRGPKGDTGVPGFPGLKGEQGEKGEPGAILTGDVPLEMMKGRKGEPGIHGAPGPMGPKGPPGHKGEFGLPGRPGRPGLNGLKGAKGDRGVTLPGPPGLPGPPGPPGPPGAVVNIKGAVFPIPARPHCKTPVGTAHPGDPELVTFHGVKGEKGSWGLPGSKGEKGDQGAQGPPGPPVDPAYLRHFLNSLKGENEDASFRGESSNNLFVSGPPGLPGYPGLVGQKGEAVVGPQGPPGIPGLPGPPGFGRPGVPGPPGPPGPPGPPAILGAAVALPGPPGPPGQPGLPGSRNLVTALSDMGDMLQKAHLVIEGTFIYLRDSGEFFIRVRDGWKKLQLGELIPIPADSPPPPALSSNPYQPQPPLNPILSANYERPVLHLVALNTPVAGDIRADFQCFQQARAAGLLSTFRAFLSSHLQDLSTVVRKAERFGLPIVNLKGQVLFNNWDSIFSGDGGQFNTHIPIYSFDGRDVMTDPSWPQKVVWHGSNPHGVRLVDKYCEAWRTTDMAVTGFASPLSTGKILDQKAYSCANRLIVLCIENSFMTDTRK
| null | null |
cell adhesion [GO:0007155]; extracellular matrix organization [GO:0030198]
|
basement membrane [GO:0005604]; collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]
|
extracellular matrix structural constituent conferring tensile strength [GO:0030020]
|
PF01391;PF20010;PF06482;PF13385;
|
2.60.120.200;3.40.1620.70;3.10.100.10;
|
Multiplexin collagen family
|
PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250}.; PTM: O-glycosylated; contains chondroitin sulfate. {ECO:0000250|UniProtKB:P39059}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Secreted {ECO:0000250|UniProtKB:P39059}.
| null | null | null | null | null |
FUNCTION: Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle.; FUNCTION: Restin potently inhibits angiogenesis.
|
Mus musculus (Mouse)
|
O35216
|
CENPA_MOUSE
|
MGPRRKPQTPRRRPSSPAPGPSRQSSSVGSQTLRRRQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGVDFWWQAQALLALQEAAEAFLIHLFEDAYLLSLHAGRVTLFPKDIQLTRRIRGFEGGLP
| null | null |
CENP-A containing chromatin assembly [GO:0034080]; establishment of mitotic spindle orientation [GO:0000132]; kinetochore assembly [GO:0051382]; mitotic cytokinesis [GO:0000281]; protein localization to CENP-A containing chromatin [GO:0061644]; protein localization to chromosome, centromeric region [GO:0071459]
|
CENP-A containing chromatin [GO:0061638]; CENP-A containing nucleosome [GO:0043505]; chromosome, centromeric region [GO:0000775]; condensed chromosome, centromeric region [GO:0000779]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]
|
DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
|
PF00125;
|
1.10.20.10;
|
Histone H3 family
|
PTM: Poly-ADP-ribosylated by PARP1.; PTM: Trimethylated by NTMT1 at the N-terminal glycine after cleavage of Met-1. Methylation is low before incorporation into nucleosomes and increases with cell cycle progression, with the highest levels in mitotic nucleosomes. {ECO:0000250|UniProtKB:P49450}.; PTM: Phosphorylated by CDK1 at Ser-62 during early mitosis; this abolishes association with chromatin and centromeres, prevents interaction with HJURP and thereby prevents premature assembly of CENPA into centromeres. Dephosphorylated at Ser-62 by PPP1CA during late mitosis. {ECO:0000250|UniProtKB:P49450}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49450}. Chromosome, centromere {ECO:0000250|UniProtKB:P49450}. Note=Localizes exclusively to sites of kinetochore assembly in centromeres. Occupies a compact domain at the inner kinetochore plate stretching across 2 thirds of the length of the constriction but encompassing only one third of the constriction width and height. Phosphorylation at Ser-62 during early mitosis abolishes association with chromatin and centromeres and results in dispersed nuclear location. {ECO:0000250|UniProtKB:P49450}.
| null | null | null | null | null |
FUNCTION: Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore. The presence of CENPA subtly modifies the nucleosome structure and the way DNA is wrapped around the nucleosome and gives rise to protruding DNA ends that are less well-ordered and rigid compared to nucleosomes containing histone H3. May serve as an epigenetic mark that propagates centromere identity through replication and cell division (By similarity). Required for recruitment and assembly of kinetochore proteins, and as a consequence required for progress through mitosis, chromosome segregation and cytokinesis (PubMed:27499292). {ECO:0000250|UniProtKB:P49450, ECO:0000269|PubMed:27499292}.
|
Mus musculus (Mouse)
|
O35217
|
MINP1_RAT
|
MLRGARSHLSASVALAAVLAAALLSSFARCSLPGRGDPVASVLSPYFGTKTRYEDVNPWLLGDPVAPRRDPELLAGTCTPVQLVALIRHGTRYPTTKQIRKLRQLQGLLQTRESVDGGSRVAAALDQWPLWYDDWMDGQLVEKGRQDMRQLALRLAALFPDLFCRENYGRLRLITSSKHRCVDSSAAFLQGLWQHYHPGLPPPDVSDMECDPPRVNDKLMRFFDHCEKFLTEVERNATALYHVEAFKTGPEMQTVLKKVAATLQVPVNNLNADLIQVAFFTCSFDLAIQGVHSPWCDVFDVDDAKVLEYLNDLKQYWKRSYGYAINSRSSCNLFQDIFLHLDKAVEQKQRSQPVSSSVILQFGHAETLLPLLSLMGYFKDKEPLTAYNFEEQVHREFRSGHIVPYASNLIFVLYHCEDAQTPQEKFQIQMLLNEKVLPLAHSQKTVALYEDLKNHYQDILQSCQTSKECNLPKVNITSDEL
|
3.1.3.62; 3.1.3.80
| null |
intracellular monoatomic cation homeostasis [GO:0030003]; phosphatidylinositol-mediated signaling [GO:0048015]
|
endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
3-phytase activity [GO:0016158]; 4-phytase activity [GO:0008707]; acid phosphatase activity [GO:0003993]; bisphosphoglycerate 3-phosphatase activity [GO:0034417]; inositol bisphosphate phosphatase activity [GO:0016312]; inositol hexakisphosphate 2-phosphatase activity [GO:0052826]; inositol pentakisphosphate phosphatase activity [GO:0052827]; inositol phosphate phosphatase activity [GO:0052745]; inositol trisphosphate phosphatase activity [GO:0046030]; inositol-1,3,4,5,6-pentakisphosphate 3-phosphatase activity [GO:0030351]; inositol-1,4,5,6-tetrakisphosphate 6-phosphatase activity [GO:0030352]; inositol-hexakisphosphate phosphatase activity [GO:0004446]
|
PF00328;
|
3.40.50.1240;
|
Histidine acid phosphatase family, MINPP1 subfamily
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9UNW1}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:8384201}. Secreted {ECO:0000250|UniProtKB:Q9UNW1}. Cell membrane {ECO:0000250|UniProtKB:Q9Z2L6}. Note=Also associated with the plasma membrane in erythrocytes. {ECO:0000250|UniProtKB:Q9Z2L6}.
|
CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:58130; EC=3.1.3.62; Evidence={ECO:0000269|PubMed:1653239}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990; Evidence={ECO:0000269|PubMed:1653239}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,2,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77115, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:195535; EC=3.1.3.62; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77116; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,2,6-trisphosphate + phosphate; Xref=Rhea:RHEA:77119, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195535, ChEBI:CHEBI:195537; EC=3.1.3.62; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77120; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,6-trisphosphate + H2O = 1D-myo-inositol 1,2-bisphosphate + phosphate; Xref=Rhea:RHEA:77131, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195537, ChEBI:CHEBI:195539; EC=3.1.3.62; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77132; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2-bisphosphate + H2O = 1D-myo-inositol 2-phosphate + phosphate; Xref=Rhea:RHEA:77135, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:195539; EC=3.1.3.62; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77136; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:20960, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58130, ChEBI:CHEBI:58747; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20961; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,3,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,2,3,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77111, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58747, ChEBI:CHEBI:195534; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77112; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,3,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,2,3-trisphosphate + phosphate; Xref=Rhea:RHEA:77123, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195534, ChEBI:CHEBI:195536; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77124; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,2,3-trisphosphate + H2O = 1D-myo-inositol 2,3-bisphosphate + phosphate; Xref=Rhea:RHEA:77127, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195536, ChEBI:CHEBI:195538; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77128; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 2,3-bisphosphate + H2O = 1D-myo-inositol 2-phosphate + phosphate; Xref=Rhea:RHEA:77139, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:195538; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77140; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,4,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77143, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57627, ChEBI:CHEBI:57733; Evidence={ECO:0000269|PubMed:1653239, ECO:0000269|PubMed:9359836}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77144; Evidence={ECO:0000269|PubMed:1653239, ECO:0000269|PubMed:9359836}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4,5,6-tetrakisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + phosphate; Xref=Rhea:RHEA:77147, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57627, ChEBI:CHEBI:203600; Evidence={ECO:0000269|PubMed:9359836}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77148; Evidence={ECO:0000269|PubMed:9359836}; CATALYTIC ACTIVITY: Reaction=(2R)-2,3-bisphosphoglycerate + H2O = (2R)-2-phosphoglycerate + phosphate; Xref=Rhea:RHEA:27381, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58248, ChEBI:CHEBI:58289; EC=3.1.3.80; Evidence={ECO:0000250|UniProtKB:Q9UNW1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27382; Evidence={ECO:0000250|UniProtKB:Q9UNW1};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40 nM for 1D-myo-inositol 1,3,4,5,6-pentakisphosphate {ECO:0000269|PubMed:1653239}; KM=0.3 nM for 1D-myo-inositol hexakisphosphate {ECO:0000269|PubMed:1653239}; Vmax=211 nmol/min/mg enzyme with 1D-myo-inositol 1,3,4,5,6-pentakisphosphate as substrate {ECO:0000269|PubMed:1653239}; Vmax=12 nmol/min/mg enzyme with 1D-myo-inositol hexakisphosphate as substrate {ECO:0000269|PubMed:1653239};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-9 with 1D-myo-inositol 1,3,4,5,6-pentakisphosphate or 1D-myo-inositol hexakisphosphate as substrate in absence of magnesium. Optimum pH is 7.4 with 1D-myo-inositol hexakisphosphate as substrate in presence of 1 mM magnesium. {ECO:0000269|PubMed:1653239};
| null |
FUNCTION: Multiple inositol polyphosphate phosphatase that hydrolyzes 1D-myo-inositol 1,3,4,5,6-pentakisphosphate (InsP5[2OH]) and 1D-myo-inositol hexakisphosphate (InsP6) to a range of less phosphorylated inositol phosphates. This regulates the availability of these various small molecule second messengers and metal chelators which control many aspects of cell physiology (PubMed:1653239, PubMed:9359836). Has a weak in vitro activity towards 1D-myo-inositol 1,4,5-trisphosphate which is unlikely to be physiologically relevant. By regulating intracellular inositol polyphosphates pools, which act as metal chelators, it may control the availability of intracellular calcium and iron, which are important for proper neuronal development and homeostasis. May have a dual substrate specificity, and function as a 2,3-bisphosphoglycerate 3-phosphatase hydrolyzing 2,3-bisphosphoglycerate to 2-phosphoglycerate. 2,3-bisphosphoglycerate (BPG) is formed as part of the Rapoport-Luebering glycolytic bypass and is a regulator of systemic oxygen homeostasis as the major allosteric effector of hemoglobin (By similarity). {ECO:0000250|UniProtKB:Q9UNW1, ECO:0000269|PubMed:1653239, ECO:0000269|PubMed:9359836}.
|
Rattus norvegicus (Rat)
|
O35219
|
KCNH2_MOUSE
|
MPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARVENCAVIYCNDGFCELCGYSRAEVMQRPCTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDGAVIMFILNFEVVMEKDMVGSPAHDTNHRGPSTSWLASGRAKTFRLKLPALLALTARESSVRTGSMHSAGAPGAVVVDVDLTPAAPSSESLALDEVSAMDNHVAGLGPAEERRALVGPGSASPVASIRGPHPSPRAQSLNPDASGSSCSLARTRSRESCASVRRASSADDIEAMRAGALPPPPRHASTGAMHPLRSGLLNSTSDSDLVRYRTISKIPQITLNFVDLKGDPFLASPTSDREIIAPKIKERTHNVTEKVTQVLSLGADVLPEYKLQAPRIHRWTILHYSPFKAVWDWLILLLVIYTAVFTPYSAAFLLKETEDGSQAPDCGYACQPLAVVDLIVDIMFIVDILINFRTTYVNANEEVVSHPGRIAVHYFKGWFLIDMVAAIPFDLLIFGSGSEELIGLLKTARLLRLVRVARKLDRYSEYGAAVLFLLMCTFALIAHWLACIWYAIGNMEQPHMDSHIGWLHNLGDQIGKPYNSSGLGGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVREFIRFHQIPNPLRQRLEEYFQHAWSYTNGIDMNAVLKGFPECLQADICLHLNRSLLQHCKPFRGATKGCLRALAMKFKTTHAPPGDTLVHAGDLLTALYFISRGSIEILRGDVVVAILGKNDIFGEPLNLYARPGKSNGDVRALTYCDLHKIHRDDLLEVLDMYPEFSDHFWSSLEITFNLRDTNMIPGSPGSAELESGFNRQRKRKLSFRRRTDKDTEQPGEVSALGQGPARVGPGPSCRGQPGGPWGESPSSGPSSPESSEDEGPGRSSSPLRLVPFSSPRPPGDPPGGEPLTEDGEKSDTCNPLSGAFSGVSNIFSFWGDSRGRQYQELPRCPAPAPSLLNIPLSSPGRRSRGDVESRLDALQRQLNRLETRLSADMATVLQLLQRQMTLVPPAYSAVTTPGPGPTSASPLLPVGPVPTLTLDSLSQVSQFVAFEELPAGAPELPQDGPTRRLSLPGQLGALTSQPLHRHGSDPGS
| null | null |
membrane repolarization during cardiac muscle cell action potential [GO:0086013]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of membrane potential [GO:0042391]; regulation of ventricular cardiac muscle cell membrane repolarization [GO:0060307]
|
monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886]
|
inward rectifier potassium channel activity [GO:0005242]; monoatomic ion channel activity [GO:0005216]; potassium channel activity [GO:0005267]; protein-containing complex binding [GO:0044877]; scaffold protein binding [GO:0097110]; voltage-gated potassium channel activity [GO:0005249]
|
PF00027;PF00520;PF13426;
|
1.10.1200.260;1.10.287.70;2.60.120.10;3.30.450.20;
|
Potassium channel family, H (Eag) (TC 1.A.1.20) subfamily, Kv11.1/KCNH2 sub-subfamily
|
PTM: Phosphorylated on serine and threonine residues. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12809}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr) (By similarity). {ECO:0000250|UniProtKB:Q12809}.
|
Mus musculus (Mouse)
|
O35226
|
PSMD4_MOUSE
|
MVLESTMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTTLTPDTGRILSKLHTVQPKGKITFCTGIRVAHLALKHRQGKNHKMRIIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGEEEVNTEKLTAFVNTLNGKDGTGSHLVTVPPGPSLADALISSPILAGEGGAMLGLGASDFEFGVDPSADPELALALRVSMEEQRQRQEEEARRAAAASAAEAGIATPGTEDSDDALLKMTINQQEFGRPGLPDLSSMTEEEQIAYAMQMSLQGTEFSQESADMDASSAMDTSDPVKEEDDYDVMQDPEFLQSVLENLPGVDPNNAAIRSVMGALASQATKDGKNDKKEEEKK
| null | null |
proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]
|
cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome regulatory particle, base subcomplex [GO:0008540]
|
identical protein binding [GO:0042802]; polyubiquitin modification-dependent protein binding [GO:0031593]
|
PF02809;PF13519;
|
6.10.250.380;6.10.300.40;3.40.50.410;
|
Proteasome subunit S5A family
| null | null | null | null | null | null | null |
FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMD4 acts as an ubiquitin receptor subunit through ubiquitin-interacting motifs and selects ubiquitin-conjugates for destruction. Displays a preferred selectivity for longer polyubiquitin chains. {ECO:0000250|UniProtKB:P55036}.
|
Mus musculus (Mouse)
|
O35227
|
ADAM7_MOUSE
|
MLTTGIFWMTVLISHIQERGIVGVEGQELVHPKKLPLLHKRDLERIHDSDIPEEYEEELLYEIKLGKKTLILHLLKAREFLSSNYSETYYNVKREVFTKHPQILDHCFYQGSIIHEFDSAASISTCNGLRGFFRVNDQRYLIEPVKYSDDGEHLVYKYNVKAPYATNHSCVGLNFTKKSALIDVENIEEHNAEDHHKEKFIELFVVADEYVYRRNNKPQNKLRKRIWGMVNFVNMIYKTLNIHVTLAGFEIWSAGDKIEIVSNLESTLLHFSTWQETVLKKRKDFDHVILLSGKWLYTSMQGIAYPGGICQILRSCSVVKDLLPDVNIIGNRMAHQLGHSLGMQHDGFPCTCPLGKCVMGDGSIPAIKFSKCSQTQYQQFLQDQKPACILNNPFPEEFNDYPFCGNKKVDEGEECDCGPVQECTNPCCDAHKCVLKPGFTCVEGECCESCQMKKEGAVCRLAKNECDISEVCTGYSPECPKDEFQANGFPCRNGEGYCFMGLCPTRNEQCSELFIGGAEESHSLCYRMNKKGNRFGYCKNKGNTFVPCEEKDLKCGKIYCSGGRPSSRLGEDKAYNLKNVKQNVTIKCRTMFLHHNSRDMGLVNSGTKCGDGMVCSNGECIEMEKAYNSTICSSPCDENDVDDNEPECQCEEGSIITEWGEALNLTSVSIMVIVLVMVIIGVGLVILLIRYQKCIKMKQVQSSPREIRGVENKGYFPEEHQTRSEPILTDIHPLHTTAESLERVPSSFSSPHYITLKSVSKDSRGIADPKQTDNVNLNLDTQSGCERLG
| null | null |
epididymis development [GO:1905867]; epithelial cell morphogenesis [GO:0003382]; positive regulation of flagellated sperm motility [GO:1902093]; positive regulation of sperm capacitation [GO:1902492]; proteolysis [GO:0006508]
|
apical part of cell [GO:0045177]; plasma membrane [GO:0005886]
|
endopeptidase activity [GO:0004175]; metalloendopeptidase activity [GO:0004222]
|
PF08516;PF00200;PF01562;PF01421;
|
3.40.390.10;4.10.70.10;
| null | null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:20945367}; Single-pass type I membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Required for normal male fertility via maintenance of epithelial cell morphology in the caput epididymis and subsequently correct epididymis lumen structure required for sperm development (PubMed:26246218). Plays a role in sperm motility, flagella morphology and tyrosine phosphorylation during sperm capacitance (PubMed:26246218). Plays a role in normal expression levels of HSPA5, ITM2B and ADAM2 in sperm both prior to and post-capacitation (PubMed:26246218). This is a non catalytic metalloprotease-like protein (Probable). {ECO:0000269|PubMed:26246218, ECO:0000305|PubMed:9322939}.
|
Mus musculus (Mouse)
|
O35231
|
KIFC3_MOUSE
|
MVPSRRTWNLGATPSLRGLWRVGRVQEPKPGMARPAPASPAARPFPHTGQGRLRTGRGKDILPSGEEDSTSRTAARPSLAQCRALSVDWPGPRSPHRLYLTVQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQPVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIRVIARVRPVTKEDGEGPEATNAVTFDPDDDSIIHLLHKGKPVSFELDKVFSPWASQQDVFQEVQALITSCIDGFNVCIFAYGQTGAGKTYTMEGTPENPGINQRALQLLFSEVQEKASDWQYNITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGYNNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSERVGKSGAEGNRLREAQHINRSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLRFAERVRSVELGPGSRRTELGSWSSQEHLEWEPACQTPQPTARAHSAPGSGTSSRPGSIRRKLQPSA
| null | null |
epithelial cell-cell adhesion [GO:0090136]; Golgi organization [GO:0007030]; microtubule-based movement [GO:0007018]; microtubule-based process [GO:0007017]; zonula adherens maintenance [GO:0045218]
|
centrosome [GO:0005813]; cytoplasmic vesicle membrane [GO:0030659]; Golgi apparatus [GO:0005794]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; zonula adherens [GO:0005915]
|
ATP binding [GO:0005524]; microtubule binding [GO:0008017]; minus-end-directed microtubule motor activity [GO:0008569]
|
PF00225;
|
3.40.850.10;
|
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11581287}. Cytoplasmic vesicle membrane {ECO:0000305|PubMed:11581287}; Peripheral membrane protein {ECO:0000305|PubMed:11581287}. Cell junction, adherens junction {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Localizes along zonula adherens only at mature cell-cell contacts (By similarity). Apical cell membrane. On membrane organelles immediately beneath the apical plasma membrane of renal tubular epithelial cells. Localized in the distal tubules and loops of Henle in the kidney, but not in the proximal tubules or the glomeruli, with stronger staining in the apical area of these epithelial cells. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Minus-end microtubule-dependent motor protein. Involved in apically targeted transport. Required for zonula adherens maintenance. {ECO:0000269|PubMed:11581287}.
|
Mus musculus (Mouse)
|
O35235
|
TNF11_MOUSE
|
MRRASRDYGKYLRSSEEMGSGPGVPHEGPLHPAPSAPAPAPPPAASRSMFLALLGLGLGQVVCSIALFLYFRAQMDPNRISEDSTHCFYRILRLHENADLQDSTLESEDTLPDSCRRMKQAFQGAVQKELQHIVGPQRFSGAPAMMEGSWLDVAQRGKPEAQPFAHLTINAASIPSGSHKVTLSSWYHDRGWAKISNMTLSNGKLRVNQDGFYYLYANICFRHHETSGSVPTDYLQLMVYVVKTSIKIPSSHNLMKGGSTKNWSGNSEFHFYSINVGGFFKLRAGEEISIQVSNPSLLDPDQDATYFGAFKVQDID
| null | null |
animal organ morphogenesis [GO:0009887]; bone development [GO:0060348]; bone resorption [GO:0045453]; calcium ion homeostasis [GO:0055074]; calcium-mediated signaling [GO:0019722]; cellular response to leukemia inhibitory factor [GO:1990830]; ERK1 and ERK2 cascade [GO:0070371]; immune response [GO:0006955]; JNK cascade [GO:0007254]; lymph node development [GO:0048535]; mammary gland alveolus development [GO:0060749]; mammary gland epithelial cell proliferation [GO:0033598]; monocyte chemotaxis [GO:0002548]; negative regulation of transcription by RNA polymerase II [GO:0000122]; ossification [GO:0001503]; osteoclast development [GO:0036035]; osteoclast differentiation [GO:0030316]; osteoclast proliferation [GO:0002158]; paracrine signaling [GO:0038001]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of bone resorption [GO:0045780]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of corticotropin-releasing hormone secretion [GO:0051466]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fever generation by positive regulation of prostaglandin secretion [GO:0071812]; positive regulation of gene expression [GO:0010628]; positive regulation of homotypic cell-cell adhesion [GO:0034112]; positive regulation of JNK cascade [GO:0046330]; positive regulation of osteoclast development [GO:2001206]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of phosphorylation [GO:0042327]; positive regulation of T cell activation [GO:0050870]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of osteoclast differentiation [GO:0045670]; tooth eruption [GO:0044691]; tumor necrosis factor-mediated signaling pathway [GO:0033209]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
cytokine activity [GO:0005125]; identical protein binding [GO:0042802]; receptor ligand activity [GO:0048018]; tumor necrosis factor receptor binding [GO:0005164]; tumor necrosis factor receptor superfamily binding [GO:0032813]
|
PF00229;
|
2.60.120.40;
|
Tumor necrosis factor family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:10224132}.; PTM: The soluble form of isoform 1 derives from the membrane form by proteolytic processing. The cleavage may be catalyzed by ADAM17. A further shorter soluble form was observed. {ECO:0000269|PubMed:10224132}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.; SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 11, soluble form]: Secreted.
| null | null | null | null | null |
FUNCTION: Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. Osteoclast differentiation and activation factor (PubMed:22437732). Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. May also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy (By similarity). Induces osteoclastogenesis by activating multiple signaling pathways in osteoclast precursor cells, chief among which is induction of long lasting oscillations in the intracellular concentration of Ca (2+) resulting in the activation of NFATC1, which translocates to the nucleus and induces osteoclast-specific gene transcription to allow differentiation of osteoclasts (PubMed:18586671, PubMed:24039232, PubMed:27336669). During osteoclast differentiation, in a TMEM64 and ATP2A2-dependent manner induces activation of CREB1 and mitochondrial ROS generation necessary for proper osteoclast generation (PubMed:23395171, PubMed:26644563). {ECO:0000250|UniProtKB:O14788, ECO:0000269|PubMed:18586671, ECO:0000269|PubMed:22437732, ECO:0000269|PubMed:23395171, ECO:0000269|PubMed:24039232, ECO:0000269|PubMed:26644563, ECO:0000269|PubMed:27336669}.
|
Mus musculus (Mouse)
|
O35240
|
ASIC3_RAT
|
MKPRSGLEEAQRRQASDIRVFASSCTMHGLGHIFGPGGLTLRRGLWATAVLLSLAAFLYQVAERVRYYGEFHHKTTLDERESHQLTFPAVTLCNINPLRRSRLTPNDLHWAGTALLGLDPAEHAAYLRALGQPPAPPGFMPSPTFDMAQLYARAGHSLEDMLLDCRYRGQPCGPENFTVIFTRMGQCYTFNSGAHGAELLTTPKGGAGNGLEIMLDVQQEEYLPIWKDMEETPFEVGIRVQIHSQDEPPAIDQLGFGAAPGHQTFVSCQQQQLSFLPPPWGDCNTASLDPDDFDPEPSDPLGSPRPRPSPPYSLIGCRLACESRYVARKCGCRMMHMPGNSPVCSPQQYKDCASPALDAMLRKDTCVCPNPCATTRYAKELSMVRIPSRASARYLARKYNRSESYITENVLVLDIFFEALNYEAVEQKAAYEVSELLGDIGGQMGLFIGASLLTILEILDYLCEVFQDRVLGYFWNRRSAQKRSGNTLLQEELNGHRTHVPHLSLGPRPPTTPCAVTKTLSASHRTCYLVTRL
| null | null |
detection of chemical stimulus involved in sensory perception [GO:0050907]; detection of chemical stimulus involved in sensory perception of pain [GO:0050968]; detection of mechanical stimulus involved in sensory perception [GO:0050974]; detection of mechanical stimulus involved in sensory perception of pain [GO:0050966]; detection of temperature stimulus involved in sensory perception [GO:0050961]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; establishment of localization in cell [GO:0051649]; monoatomic cation transport [GO:0006812]; monoatomic ion transmembrane transport [GO:0034220]; response to acidic pH [GO:0010447]; response to heat [GO:0009408]; response to mechanical stimulus [GO:0009612]; sensory perception of sour taste [GO:0050915]; sodium ion transmembrane transport [GO:0035725]; sodium ion transport [GO:0006814]
|
perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
enterobactin transmembrane transporter activity [GO:0042931]; ligand-gated sodium channel activity [GO:0015280]; monoatomic cation channel activity [GO:0005261]; pH-gated monoatomic ion channel activity [GO:0160128]
|
PF00858;
|
1.10.3590.10;1.10.287.820;1.10.287.770;
|
Amiloride-sensitive sodium channel (TC 1.A.6) family, ASIC3 subfamily
|
PTM: Phosphorylated by PKA (By similarity). Phosphorylated by PKC. In vitro, PRKCABP/PICK-1 is necessary for PKC phosphorylation and activation of a ASIC3/ACCN3-ASIC2/ASIC2b channel, but does not activate a homomeric ASIC3/ACCN3 channel. {ECO:0000250, ECO:0000269|PubMed:14976185}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=In part cytoplasmic in cochlea cells (By similarity). Cell surface expression may be stabilized by interaction with LIN7B and cytoplasmic retention by interaction with DLG4. {ECO:0000250, ECO:0000269|PubMed:11842212, ECO:0000269|PubMed:15317815, ECO:0000269|PubMed:22850675}.
| null | null | null | null | null |
FUNCTION: Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Generates a biphasic current with a fast inactivating and a slow sustained phase. In sensory neurons is proposed to mediate the pain induced by acidosis that occurs in ischemic, damaged or inflamed tissue. May be involved in hyperalgesia. May play a role in mechanoreception. Heteromeric channel assembly seems to modulate channel properties. {ECO:0000269|PubMed:11120882, ECO:0000269|PubMed:11528414, ECO:0000269|PubMed:12668052, ECO:0000269|PubMed:22850675, ECO:0000269|PubMed:28396446}.
|
Rattus norvegicus (Rat)
|
O35244
|
PRDX6_RAT
|
MPGGLLLGDEAPNFEANTTIGHIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFAKRNVKLIALSIDSVEDHFAWSKDINAYNGAAPTEKLPFPIIDDKDRDLAILLGMLDPAEKDEKGMPVTARVVFIFGPDKKLKLSILYPATTGRNFDEILRVVDSLQLTASNPVATPVDWKKGESVMVLPTLPEEEAKQLFPKGVFTKELPSGKKYLRYTPQP
|
1.11.1.27; 2.3.1.23; 3.1.1.4
| null |
bleb assembly [GO:0032060]; cell redox homeostasis [GO:0045454]; cellular oxidant detoxification [GO:0098869]; cellular response to oxidative stress [GO:0034599]; glycerophospholipid catabolic process [GO:0046475]; hydrogen peroxide catabolic process [GO:0042744]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; response to oxidative stress [GO:0006979]; response to reactive oxygen species [GO:0000302]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; lysosome [GO:0005764]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
1-acylglycerophosphocholine O-acyltransferase activity [GO:0047184]; calcium-independent phospholipase A2 activity [GO:0047499]; glutathione peroxidase activity [GO:0004602]; identical protein binding [GO:0042802]; peroxidase activity [GO:0004601]; peroxiredoxin activity [GO:0051920]; phospholipase A2 activity [GO:0004623]; ubiquitin protein ligase binding [GO:0031625]
|
PF10417;PF00578;
|
3.40.30.10;
|
Peroxiredoxin family, Prx6 subfamily
|
PTM: Phosphorylation at Thr-177 by MAP kinases increases the phospholipase activity of the enzyme (PubMed:19140803). Phosphorylated form exhibits a greater lysophosphatidylcholine acyltransferase activity compared to the non-phosphorylated form (PubMed:26830860). {ECO:0000269|PubMed:19140803, ECO:0000269|PubMed:26830860}.; PTM: Irreversibly inactivated by overoxidation of Cys-47 to sulfinic acid (Cys-SO(2)H) and sulfonic acid (Cys-SO(3)H) forms upon oxidative stress. {ECO:0000250|UniProtKB:P30041}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19700648}. Lysosome {ECO:0000269|PubMed:19700648}. Note=Also found in lung secretory organelles (lamellar bodies). {ECO:0000269|PubMed:19700648}.
|
CATALYTIC ACTIVITY: Reaction=a hydroperoxide + 2 glutathione = an alcohol + glutathione disulfide + H2O; Xref=Rhea:RHEA:62632, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.27; Evidence={ECO:0000269|PubMed:15004285}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000269|PubMed:17652308, ECO:0000269|PubMed:8999971}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937, ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168, ChEBI:CHEBI:58342; EC=2.3.1.23; Evidence={ECO:0000269|PubMed:26830860}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:35983, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P30041}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35984; Evidence={ECO:0000250|UniProtKB:P30041}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P30041}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000250|UniProtKB:P30041};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for dipalmitoyl phosphatidylcholine {ECO:0000269|PubMed:8999971}; Vmax=1.89 nmol/h/mg enzyme for dipalmitoyl phosphatidylcholine {ECO:0000269|PubMed:8999971};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4 (for phospholipase activity). {ECO:0000269|PubMed:8999971};
| null |
FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (PubMed:15004285). Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (By similarity). Also has phospholipase activity, can therefore either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (PubMed:15004285, PubMed:17652308, PubMed:8999971). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (By similarity). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (By similarity). Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (PubMed:26830860). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (By similarity). {ECO:0000250|UniProtKB:P30041, ECO:0000269|PubMed:15004285, ECO:0000269|PubMed:17652308, ECO:0000269|PubMed:26830860, ECO:0000269|PubMed:8999971}.
|
Rattus norvegicus (Rat)
|
O35245
|
PKD2_MOUSE
|
MVNSRRVQPQPPGDAGRSPAPRASGPGRLVAGGAGLAVPGGLGEQRGLEIEMERIRQAAARDPPAGASASPSPPLSSCSRQAWSRDNPGFEAEEDDDDDEVEGEEGGMVVEMDVEWRPGSRRSASSSAVSSVGARGRGLGSYRGAAHLSGRRRRLEDQGAQCPSPAGGGDPLHRHLPLEGQPPRVAWAERLVRGLRGLWGTRLMEESNANREKYLKSVLRELVTYLFFLVVLCILTYGMMSSNVYYYTRTLSQLFIDTPVSKTEKTNFKTLSSMEDFWKFTEGSFLDGLYWKAQTSNHTQADNRSFIFYENLLLGVPRLRQLRVRNGSCSIPQDLRDEIKECYDVYSVSSEDRAPFGPRNGTAWMYTSEKELNGSSHWGIIASYSGAGYYLDLSRTREETAAQLAGLRRNFWLDRGTRAAFIDFSVYNANINLFCVVRLLAEFPATGGVVPSWQFQPVKLIRYVTAFDFFLAACEIIFCFFIIYYVVEEILEIRIHRLSYFRSFWNCLDVVIVVLSVVAMVINIYRMSNAEGLLQFLEDQNSFPNFEHVAYWQIQFNNISAVMVFLVWIKLFKFINFNRTMSQLSTTMSRCAKDLFGFTIMFSIIFLAYAQLAYLVFGTQVDDFSTFQECIFTQFRIILGDINFAEIEEANRVLGPLYFTTFVFFMFFILLNMFLAIINDSYSEVKSDLAQQKAEMELSDLIRKGCQKALVKLKLKRNTVDAISESLRQGGGKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEREHQQMRDDLEKEREDLDLEHSSLPRPMSSRSFPRSLDDSEEEDDEDSGHSSRRRGSISSGVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEIMERAKLKRREVLGRLLDGVAEDARLGRDSEIHREQMERLVREELERWESDDAASQTGHGVSTQVGLGGQPHPRNPRPPSSQSAEGLEGGGGNGSANVHA
| null | null |
aorta development [GO:0035904]; branching involved in ureteric bud morphogenesis [GO:0001658]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; cell-cell signaling by wnt [GO:0198738]; cellular response to calcium ion [GO:0071277]; cellular response to cAMP [GO:0071320]; cellular response to fluid shear stress [GO:0071498]; cellular response to hydrostatic pressure [GO:0071464]; cellular response to osmotic stress [GO:0071470]; cilium organization [GO:0044782]; detection of mechanical stimulus [GO:0050982]; detection of nodal flow [GO:0003127]; determination of left/right symmetry [GO:0007368]; determination of liver left/right asymmetry [GO:0071910]; embryonic placenta development [GO:0001892]; establishment of localization in cell [GO:0051649]; heart development [GO:0007507]; heart looping [GO:0001947]; intracellular calcium ion homeostasis [GO:0006874]; kidney development [GO:0001822]; liver development [GO:0001889]; mesonephric duct development [GO:0072177]; metanephric ascending thin limb development [GO:0072218]; metanephric cortex development [GO:0072214]; metanephric cortical collecting duct development [GO:0072219]; metanephric distal tubule development [GO:0072235]; metanephric mesenchyme development [GO:0072075]; metanephric part of ureteric bud development [GO:0035502]; metanephric S-shaped body morphogenesis [GO:0072284]; metanephric smooth muscle tissue development [GO:0072208]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; neural tube development [GO:0021915]; placenta blood vessel development [GO:0060674]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of gene expression [GO:0010628]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of transcription by RNA polymerase II [GO:0045944]; potassium ion transmembrane transport [GO:0071805]; protein heterotetramerization [GO:0051290]; protein homotetramerization [GO:0051289]; protein tetramerization [GO:0051262]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of calcium ion import [GO:0090279]; regulation of cell cycle [GO:0051726]; regulation of cell population proliferation [GO:0042127]; release of sequestered calcium ion into cytosol [GO:0051209]; renal artery morphogenesis [GO:0061441]; renal tubule morphogenesis [GO:0061333]; spinal cord development [GO:0021510]; Wnt signaling pathway [GO:0016055]
|
basal cortex [GO:0045180]; basolateral plasma membrane [GO:0016323]; cation channel complex [GO:0034703]; ciliary basal body [GO:0036064]; ciliary membrane [GO:0060170]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytoplasmic side of endoplasmic reticulum membrane [GO:0098554]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; lamellipodium [GO:0030027]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; membrane [GO:0016020]; migrasome [GO:0140494]; mitotic spindle [GO:0072686]; motile cilium [GO:0031514]; non-motile cilium [GO:0097730]; plasma membrane [GO:0005886]; polycystin complex [GO:0002133]
|
alpha-actinin binding [GO:0051393]; ATPase binding [GO:0051117]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-induced calcium release activity [GO:0048763]; channel activity [GO:0015267]; HLH domain binding [GO:0043398]; identical protein binding [GO:0042802]; muscle alpha-actinin binding [GO:0051371]; outward rectifier potassium channel activity [GO:0015271]; phosphoprotein binding [GO:0051219]; potassium channel activity [GO:0005267]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102]; transcription regulator inhibitor activity [GO:0140416]; transmembrane transporter binding [GO:0044325]; voltage-gated calcium channel activity [GO:0005245]; voltage-gated sodium channel activity [GO:0005248]
|
PF18109;PF08016;PF20519;
|
1.10.287.70;1.20.5.340;1.10.238.10;1.20.120.350;
|
Polycystin family
|
PTM: N-glycosylated (PubMed:11854751). The four subunits in a tetramer probably differ in the extent of glycosylation; simultaneous glycosylation of all experimentally validated sites would probably create steric hindrance (By similarity). {ECO:0000250|UniProtKB:Q13563, ECO:0000269|PubMed:11854751}.; PTM: Phosphorylated (PubMed:16551655). Phosphorylation is important for protein function; a mutant that lacks the N-terminal phosphorylation sites cannot complement a zebrafish pkd2-deficient mutant. PKD-mediated phosphorylation at the C-terminus regulates its function in the release of Ca(2+) stores from the endoplasmic reticulum. PKA-mediated phosphorylation at a C-terminal site strongly increases the open probability of the channel, but does not increase single channel conductance. {ECO:0000250|UniProtKB:Q13563, ECO:0000269|PubMed:16551655}.
|
SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:12514735, ECO:0000269|PubMed:18695040, ECO:0000269|PubMed:21307093, ECO:0000269|PubMed:22983710, ECO:0000269|PubMed:25405894, ECO:0000269|PubMed:27760766}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13563}. Cell membrane {ECO:0000269|PubMed:16551655, ECO:0000269|PubMed:27214281}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13563}. Basolateral cell membrane {ECO:0000269|PubMed:10770959, ECO:0000269|PubMed:9568711}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13563}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:10770959, ECO:0000269|PubMed:16551655, ECO:0000269|PubMed:9568711}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:11854751, ECO:0000269|PubMed:25405894, ECO:0000305|PubMed:10913159}. Golgi apparatus {ECO:0000269|PubMed:25405894}. Vesicle {ECO:0000250|UniProtKB:Q13563}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:Q13563}. Note=PKD2 localization to the plasma and ciliary membranes requires PKD1. PKD1:PKD2 interaction is required to reach the Golgi apparatus form endoplasmic reticulum and then traffic to the cilia (PubMed:25405894). Detected on kidney tubule basolateral membranes and basal cytoplasmic vesicles (PubMed:10770959, PubMed:9568711). Retained in the endoplasmic reticulum by interaction with PACS1 and PACS2. Cilium localization requires GANAB (By similarity). Detected on migrasomes and on extracellular exosomes in urine (By similarity). {ECO:0000250|UniProtKB:Q13563, ECO:0000269|PubMed:10770959, ECO:0000269|PubMed:25405894, ECO:0000269|PubMed:9568711}.
| null | null | null | null | null |
FUNCTION: Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B. Can also form a functional, homotetrameric ion channel (PubMed:27214281). Functions as a cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (PubMed:12514735, PubMed:18695040, PubMed:27760766, PubMed:31048699). Functions as outward-rectifying K(+) channel, but is also permeable to Ca(2+), and to a much lesser degree also to Na(+) (PubMed:27760766). May contribute to the release of Ca(2+) stores from the endoplasmic reticulum (By similarity). Together with TRPV4, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). PKD1 and PKD2 may function through a common signaling pathway that is necessary to maintain the normal, differentiated state of renal tubule cells (PubMed:10615132, PubMed:9568711). Acts as a regulator of cilium length, together with PKD1. The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling (PubMed:20096584). Also involved in left-right axis specification via its role in sensing nodal flow; forms a complex with PKD1L1 in cilia to facilitate flow detection in left-right patterning (PubMed:21307093, PubMed:22983710). Detection of asymmetric nodal flow gives rise to a Ca(2+) signal that is required for normal, asymmetric expression of genes involved in the specification of body left-right laterality (PubMed:12062060, PubMed:21307093, PubMed:22983710). {ECO:0000250|UniProtKB:Q13563, ECO:0000269|PubMed:12062060, ECO:0000269|PubMed:12514735, ECO:0000269|PubMed:18695040, ECO:0000269|PubMed:20096584, ECO:0000269|PubMed:21307093, ECO:0000269|PubMed:22983710, ECO:0000269|PubMed:27214281, ECO:0000269|PubMed:27760766, ECO:0000269|PubMed:31048699, ECO:0000305|PubMed:10615132, ECO:0000305|PubMed:9568711}.
|
Mus musculus (Mouse)
|
O35250
|
EXOC7_MOUSE
|
MIPPQEASARRREIEDKLKQEEETLSFIRDSLEKSDQLTRNMVSILSSFESRLMKLENSIIPVHKQTENLQRLQENVEKTLSCLDHVISYYHVASDTEKIIREGPTGRLEEYLGSMAKIQKAVEYFQDNSPDSPELNKVKLLFERGKESLESEFRSLMTRHSKVVSPVLLLDLISADDELEVQEDVVLEHLPESVLRDVVRISRWLVEYGRNQDFMNVYYQIRSSQLDRSIKGLKEHFRKSSSSSGVPYSPAIPNKRKDTPTKKPIKRPGTIRKAQNLLKQYSQHGLDGKKGGSNLIPLEGRDDMLDVETDAYIHCVSAFVKLAQSEYRLLMEIIPEHHQKKTFDSLIQDALDGLMLEGENIVSAARKAIIRHDFSTVLTVFPILRHLKQTKPEFDQVLQGTAASTKNKLPGLITSMETIGAKALEDFADNIKNDPDKEYNMPKDGTVHELTSNAILFLQQLLDFQETAGAMLASQVLGDTYNIPLDPRETSSSATSYSSEFSKRLLSTYICKVLGNLQLNLLSKSKVYEDPALSAIFLHNNYNYILKSLEKSELIQLVAVTQKTAERSYREHIEQQIQTYQRSWLKVTDYIAEKNLPVFQPGVKLRDKERQMIKERFKGFNDGLEELCKIQKVWAIPDTEQRDKIRQAQKDIVKETYGAFLHRYGSVPFTKNPEKYIKYRVEQVGDMIDRLFDTSA
| null | null |
exocytosis [GO:0006887]; membrane fission [GO:0090148]; mitotic cytokinesis [GO:0000281]; protein transmembrane transport [GO:0071806]; regulation of entry of bacterium into host cell [GO:2000535]; vesicle docking involved in exocytosis [GO:0006904]; vesicle tethering involved in exocytosis [GO:0090522]
|
centriolar satellite [GO:0034451]; cytosol [GO:0005829]; exocyst [GO:0000145]; Flemming body [GO:0090543]; growth cone membrane [GO:0032584]; plasma membrane [GO:0005886]
|
phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]
|
PF03081;PF20669;
|
1.20.1280.170;
|
EXO70 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12687004}. Cell membrane {ECO:0000269|PubMed:12687004}; Peripheral membrane protein. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q9UPT5}. Note=Translocates, as a preformed complex with SEC6 and SEC8, to the plasma membrane in response to insulin through the activation of ARHQ (PubMed:12687004). Colocalizes with CNTRL/centriolin at the midbody ring (By similarity). {ECO:0000250|UniProtKB:Q9UPT5, ECO:0000269|PubMed:12687004}.
| null | null | null | null | null |
FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. In adipocytes, plays a crucial role in targeting SLC2A4 vesicle to the plasma membrane in response to insulin, perhaps directing the vesicle to the precise site of fusion. It is required for neuron survival and plays an essential role in cortical development (By similarity). {ECO:0000250|UniProtKB:E7FC72, ECO:0000269|PubMed:12687004}.
|
Mus musculus (Mouse)
|
O35251
|
VEGFD_RAT
|
MYGEWAAVNILMMSYVYLVQGFSIEHRAVKDVSLERSSRSVLERSEQQIRAASTLEELLQVAHSEDWKLWRCRLKLKSLANVDSRSTSHRSTRFAATFYDTETLKVIDEEWQRTQCSPRETCVEVASELGKTTNTFFKPPCVNVFRCGGCCNEESVMCMNTSTSYISKQLFEISVPLTSVPELVPVKIANHTGCKCLPTGPRHPYSIIRRSIQIPEEDQCPHSKKLCPVDMLWDNTKCKCVLQDENPLPGTEDHSYLQEPALCGPHMMFDEDRCECVCKAPCPGDLIQHPENCSCFECKESLESCCQKHKMFHPDTCRSMVFSLSP
| null | null |
dopaminergic neuron differentiation [GO:0071542]; fibroblast proliferation [GO:0048144]; induction of positive chemotaxis [GO:0050930]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cell division [GO:0051781]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of mast cell chemotaxis [GO:0060754]; positive regulation of protein phosphorylation [GO:0001934]; regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030947]; response to bacterium [GO:0009617]; response to hypoxia [GO:0001666]; response to interleukin-1 [GO:0070555]; signal transduction [GO:0007165]; sprouting angiogenesis [GO:0002040]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; vascular endothelial growth factor signaling pathway [GO:0038084]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]
|
chemoattractant activity [GO:0042056]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; vascular endothelial growth factor receptor 3 binding [GO:0043185]; vascular endothelial growth factor receptor binding [GO:0005172]
|
PF03128;PF00341;
|
2.10.90.10;
|
PDGF/VEGF growth factor family
|
PTM: Undergoes a complex proteolytic maturation which generates a variety of processed secreted forms with increased activity toward VEGFR-3 and VEGFR-2. VEGF-D first form an antiparallel homodimer linked by disulfide bonds before secretion. The fully processed VEGF-D is composed mostly of two VEGF homology domains (VHDs) bound by non-covalent interactions (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Growth factor active in angiogenesis, lymphangiogenesis and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in the formation of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates VEGFR-3 (Flt4) receptor (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O35253
|
SMAD7_MOUSE
|
MFRTKRSALVRRLWRSRAPGGEDEEEGVGGGGGGGELRGEGATDGRAYGAGGGGAGRAGCCLGKAVRGAKGHHHPHPPTSGAGAAGGAEADLKALTHSVLKKLKERQLELLLQAVESRGGTRTACLLLPGRLDCRLGPGAPASAQPAQPPSSYSLPLLLCKVFRWPDLRHSSEVKRLCCCESYGKINPELVCCNPHHLSRLCELESPPPPYSRYPMDFLKPTAGCPDAVPSSAETGGTNYLAPGGLSDSQLLLEPGDRSHWCVVAYWEEKTRVGRLYCVQEPSLDIFYDLPQGNGFCLGQLNSDNKSQLVQKVRSKIGCGIQLTREVDGVWVYNRSSYPIFIKSATLDNPDSRTLLVHKVFPGFSIKAFDYEKAYSLQRPNDHEFMQQPWTGFTVQISFVKGWGQCYTRQFISSCPCWLEVIFNSR
| null | null |
adherens junction assembly [GO:0034333]; anatomical structure morphogenesis [GO:0009653]; artery morphogenesis [GO:0048844]; cell differentiation [GO:0030154]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to transforming growth factor beta stimulus [GO:0071560]; intracellular signal transduction [GO:0035556]; negative regulation of activin receptor signaling pathway [GO:0032926]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of chondrocyte proliferation [GO:1902731]; negative regulation of ossification [GO:0030279]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of SMAD protein signal transduction [GO:0060392]; negative regulation of T cell cytokine production [GO:0002725]; negative regulation of T-helper 17 cell differentiation [GO:2000320]; negative regulation of T-helper 17 type immune response [GO:2000317]; negative regulation of transcription by competitive promoter binding [GO:0010944]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of cell-cell adhesion [GO:0022409]; positive regulation of chondrocyte hypertrophy [GO:1903043]; protein stabilization [GO:0050821]; protein-containing complex localization [GO:0031503]; regulation of cardiac muscle contraction [GO:0055117]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; regulation of ventricular cardiac muscle cell membrane depolarization [GO:0060373]; response to laminar fluid shear stress [GO:0034616]; SMAD protein signal transduction [GO:0060395]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ureteric bud development [GO:0001657]; ventricular cardiac muscle tissue morphogenesis [GO:0055010]; ventricular septum morphogenesis [GO:0060412]
|
adherens junction [GO:0005912]; centrosome [GO:0005813]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; heteromeric SMAD protein complex [GO:0071144]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
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activin receptor binding [GO:0070697]; beta-catenin binding [GO:0008013]; collagen binding [GO:0005518]; I-SMAD binding [GO:0070411]; metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714]; transcription regulator inhibitor activity [GO:0140416]; type I transforming growth factor beta receptor binding [GO:0034713]; ubiquitin ligase-substrate adaptor activity [GO:1990756]; ubiquitin protein ligase binding [GO:0031625]
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PF03165;PF03166;
|
2.60.200.10;3.90.520.10;
|
Dwarfin/SMAD family
|
PTM: Phosphorylation on Ser-249 does not affect its stability, nuclear localization or inhibitory function in TGFB signaling; however it affects its ability to regulate transcription (PubMed:11278814). Phosphorylated by PDPK1 (By similarity). {ECO:0000250|UniProtKB:O15105, ECO:0000269|PubMed:11278814}.; PTM: Ubiquitinated by WWP1 (PubMed:15221015). Polyubiquitinated by RNF111, which is enhanced by AXIN1 and promotes proteasomal degradation (PubMed:14657019). In response to TGF-beta, ubiquitinated by SMURF1; which promotes its degradation (By similarity). Ubiquitinated by ARK2C, promoting proteasomal degradation, leading to enhance the BMP-Smad signaling (PubMed:23610558). {ECO:0000250|UniProtKB:O15105, ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:15221015, ECO:0000269|PubMed:23610558}.; PTM: Acetylation prevents ubiquitination and degradation mediated by SMURF1. {ECO:0000250|UniProtKB:O15105}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11278814, ECO:0000269|PubMed:15496141}. Cytoplasm {ECO:0000269|PubMed:11278814, ECO:0000269|PubMed:15496141}. Note=Interaction with NEDD4L or RNF111 induces translocation from the nucleus to the cytoplasm (PubMed:15496141). TGF-beta stimulates its translocation from the nucleus to the cytoplasm. PDPK1 inhibits its translocation from the nucleus to the cytoplasm in response to TGF-beta (By similarity). {ECO:0000250|UniProtKB:O15105, ECO:0000269|PubMed:15496141}.
| null | null | null | null | null |
FUNCTION: Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access. Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. {ECO:0000250|UniProtKB:O15105}.
|
Mus musculus (Mouse)
|
O35254
|
GORS1_RAT
|
MGLGASSEQPAGGEGFHLHGVQENSPAQQAGLEPYFDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEHVWHVLDVEPSSPAALAGLRPYTDYIVGSDQILQESEDFFTLIESHEGKPLKLMVYNSESDSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQPSSQYKKPPSASSPGTPAKTPQPNAFPLGAPPPWPIPQDSSGPELGSRQSDYMEALPQVPGGFMEEQLPGPGSPGHGTADYGGCLHSMEIPLQPPPPVQRVMDPGFLDVSGMSLLDSNNTSVCPSLSSSSLLTPTAVSALGPEDIGSSSSSHERGGEATWSGSEFEISFPDSPGSQAQVDHLPRLTLPDGLTSAASPEEGLSAELLEAQTEEPAHTASLDCMAQTEGPAGQVQAAPDPEPGLCEGPW
| null | null |
establishment of protein localization to plasma membrane [GO:0061951]; Golgi organization [GO:0007030]; Golgi ribbon formation [GO:0090161]; negative regulation of dendrite morphogenesis [GO:0050774]; protein N-linked glycosylation [GO:0006487]; protein transport [GO:0015031]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
metal ion binding [GO:0046872]
|
PF04495;
|
2.30.42.10;
|
GORASP family
|
PTM: Phosphorylated by CDC2/B1 and PLK kinases during mitosis. Phosphorylation cycle correlates with the cisternal stacking cycle. Phosphorylation of the homodimer prevents the association of dimers into higher-order oligomers, leading to cisternal unstacking. {ECO:0000269|PubMed:11050165, ECO:0000269|PubMed:12839990, ECO:0000269|PubMed:9346242}.; PTM: Target for caspase-3 cleavage during apoptosis. The cleavage contributes to Golgi fragmentation and occurs very early in the execution phase of apoptosis. {ECO:0000269|PubMed:11815631}.; PTM: Myristoylated. {ECO:0000269|PubMed:9346242}.
|
SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:11706049, ECO:0000269|PubMed:11739401, ECO:0000269|PubMed:12015985, ECO:0000269|PubMed:12839990, ECO:0000269|PubMed:9346242}; Peripheral membrane protein {ECO:0000269|PubMed:9346242}; Cytoplasmic side {ECO:0000269|PubMed:9346242}.
| null | null | null | null | null |
FUNCTION: Key structural protein of the Golgi apparatus (By similarity). The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon (By similarity). Acting in concert with GORASP2/GRASP55, is required for the formation and maintenance of the Golgi ribbon, and may be dispensable for the formation of stacks (By similarity). However, other studies suggest that GORASP1 plays an important role in assembly and membrane stacking of the cisternae, and in the reassembly of Golgi stacks after breakdown during mitosis (PubMed:12839990, PubMed:23940043, PubMed:9346242). Caspase-mediated cleavage of GORASP1 is required for fragmentation of the Golgi during apoptosis (PubMed:11815631, PubMed:12015985). Also mediates, via its interaction with GOLGA2/GM130, the docking of transport vesicles with the Golgi membranes (By similarity). Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (By similarity). {ECO:0000250|UniProtKB:Q91X51, ECO:0000250|UniProtKB:Q9BQQ3, ECO:0000269|PubMed:11815631, ECO:0000269|PubMed:12015985, ECO:0000269|PubMed:12839990, ECO:0000269|PubMed:23940043, ECO:0000269|PubMed:9346242}.
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Rattus norvegicus (Rat)
|
O35260
|
NACC1_RAT
|
MAQTLQMEIPNFGNSILECLNEQRLQGLYCDVSVVVKGHAFKAHRAVLAASSSYFRDLFNSSRSAVVELPAAVQPQSFQQILTFCYTGRLSMNMGDQFLLIYTAGFLQIQEIMEKGTEFFLKVSSPSCDSQGLHPEEAPSSEPQSPVAQILGWPACSTPLPLVSRVKTEQELDSVQCTPMAKRLWDSSQKEAGGSGGNNGSRKMAKFSTPDLAPNRMPQPVSVATATAAVAVVAVGGCVSGPSMSERTSPGTSSAYTSDSPSSYHNEEDEEEDAGEEGTDEQYRQICNMYTMYSMLNVGQTVEKVEALPEQVVLESHSRIRVRQDLASLPAELINQIGNRCHPKLYDEGDPSEKLELVTGTNVYITRAQLMNCHVSAGTRHKVLLRRLLASFFDRNTLANSCGTGIRSSTNDPRRKPLDSRVLHAVKYYCQNFAPNFKESEMNAIAADMCTNARRVVRKSWLPKTKPLHLVEGDNYSSFISDTGKIEPDMMSMEHSFETASHDGEAGPSAEVLQ
| null | null |
negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of cell population proliferation [GO:0008284]; regulation of transcription by RNA polymerase II [GO:0006357]
|
cell junction [GO:0030054]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF10523;PF00651;
|
1.10.10.2590;
| null |
PTM: Phosphorylated by protein kinase C (PKC). {ECO:0000269|PubMed:16045493}.
|
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Punctate distribution in nucleus. In differentiated PC12 cells diffusely distributed in the cytoplasm and is dependent on phosphorylation.
| null | null | null | null | null |
FUNCTION: Functions as a transcriptional repressor. Isoform 1 is a stronger transcriptional repressor than isoform 2. Seems to function as a transcriptional corepressor in neuronal cells through recruitment of HDAC3 and HDAC4. Contributes to tumor progression, and tumor cell proliferation and survival. This may be mediated at least in part through repressing transcriptional activity of GADD45GIP1. Required for recruiting the proteasome from the nucleus to the cytoplasm and dendritic spines. {ECO:0000269|PubMed:11906783, ECO:0000269|PubMed:16033423, ECO:0000269|PubMed:17254023, ECO:0000269|PubMed:17699672}.
|
Rattus norvegicus (Rat)
|
O35261
|
E2F3_MOUSE
|
MRKGIQPALEQYLVTAGGGEGAAVVAAAAAASMDKRALLASPGFAAAAAPGTYIQILTTNPSTTSCATSLQSGALTAGPLLPSVPGTEPAASSLYTTPQGPSSRVGLLQQPPAPGRGGGGGPPAKRRLELGESGHQYLSDGLKTPKGKGRAALRSPDSPKTPKSPSEKTRYDTSLGLLTKKFIQLLSQSPDGVLDLNKAAEVLKVQKRRIYDITNVLEGIHLIKKKSKNNVQWMGCSLSEDGGMLAQCQGLSKEVTELSQEEKKLDELIQSCTLDLKLLTEDSENQRLAYVTYQDIRKISGLKDQTVIVVKAPPETRLEVPDSIESLQIHLASTQGPIEVYLCPEETETHRPMKTNNQDHNGNIPKPTSKDLASNNSGHSDCSVSTANLSPLASPANLLQQTEDQIPSNLEGPFVNLLPPLLQEDYLLSLGEEEGISDLFDAYDLEKLPLVEDFMCS
| null | null |
G1/S transition of mitotic cell cycle [GO:0000082]; negative regulation of fat cell proliferation [GO:0070345]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of vascular associated smooth muscle cell apoptotic process [GO:1905461]; protein import into nucleus [GO:0006606]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]
|
RNA polymerase II transcription regulator complex [GO:0090575]
|
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]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF16421;PF02319;
|
6.10.250.540;1.10.10.10;
|
E2F/DP family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F3 binds specifically to RB1 in a cell-cycle dependent manner. Inhibits adipogenesis, probably through the repression of CEBPA binding to its target gene promoters (PubMed:20176812). {ECO:0000269|PubMed:20176812}.
|
Mus musculus (Mouse)
|
O35263
|
PA1B3_RAT
|
MSGEGENPASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQCEIWRELFSPLHALNFGIGGDSTQHVLWRLENGELEHIRPKIVVVWVGTNNHSHTAEQVTGGIKAIVQLVNKLQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAALAGYPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVCRALHSLLLRLLAQDQGQGIPLPETAP
|
3.1.1.47
| null |
lipid catabolic process [GO:0016042]; spermatogenesis [GO:0007283]
|
1-alkyl-2-acetylglycerophosphocholine esterase complex [GO:0008247]; cytoplasm [GO:0005737]
|
1-alkyl-2-acetylglycerophosphocholine esterase activity [GO:0003847]; identical protein binding [GO:0042802]; platelet-activating factor acetyltransferase activity [GO:0047179]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]
|
PF13472;
|
3.40.50.1110;
|
'GDSL' lipolytic enzyme family, Platelet-activating factor acetylhydrolase IB beta/gamma subunits subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47; Evidence={ECO:0000269|PubMed:9660828}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778; Evidence={ECO:0000305|PubMed:9660828}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496; Evidence={ECO:0000269|PubMed:9660828}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480; Evidence={ECO:0000305|PubMed:9660828}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphate + H2O = 1-O-hexadecyl-sn-glycero-3-phosphate + acetate + H(+); Xref=Rhea:RHEA:41704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:77580, ChEBI:CHEBI:78385; Evidence={ECO:0000250|UniProtKB:Q29460}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41705; Evidence={ECO:0000250|UniProtKB:Q29460};
| null | null | null | null |
FUNCTION: Alpha1 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF (PubMed:9660828). The activity and substrate specificity of PAF-AH (I) are affected by its subunit composition. Both alpha1/alpha1 homodimer (PAFAH1B3/PAFAH1B3 homodimer) and alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B2 heterodimer) hydrolyze 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA) more efficiently than PAF, but they have little hydrolytic activity towards 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE). Plays an important role during the development of brain (By similarity). {ECO:0000250|UniProtKB:Q29460, ECO:0000269|PubMed:9660828}.
|
Rattus norvegicus (Rat)
|
O35264
|
PA1B2_RAT
|
MSQGDSNPAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQYEIWRELFSPLHALNFGIGGDTTRHVLWRLKNGELENIKPKVIVVWVGTNNHENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDIDGGFVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLLEETPEEKQTTIA
|
3.1.1.47
| null |
lipid catabolic process [GO:0016042]; positive regulation of macroautophagy [GO:0016239]; spermatogenesis [GO:0007283]
|
1-alkyl-2-acetylglycerophosphocholine esterase complex [GO:0008247]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; plasma membrane [GO:0005886]
|
1-alkyl-2-acetylglycerophosphocholine esterase activity [GO:0003847]; identical protein binding [GO:0042802]; platelet-activating factor acetyltransferase activity [GO:0047179]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]
|
PF13472;
|
3.40.50.1110;
|
'GDSL' lipolytic enzyme family, Platelet-activating factor acetylhydrolase IB beta/gamma subunits subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47; Evidence={ECO:0000269|PubMed:9660828}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778; Evidence={ECO:0000305|PubMed:9660828}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496; Evidence={ECO:0000269|PubMed:9660828}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480; Evidence={ECO:0000305|PubMed:9660828}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphate + H2O = 1-O-hexadecyl-sn-glycero-3-phosphate + acetate + H(+); Xref=Rhea:RHEA:41704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:77580, ChEBI:CHEBI:78385; Evidence={ECO:0000250|UniProtKB:P68401}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41705; Evidence={ECO:0000250|UniProtKB:P68401}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphoethanolamine + H2O = 1-O-hexadecyl-sn-glycero-3-phosphoethanolamine + acetate + H(+); Xref=Rhea:RHEA:41708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:78387, ChEBI:CHEBI:78390; Evidence={ECO:0000250|UniProtKB:P68401}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41709; Evidence={ECO:0000250|UniProtKB:P68401};
| null | null | null | null |
FUNCTION: Alpha2 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF (PubMed:9660828). The activity and substrate specificity of PAF-AH (I) are affected by its subunit composition. The alpha2/alpha2 homodimer (PAFAH1B2/PAFAH1B2 homodimer) hydrolyzes PAF and 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE) more efficiently than 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA). In contrast, the alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B3 heterodimer) hydrolyzes AAGPA more efficiently than PAF, but has little hydrolytic activity towards AAGPE (By similarity). May play a role in male germ cell meiosis during the late pachytenestage and meiotic divisions as well as early spermiogenesis (By similarity). {ECO:0000250|UniProtKB:P68401, ECO:0000250|UniProtKB:Q61206, ECO:0000269|PubMed:9660828}.
|
Rattus norvegicus (Rat)
|
O35274
|
NEB2_RAT
|
MMKTEPRGPGGPLRSASPHRSAYEAGIQALKPPDAPGPDEAPKAAHHKKYGSNVHRIKSMFLQMGTTTGPPGEAGGASGMAEAPRASDRGVRLSLPRASSLNENVDHSALLKLGTSVSERVSRFDSKPAPSAQPAPPPHPPSRLQETRKLFERSVPAASGGDKEAVARRLLRQERASLQDRKLDVVVRFNGSTEALDKLDADAVSPTVSQLSAVFEKADSRTGLHRAPGPPRAAGAPQVNSKLVTKRSRVFQPPPPPPAPSGDAATEKDRGPGGQQPPQHRVAPARPPPKPREVRKIKPVEVEESGESEAESAPGEVIQAEVTVHAALENGSTTATTASPAPEEPKAEAVPEEEASSSVATLERGVDNGRAPDMAPEEVDESKKEDFSEADLVDVSAYSGLGEDSGGSALEEDDEEDEEDGEPPYEPESGCVEIPGLSEEEDPAPSRKIHFSTAPIQVFSTYSNEDYDRRNEDVDPMAASAEYELEKRVERLELFPVELEKDSEGLGISIIGMGAGADMGLEKLGIFVKTVTEGGAAHRDGRIQVNDLLVEVDGTSLVGVTQSFAASVLRNTKGRVRFMIGRERPGEQSEVAQLIQQTLEQERWQREMMEQRYAQYGEDDEETGEYATDEDEELSPTFPGGEMAIEVFELAENEDALSPVEMEPEKLVHKFKELQIKHAVTEAEIQQLKRKLQSLEQEKGRWRVEKAQLEQSVEENKERMEKLEGYWGEAQSLCQAVDEHLRETQAQYQALERKYSKAKRLIKDYQQKEIEFLKKETAQRRVLEESELARKEEMDKLLDKISELEGNLQTLRNSNST
| null | null |
actin filament depolymerization [GO:0030042]; actin filament organization [GO:0007015]; calcium-mediated signaling [GO:0019722]; cell migration [GO:0016477]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to estradiol stimulus [GO:0071392]; cellular response to morphine [GO:0071315]; cellular response to organic cyclic compound [GO:0071407]; cellular response to peptide [GO:1901653]; cellular response to xenobiotic stimulus [GO:0071466]; cerebral cortex development [GO:0021987]; dendrite development [GO:0016358]; developmental process involved in reproduction [GO:0003006]; filopodium assembly [GO:0046847]; hippocampus development [GO:0021766]; learning [GO:0007612]; male mating behavior [GO:0060179]; negative regulation of cell growth [GO:0030308]; neuron projection development [GO:0031175]; positive regulation of protein localization [GO:1903829]; positive regulation of protein localization to actin cortical patch [GO:1904372]; positive regulation of protein localization to plasma membrane [GO:1903078]; protein localization to actin cytoskeleton [GO:1903119]; protein localization to cell periphery [GO:1990778]; regulation of opioid receptor signaling pathway [GO:2000474]; regulation of protein phosphorylation [GO:0001932]; reproductive system development [GO:0061458]; response to amino acid [GO:0043200]; response to amphetamine [GO:0001975]; response to estradiol [GO:0032355]; response to immobilization stress [GO:0035902]; response to kainic acid [GO:1904373]; response to L-phenylalanine derivative [GO:1904386]; response to nicotine [GO:0035094]; response to organic cyclic compound [GO:0014070]; response to organonitrogen compound [GO:0010243]; response to prostaglandin E [GO:0034695]; response to steroid hormone [GO:0048545]; response to xenobiotic stimulus [GO:0009410]
|
actin cytoskeleton [GO:0015629]; adherens junction [GO:0005912]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytoplasmic side of dendritic spine plasma membrane [GO:1990780]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; dendritic spine head [GO:0044327]; dendritic spine membrane [GO:0032591]; dendritic spine neck [GO:0044326]; filopodium [GO:0030175]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; ruffle membrane [GO:0032587]
|
actin binding [GO:0003779]; actin filament binding [GO:0051015]; D2 dopamine receptor binding [GO:0031749]; kinase binding [GO:0019900]; nucleic acid binding [GO:0003676]; protein kinase activity [GO:0004672]; protein phosphatase 1 binding [GO:0008157]; protein phosphatase inhibitor activity [GO:0004864]; protein-containing complex binding [GO:0044877]; transmembrane transporter binding [GO:0044325]
|
PF00595;PF17817;
|
2.30.42.10;
| null |
PTM: Stimulation of D1 (but not D2) dopamine receptors induces Ser-94 and Ser-177 phosphorylation. Dephosphorylation of these residues is mediated by PP1 and possibly PP2A. Spinophilin unphosphorylated or phosphorylated at Ser-94 is concentrated in the postsynaptic density, whereas spinophilin phosphorylated at Ser-177 is absent from the postsynaptic density and enriched in the cytosol. Phosphorylation of spinophilin disrupts its association with F-actin, but does not affect its binding to PP1. {ECO:0000269|PubMed:12417592, ECO:0000269|PubMed:15228588}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus {ECO:0000250}. Postsynaptic density {ECO:0000269|PubMed:15514983}. Cell junction, adherens junction. Cell projection, dendritic spine {ECO:0000269|PubMed:15514983}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}. Note=Enriched at synapse and cadherin-based cell-cell adhesion sites. In neurons, both cytosolic and membrane-associated, and highly enriched in the postsynaptic density apposed to exitatory synapses (PubMed:15514983). Colocalizes with PPP1R2 at actin-rich adherens junctions in epithelial cells and in dendritic spines. Accumulates in the lamellipodium, filopodium and ruffle membrane in response to hepatocyte growth factor (HGF) treatment (By similarity). {ECO:0000250, ECO:0000269|PubMed:15514983}.
| null | null | null | null | null |
FUNCTION: Seems to act as a scaffold protein in multiple signaling pathways. Modulates excitatory synaptic transmission and dendritic spine morphology. Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May play an important role in linking the actin cytoskeleton to the plasma membrane at the synaptic junction. Believed to target protein phosphatase 1/PP1 to dendritic spines, which are rich in F-actin, and regulates its specificity toward ion channels and other substrates, such as AMPA-type and NMDA-type glutamate receptors. Plays a role in regulation of G-protein coupled receptor signaling, including dopamine D2 receptors and alpha-adrenergic receptors. May establish a signaling complex for dopaminergic neurotransmission through D2 receptors by linking receptors downstream signaling molecules and the actin cytoskeleton. Binds to ADRA1B and RGS2 and mediates regulation of ADRA1B signaling. May confer to Rac signaling specificity by binding to both, RacGEFs and Rac effector proteins. Probably regulates p70 S6 kinase activity by forming a complex with TIAM1. Required for hepatocyte growth factor (HGF)-induced cell migration (By similarity). {ECO:0000250, ECO:0000269|PubMed:15743906, ECO:0000269|PubMed:15793568}.
|
Rattus norvegicus (Rat)
|
O35276
|
NRP2_RAT
|
MDMFPLTWIFLALYFSGHKVRSQQDPPCGGRLNSKDAGYITSPGYPQDYPSHQNCEWVVYAPEPNQKIVLNFNPHFEIEKHDCKYDFIEIRDGDSESADLLGKHCGNIAPPTIISSGSVLYIKFTSDYARQGAGFSLRYEIFKTGSEDCSKNFTSPNGTIESPGFPEKYPHNLDCTFTILAKPRMEIILQFLTFDLEHDPLQVGEGDCKYDWLDIWDGIPHVGPLIGKYCGTKTPSKLRSSTGILSLTFHTDMAVAKDGFSARYYLVHQEPPENFQCNAPLGMESGRIANEQISASSTFSDGRWTPQQSRLHGDDNGWTPNVDSNKEYLQVDLRFLTMLTAIATQGAISRETQKGYYVKSYKLEVSTNGEDWMVYRHGKNHKVFQANNDATELVLNKLHTPLLTRFIRIRPQTWHLGIALRLELFGCRVTDAPCSNMLGMLSGLIADTQISASSTREYLWSPSAARLVSSRSGWFPRNPQAQPGEEWLQVDLGTPKTVKGVIIQGARGGDSITAMEARAFVRKFKVSYSLNGKDWEYIQDPRTQQPKLFEGNMHYDTPDIRRFEPVPAQYVRVYPERWSPAGIGMRLEVLGCDWTDSKPTVETLGPTVKSEETTTPYPMDEDATECGENCSFEDDKDLQLPSGFNCNFDFPEETCGWMYDRAKWLQSTWISSANPNDRTFPDDKNFLKLQSDGGREGQFGRLISPPVHLPRSPVCMEFQYQAMGGHGVALQVVREARQESKLLWVIREDQGSEWKHGRIILPSYDMEYQIVFEGVIGKGRSGEISIDDIRISTDVPLENCMEPISAFAVDIPEIHGGEGYEDEIDDDYEGDWNNSSSTSGAGSPSSGKEKSWLYTLDPILITIIAMSSLGVLLGATCAGLLLYCTCSYSGLSSRSCTTLENYNFELYDGLKHKVKINHQKCCSEA
| null | null |
angiogenesis [GO:0001525]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; cellular response to leukemia inhibitory factor [GO:1990830]; dorsal root ganglion morphogenesis [GO:1904835]; facial nerve structural organization [GO:0021612]; facioacoustic ganglion development [GO:1903375]; gonadotrophin-releasing hormone neuronal migration to the hypothalamus [GO:0021828]; heart development [GO:0007507]; negative chemotaxis [GO:0050919]; nerve development [GO:0021675]; neural crest cell migration involved in autonomic nervous system development [GO:1901166]; neuron migration [GO:0001764]; outflow tract septum morphogenesis [GO:0003148]; regulation of postsynapse organization [GO:0099175]; semaphorin-plexin signaling pathway [GO:0071526]; sensory neuron axon guidance [GO:0097374]; sympathetic ganglion development [GO:0061549]; sympathetic neuron projection extension [GO:0097490]; sympathetic neuron projection guidance [GO:0097491]; trigeminal ganglion development [GO:0061551]; trunk neural crest cell migration [GO:0036484]; ventral trunk neural crest cell migration [GO:0036486]; vestibulocochlear nerve structural organization [GO:0021649]
|
axon [GO:0030424]; glutamatergic synapse [GO:0098978]; postsynaptic membrane [GO:0045211]
|
heparin binding [GO:0008201]; metal ion binding [GO:0046872]; semaphorin receptor activity [GO:0017154]; vascular endothelial growth factor receptor activity [GO:0005021]
|
PF00431;PF11980;PF00754;PF00629;
|
2.60.120.200;2.60.120.260;2.60.120.290;
|
Neuropilin family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O60462}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O60462}.
| null | null | null | null | null |
FUNCTION: High affinity receptor for semaphorins 3C, 3F, VEGF-165 and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF.
|
Rattus norvegicus (Rat)
|
O35280
|
CHK1_MOUSE
|
MAVPFVEDWDLVQTLGEGAYGEVQLAVNRITEEAVAVKIVDMKRAIDCPENIKKEICINKMLSHENVVKFYGHRREGHIQYLFLEYCSGGELFDRIEPDIGMPEQDAQRFFHQLMAGVVYLHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRHNNRERLLNKMCGTLPYVAPELLKRKEFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLALLHKILVETPSARITIPDIKKDRWYNKPLNRGAKRPRATSGGMSESSSGFSKHIHSNLDFSPVNNGSSEETVKFSSSQPEPRTGLSLWDTGPSNVDKLVQGISFSQPTCPEHMLVNSQLLGTPGSSQNPWQRLVKRMTRFFTKLDADKSYQCLKETFEKLGYQWKKSCMNQVTVSTTDRRNNKLIFKINLVEMDEKILVDFRLSKGDGLEFKRHFLKIKGKLSDVVSSQKVWFPVT
|
2.7.11.1
| null |
apoptotic process involved in development [GO:1902742]; cellular response to caffeine [GO:0071313]; cellular response to mechanical stimulus [GO:0071260]; chromatin remodeling [GO:0006338]; DNA damage checkpoint signaling [GO:0000077]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; G2/M transition of mitotic cell cycle [GO:0000086]; inner cell mass cell proliferation [GO:0001833]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; mitotic G2/M transition checkpoint [GO:0044818]; negative regulation of DNA biosynthetic process [GO:2000279]; negative regulation of G2/M transition of mitotic cell cycle [GO:0010972]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of mitotic nuclear division [GO:0045839]; nucleus organization [GO:0006997]; peptidyl-threonine phosphorylation [GO:0018107]; positive regulation of cell cycle [GO:0045787]; regulation of cell population proliferation [GO:0042127]; regulation of double-strand break repair via homologous recombination [GO:0010569]; regulation of gene expression [GO:0010468]; regulation of mitotic centrosome separation [GO:0046602]; signal transduction in response to DNA damage [GO:0042770]
|
centrosome [GO:0005813]; chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; replication fork [GO:0005657]
|
ATP binding [GO:0005524]; histone H3T11 kinase activity [GO:0035402]; protein domain specific binding [GO:0019904]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
3.30.310.80;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, NIM1 subfamily
|
PTM: Phosphorylated by ATR in a RAD17-dependent manner in response to ultraviolet irradiation and inhibition of DNA replication. Phosphorylated by ATM in response to ionizing irradiation. ATM and ATR can both phosphorylate Ser-317 and Ser-345 and this results in enhanced kinase activity. Phosphorylation at Ser-345 induces a change in the conformation of the protein, activates the kinase activity and is a prerequisite for interaction with FBXO6 and subsequent ubiquitination at Lys-436. Phosphorylation at Ser-345 also increases binding to 14-3-3 proteins and promotes nuclear retention. Conversely, dephosphorylation at Ser-345 by PPM1D may contribute to exit from checkpoint mediated cell cycle arrest. Phosphorylation at Ser-280 by AKT1/PKB, may promote mono and/or diubiquitination. Also phosphorylated at undefined residues during mitotic arrest, resulting in decreased activity. {ECO:0000269|PubMed:15710331, ECO:0000269|PubMed:17376776}.; PTM: Ubiquitinated (PubMed:15710331). Mono or diubiquitination promotes nuclear exclusion (PubMed:15710331). The activated form (phosphorylated on Ser-345) is polyubiquitinated at Lys-436 by some SCF-type E3 ubiquitin ligase complex containing FBXO6 promoting its degradation (By similarity). Ubiquitination and degradation are required to terminate the checkpoint and ensure that activated CHEK1 does not accumulate as cells progress through S phase, when replication forks encounter transient impediments during normal DNA replication. 'Lys-63'-mediated ubiquitination by TRAF4 at Lys-132 activates cell cycle arrest and activation of DNA repair (By similarity). {ECO:0000250|UniProtKB:O14757, ECO:0000269|PubMed:15710331}.; PTM: Proteolytically cleaved at the C-terminus by SPRTN during normal DNA replication, thereby promoting CHEK1 removal from chromatin and activating the protein kinase activity. {ECO:0000250|UniProtKB:O14757}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15710331, ECO:0000269|PubMed:9382850}. Chromosome {ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:9382850}. Cytoplasm {ECO:0000250|UniProtKB:O14757}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O14757}. Note=Nuclear export is mediated at least in part by XPO1/CRM1. Also localizes to the centrosome specifically during interphase, where it may protect centrosomal CDC2 kinase from inappropriate activation by cytoplasmic CDC25B. Proteolytic cleavage at the C-terminus by SPRTN promotes removal from chromatin. {ECO:0000250|UniProtKB:O14757}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:18243098}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:18243098};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA (PubMed:10859163, PubMed:10859164, PubMed:15261141). May also negatively regulate cell cycle progression during unperturbed cell cycles (PubMed:10859163, PubMed:10859164, PubMed:15261141). This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome (PubMed:10859163, PubMed:10859164, PubMed:15261141). Recognizes the substrate consensus sequence [R-X-X-S/T] (PubMed:10859163, PubMed:10859164, PubMed:15261141). Binds to and phosphorylates CDC25A, CDC25B and CDC25C. Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C. Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A. Phosphorylation of CDC25A at 'Ser-76' primes the protein for subsequent phosphorylation at 'Ser-79', 'Ser-82' and 'Ser-88' by NEK11, which is required for polyubiquitination and degradation of CDCD25A. Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. Also phosphorylates NEK6. Binds to and phosphorylates RAD51 at 'Thr-309', which promotes the release of RAD51 from BRCA2 and enhances the association of RAD51 with chromatin, thereby promoting DNA repair by homologous recombination. Phosphorylates multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and promotes cell cycle arrest and suppression of cellular proliferation. Also promotes repair of DNA cross-links through phosphorylation of FANCE. Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A. This may enhance chromatin assembly both in the presence or absence of DNA damage. May also play a role in replication fork maintenance through regulation of PCNA (By similarity). May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones. Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes (PubMed:18243098). May also phosphorylate RB1 to promote its interaction with the E2F family of transcription factors and subsequent cell cycle arrest. Phosphorylates SPRTN, promoting SPRTN recruitment to chromatin (By similarity). Reduces replication stress and activates the G2/M checkpoint, by phosphorylating and inactivating PABIR1/FAM122A and promoting the serine/threonine-protein phosphatase 2A-mediated dephosphorylation and stabilization of WEE1 levels and activity (By similarity). {ECO:0000250|UniProtKB:O14757, ECO:0000269|PubMed:10859163, ECO:0000269|PubMed:10859164, ECO:0000269|PubMed:15261141, ECO:0000269|PubMed:18243098}.
|
Mus musculus (Mouse)
|
O35284
|
BATF_MOUSE
|
MPHSSDSSDSSFSRSPPPGKQDSSDDVRKVQRREKNRIAAQKSRQRQTQKADTLHLESEDLEKQNAALRKEIKQLTEELKYFTSVLSSHEPLCSVLASGTPSPPEVVYSAHAFHQPHISSPRFQP
| null | null |
defense response to protozoan [GO:0042832]; DNA damage response [GO:0006974]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; hematopoietic stem cell differentiation [GO:0060218]; isotype switching [GO:0045190]; lymphoid progenitor cell differentiation [GO:0002320]; myeloid dendritic cell differentiation [GO:0043011]; positive regulation of cytokine production [GO:0001819]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; T-helper 17 cell differentiation [GO:0072539]; T-helper 17 cell lineage commitment [GO:0072540]; T-helper 2 cell differentiation [GO:0045064]
|
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
|
PF00170;
|
1.20.5.170;
|
BZIP family
|
PTM: Phosphorylated on serine and threonine residues and at least one tyrosine residue. Phosphorylation at Ser-43 inhibit DNA binding activity and transforms it as a negative regulator of AP-1 mediated transcription. {ECO:0000269|PubMed:12809553}.
|
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Present in the nucleus and cytoplasm, but shows increased nuclear translocation after activation of T-cells.
| null | null | null | null | null |
FUNCTION: AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells and class-switch recombination (CSR) in B-cells. Acts via the formation of a heterodimer with JUNB that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4 (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 (or IRF8) and activation of genes. Controls differentiation of T-helper cells producing interleukin-17 (Th17 cells) by binding to Th17-associated gene promoters: regulates expression of the transcription factor RORC itself and RORC target genes such as IL17 (IL17A or IL17B). Also involved in differentiation of follicular T-helper cells (TfH) by directing expression of BCL6 and MAF. In B-cells, involved in class-switch recombination (CSR) by controlling the expression of both AICDA and of germline transcripts of the intervening heavy-chain region and constant heavy-chain region (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic cell differentiation via interaction with IRF4 and IRF8 to mediate cooperative gene activation. Regulates effector CD8(+) T-cell differentiation by regulating expression of SIRT1. Following DNA damage, part of a differentiation checkpoint that limits self-renewal of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to differentiation of HSCs, thereby restricting self-renewal of HSCs. {ECO:0000269|PubMed:11466704, ECO:0000269|PubMed:12594265, ECO:0000269|PubMed:19578362, ECO:0000269|PubMed:20421391, ECO:0000269|PubMed:21572431, ECO:0000269|PubMed:22001828, ECO:0000269|PubMed:22385964, ECO:0000269|PubMed:22983707, ECO:0000269|PubMed:22992523, ECO:0000269|PubMed:22992524, ECO:0000269|PubMed:23021777}.
|
Mus musculus (Mouse)
|
O35286
|
DHX15_MOUSE
|
MSKRHRLDLGEDYPSGKKRAGTDGKDRERDRDREDRSKDRDRERDRGDREREREKEKEKELRASTNAMLISAGLPPLKASHSAHSTHSAHSTHSTHSAHSTHTGHTGHTSLPQCINPFTNLPHTPRYYDILKKRLQLPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPKRGVACTQPRRVAAMSVAQRVADEMDVMLGQEVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATLDAGKFQIYFDNCPLLTIPGRTHPVEIFYTPEPERDYLEAAIRTVIQIHMCEEEEGDLLLFLTGQEEIDEACKRIKREVDDLGPEVGDIKIIPLYSTLPPQQQQRIFEPPPPKKQNGAIGRKVVVSTNIAETSLTIDGVVFVIDPGFAKQKVYNPRIRVESLLVTAISKASAQQRAGRAGRTRPGKCFRLYTEKAYKTEMQDNTYPEILRSNLGSVVLQLKKLGIDDLVHFDFMDPPAPETLMRALELLNYLAALNDDGDLTELGSMMAEFPLDPQLAKMVIASCDYNCSNEVLSITAMLSVPQCFVRPTEAKKAADEAKMRFAHIDGDHLTLLNVYHAFKQNHESVQWCYDNFINYRSLMSADNVRQQLSRIMDRFNLPRRSTDFTSRDYYINIRKALVTGYFMQVAHLERTGHYLTVKDNQVVQLHPSTVLDHKPEWVLYNEFVLTTKNYIRTCTDIKPEWLVKIAPQYYDMSNFPQCEAKRQLDRIIAKLQSKEYSQY
|
3.6.4.13
| null |
antiviral innate immune response [GO:0140374]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; mRNA processing [GO:0006397]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; response to alkaloid [GO:0043279]; response to toxic substance [GO:0009636]; RNA splicing [GO:0008380]
|
nuclear speck [GO:0016607]; nucleolus [GO:0005730]; spliceosomal complex [GO:0005681]; U12-type spliceosomal complex [GO:0005689]; U2-type post-mRNA release spliceosomal complex [GO:0071008]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; helicase activity [GO:0004386]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]
|
PF00270;PF21010;PF04408;PF00271;PF07717;
|
1.20.120.1080;3.40.50.300;
|
DEAD box helicase family, DEAH subfamily, DDX15/PRP43 sub-subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9342318}. Nucleus, nucleolus {ECO:0000269|PubMed:9342318}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:O43143};
| null | null | null | null |
FUNCTION: RNA helicase involved in mRNA processing and antiviral innate immunity (PubMed:26494172, PubMed:34161762). Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA (By similarity). In cooperation with TFIP11 seem to be involved in the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns (By similarity). Plays a key role in antiviral innate immunity by promoting both MAVS-dependent signaling and NLRP6 inflammasome (PubMed:26494172). Acts as an RNA virus sensor: recognizes and binds viral double stranded RNA (dsRNA) and activates the MAVS-dependent signaling to produce interferon-beta and interferon lambda-3 (IFNL3) (By similarity). Involved in intestinal antiviral innate immunity together with NLRP6: recognizes and binds viral dsRNA and promotes activation of the NLRP6 inflammasome in intestinal epithelial cells to restrict infection by enteric viruses (PubMed:26494172, PubMed:34161762, PubMed:34678144). The NLRP6 inflammasome acts by promoting maturation and secretion of IL18 in the extracellular milieu (PubMed:34161762). Also involved in antibacterial innate immunity by promoting Wnt-induced antimicrobial protein expression in Paneth cells (PubMed:33483420). {ECO:0000250|UniProtKB:O43143, ECO:0000269|PubMed:26494172, ECO:0000269|PubMed:33483420, ECO:0000269|PubMed:34161762, ECO:0000269|PubMed:34678144}.
|
Mus musculus (Mouse)
|
O35291
|
RNAS2_MOUSE
|
MGPKLLESRLCLLLLLGLVLMLASCQAQILSQKFYTQHIYNSTYPRCDAVMRVVNRYRPRCKDINTFLHTSFADVVAVCGHPNITCNNLTRKNCHASSFQVFITFCNLTMPTRICTQCRYQTTGSVKYYRVACENRTPQDTPMYPVVPVHLDGTF
|
4.6.1.18
| null |
chemotaxis [GO:0006935]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response in mucosa [GO:0002227]
|
extracellular space [GO:0005615]; lysosome [GO:0005764]
|
lyase activity [GO:0016829]; nucleic acid binding [GO:0003676]; ribonuclease A activity [GO:0004522]; RNA nuclease activity [GO:0004540]
|
PF00074;
|
3.10.130.10;
|
Pancreatic ribonuclease family
| null |
SUBCELLULAR LOCATION: Lysosome {ECO:0000305}. Cytoplasmic granule. Note=Matrix of eosinophil's large specific granule.
|
CATALYTIC ACTIVITY: Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; Evidence={ECO:0000250|UniProtKB:P47784}; CATALYTIC ACTIVITY: Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; Evidence={ECO:0000250|UniProtKB:P47784};
| null | null | null | null |
FUNCTION: This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Possesses a wide variety of biological activities.
|
Mus musculus (Mouse)
|
O35293
|
CP2F2_RAT
|
MDGVSTAILLLLLAVISLSLTFTSWGKGQLPPGPKPLPILGNLLQLRSQDLLTSLTKLSKDYGSVFTVYLGPRRVIVLSGYQTVKEALVDKGEEFSGRGSYPIFFNFTKGNGIAFSDGERWKILRRFSVQILRNFGMGKRSIEERILEEGSFLLDVLRKTEGKPFDPVFILSRSVSNIICSVIFGSRFDYDDERLLTIIHFINDNFQIMSSPWGEMYNIFPSLLDWVPGPHRRVFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMVQEKQDPLSHFNMDTLLMTTHNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDCVVGRSRMPTLEDRASMPYTDAVIHEVQRFADVIPMNLPHRVIRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGEPLARMELFIYLTSILQNFTLHPLVEPEDIDLTPLSSGLGNLPRPFQLCMRIR
|
1.14.14.-
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
|
epoxygenase P450 pathway [GO:0019373]; naphthalene catabolic process [GO:1901170]; response to toxic substance [GO:0009636]; trichloroethylene metabolic process [GO:0018979]; xenobiotic metabolic process [GO:0006805]
|
cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]
|
arachidonic acid epoxygenase activity [GO:0008392]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]; oxygen binding [GO:0019825]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
| null | null | null | null | null |
FUNCTION: Involved in the regio- and stereoselective transformation of naphthalene to trans-1R-hydroxy-2R-glutathionyl-1,2-dihydronaphthalene in the presence of glutathione and glutathione S-transferases. It specifically catalyzes the production of a very reactive and potentially toxic intermediate, the 2R,2S arene oxide, that is associated with necrosis of the unciliated bronchiolar epithelial cells or club cells in lung. {ECO:0000269|PubMed:15509722}.
|
Rattus norvegicus (Rat)
|
O35295
|
PURB_MOUSE
|
MADGDSGSERGGGGGGGGGPGGFQPAPRGGGGGGGGPGGEQETQELASKRLDIQNKRFYLDVKQNAKGRFLKIAEVGAGGSKSRLTLSMAVAAEFRDSLGDFIEHYAQLGPSSPEQLAAGAEEGGGPRRALKSEFLVRENRKYYLDLKENQRGRFLRIRQTVNRGGGGFGGGPGPGGLQSGQTIALPAQGLIEFRDALAKLIDDYGGDEDELAGGPGGGAGGPGGGLYGELPEGTSITVDSKRFFFDVGCNKYGVFLRVSEVKPSYRNAITVPFKAWGKFGGAFCRYADEMKEIQERQRDKLYERRGGGSGGGDESEGEEVDED
| null | null |
DNA unwinding involved in DNA replication [GO:0006268]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
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]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; double-stranded DNA binding [GO:0003690]; double-stranded telomeric DNA binding [GO:0003691]; mRNA binding [GO:0003729]; mRNA regulatory element binding translation repressor activity [GO:0000900]; purine-rich negative regulatory element binding [GO:0032422]; RNA binding [GO:0003723]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; single-stranded DNA binding [GO:0003697]; SMAD binding [GO:0046332]
|
PF04845;
|
3.10.450.700;3.30.2450.30;
|
PUR DNA-binding protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33743134}.
| null | null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. {ECO:0000269|PubMed:27064749};
|
FUNCTION: Transcriptional regulator which can act as an activator or a repressor (PubMed:11751932, PubMed:12874279, PubMed:27064749, PubMed:31918924, PubMed:33743134, PubMed:9334258). Represses the transcription of ACTA2 in fibroblasts and smooth muscle cells via its ability to interact with the purine-rich strand of a MCAT-containing element in the 5' flanking region of the gene (PubMed:11751932, PubMed:12874279, PubMed:27064749, PubMed:9334258). Represses the transcription of MYOCD, capable of repressing all isoforms of MYOCD but the magnitude of the repressive effects is most notable for the SMC-specific isoforms (PubMed:33743134). Promotes hepatic glucose production by activating the transcription of ADCY6, leading to cAMP accumulation, increased PKA activity, CREB activation, and increased transcription of PCK1 and G6PC genes (PubMed:31918924). Has capacity to bind repeated elements in single-stranded DNA such as the purine-rich single strand of the PUR element located upstream of the MYC gene (By similarity). Participates in transcriptional and translational regulation of alpha-MHC expression in cardiac myocytes by binding to the purine-rich negative regulatory (PNR) element (By similarity). Modulates constitutive liver galectin-3 gene transcription by binding to its promoter (By similarity). May play a role in the dendritic transport of a subset of mRNAs (By similarity). {ECO:0000250|UniProtKB:Q68A21, ECO:0000250|UniProtKB:Q96QR8, ECO:0000269|PubMed:11751932, ECO:0000269|PubMed:12874279, ECO:0000269|PubMed:27064749, ECO:0000269|PubMed:31918924, ECO:0000269|PubMed:33743134, ECO:0000269|PubMed:9334258}.
|
Mus musculus (Mouse)
|
O35298
|
AOAH_MOUSE
|
MKFPWKVFKTTLLLLLLSHSLASVPSEDQPGDSYSHGQSCLGCVVLVSVIEQLAEVHNSSVQVAMERLCSYLPEKLFLKTACYFLVQTFGSDIIKLLDEAMKADVVCYALEFCKRGAVQPQCHLYPLPQEAWESALEKARQVLRRSSTMKYPRSGRNICSLPFLTKICQKIELSIKKAVPFKDIDSDKHSVFPTLRGYHWRGRDCNDSDKTVYPGRRPDNWDIHQDSNCNGIWGIDPKDGIPYEKKFCEGSQPRGIILLGDSAGAHFHIPPEWLTASQMSVNSFLNLPSALTDELNWPQLSGVTGFLDSTSGIEEKSIYHRLRKRNHCNHRDYQSISKNGASSRNLKNFIESLSRNQASDHPAIVLYAMIGNDVCNSKADTVPEMTTPEQMYANVMQTLTHLNSHLPNGSHVILYGLPDGTFLWDSLHNRYHPLGQLNKDVTYAQFFSFLRCLQLNPCNGWMSSNKTLRTLTSERAEQLSNTLKKIATTETFANFDLFYVDFAFHEIIEDWQKRGGQPWQLIEPVDGFHPNEVASLLQANRVWEKIQLQWPHVLGKENPFNSQIEEVFGDQGGH
|
3.1.1.77
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:29343645}; Note=Binds 3 Ca(2+) ions per subunit. The calcium ions probably have a structural role. {ECO:0000269|PubMed:29343645};
|
fatty acid metabolic process [GO:0006631]; lipopolysaccharide catabolic process [GO:0009104]; lipopolysaccharide metabolic process [GO:0008653]; negative regulation of inflammatory response [GO:0050728]
|
cytoplasmic vesicle [GO:0031410]; extracellular region [GO:0005576]
|
acyloxyacyl hydrolase activity [GO:0050528]; calcium ion binding [GO:0005509]
|
PF00657;PF20825;
|
1.10.225.10;3.40.50.1110;
| null |
PTM: Cleaved into a large and a small subunit. {ECO:0000250|UniProtKB:P28039}.; PTM: The small subunit is N-glycosylated. {ECO:0000250|UniProtKB:P28039}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15155618}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P28039}. Note=Detected in urine. {ECO:0000269|PubMed:15155618}.
|
CATALYTIC ACTIVITY: Reaction=a 3-(acyloxy)acyl derivative of bacterial toxin + H2O = 3-hydroxyacyl derivative of bacterial toxin + a fatty acid + H(+); Xref=Rhea:RHEA:12032, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:136853, ChEBI:CHEBI:140675; EC=3.1.1.77; Evidence={ECO:0000305|PubMed:12810692, ECO:0000305|PubMed:15155618, ECO:0000305|PubMed:17322564, ECO:0000305|PubMed:18779055, ECO:0000305|PubMed:19860560};
| null | null | null | null |
FUNCTION: Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (LPS) (PubMed:12810692, PubMed:15155618, PubMed:17322564, PubMed:19860560). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses (PubMed:17322564, PubMed:19860560, PubMed:28622363). In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria (PubMed:18779055). {ECO:0000269|PubMed:12810692, ECO:0000269|PubMed:15155618, ECO:0000269|PubMed:17322564, ECO:0000269|PubMed:18779055, ECO:0000269|PubMed:19860560, ECO:0000269|PubMed:28622363}.
|
Mus musculus (Mouse)
|
O35303
|
DNM1L_RAT
|
MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGVVTRRPLILQLVHVSPEDKRKTTGEENDPATWKNSRHLSKGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKVFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGEPVDDKSATLLQLITKFATEYCNTIEGTAKYIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRRNRLARELPSAVSRDKSSKVPSALAPASQEPSPAASAEADGKLIQDNRRETKNVASAGGGIGDGGRIGDGGQEPTTGNWRGMLKTSKAEELLAEEKSKPIPIMPASPQKGHAVNLLDVPVPVARKLSAREQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKALQGASQIIAEIRETHLW
|
3.6.5.5
| null |
calcium ion transport [GO:0006816]; cellular response to hypoxia [GO:0071456]; cellular response to lipid [GO:0071396]; endocytosis [GO:0006897]; heart contraction [GO:0060047]; intracellular distribution of mitochondria [GO:0048312]; membrane fusion [GO:0061025]; mitochondrial fission [GO:0000266]; mitochondrial fragmentation involved in apoptotic process [GO:0043653]; mitochondrial membrane fission [GO:0090149]; mitochondrion organization [GO:0007005]; mitocytosis [GO:0160040]; necroptotic process [GO:0070266]; negative regulation of mitochondrial fusion [GO:0010637]; peroxisome fission [GO:0016559]; positive regulation of apoptotic process [GO:0043065]; positive regulation of dendritic spine morphogenesis [GO:0061003]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of mitochondrial fission [GO:0090141]; positive regulation of neutrophil chemotaxis [GO:0090023]; positive regulation of protein secretion [GO:0050714]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; positive regulation of synaptic vesicle endocytosis [GO:1900244]; positive regulation of synaptic vesicle exocytosis [GO:2000302]; protein complex oligomerization [GO:0051259]; protein localization to mitochondrion [GO:0070585]; protein-containing complex assembly [GO:0065003]; regulation of ATP metabolic process [GO:1903578]; regulation of gene expression [GO:0010468]; regulation of mitochondrion organization [GO:0010821]; regulation of mitophagy [GO:1901524]; regulation of peroxisome organization [GO:1900063]; release of cytochrome c from mitochondria [GO:0001836]; response to endoplasmic reticulum stress [GO:0034976]; response to flavonoid [GO:1905395]; response to hypobaric hypoxia [GO:1990910]; rhythmic process [GO:0048511]; synaptic vesicle endocytosis [GO:0048488]; synaptic vesicle recycling via endosome [GO:0036466]
|
brush border [GO:0005903]; clathrin-coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; microtubule [GO:0005874]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; perinuclear region of cytoplasm [GO:0048471]; peroxisome [GO:0005777]; presynaptic endocytic zone membrane [GO:0098835]; protein-containing complex [GO:0032991]; secretory vesicle [GO:0099503]; synaptic vesicle membrane [GO:0030672]
|
BH2 domain binding [GO:0051433]; clathrin binding [GO:0030276]; GTP binding [GO:0005525]; GTP-dependent protein binding [GO:0030742]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; microtubule binding [GO:0008017]; protein homodimerization activity [GO:0042803]; protein serine/threonine kinase binding [GO:0120283]; protein-containing complex binding [GO:0044877]; small GTPase binding [GO:0031267]; ubiquitin protein ligase binding [GO:0031625]
|
PF01031;PF00350;PF02212;
|
1.20.120.1240;3.40.50.300;
|
TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family
|
PTM: Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission (By similarity). Phosphorylation on Ser-656 by CAMK1 and PKA inhibits the GTPase activity, leading to a defect in mitochondrial fission promoting mitochondrial elongation (By similarity). Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission (By similarity). Phosphorylation on Ser-635 by PINK1 activates the GTPase activity and promotes mitochondrial fission (By similarity). Phosphorylation on Ser-635 by CDK1 also promotes mitochondrial fission (PubMed:17301055). Phosphorylated in a circadian manner at Ser-656 (By similarity). Dephosphorylated by PGAM5 (By similarity). {ECO:0000250|UniProtKB:O00429, ECO:0000269|PubMed:17301055}.; PTM: Sumoylated on various lysine residues within the B domain, probably by MUL1. Sumoylation positively regulates mitochondrial fission. Desumoylated by SENP5 during G2/M transition of mitosis. Appears to be linked to its catalytic activity (By similarity). {ECO:0000250}.; PTM: S-nitrosylation increases DNM1L dimerization, mitochondrial fission and causes neuronal damage. {ECO:0000250}.; PTM: O-GlcNAcylation augments the level of the GTP-bound active form of DNM1L and induces translocation from the cytoplasm to mitochondria in cardiomyocytes. It also decreases phosphorylation at Ser-656. {ECO:0000269|PubMed:17301055}.; PTM: Ubiquitination by MARCHF5 affects mitochondrial morphology. {ECO:0000250|UniProtKB:O00429}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12861026, ECO:0000269|PubMed:22745122}. Golgi apparatus {ECO:0000250|UniProtKB:O00429}. Endomembrane system {ECO:0000250|UniProtKB:O00429}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8K1M6}. Mitochondrion outer membrane {ECO:0000269|PubMed:12861026, ECO:0000269|PubMed:22745122}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8K1M6}. Peroxisome {ECO:0000269|PubMed:12499366}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:23792689}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:23792689}. Note=Mainly cytosolic. Recruited by RALA and RALBP1 to mitochondrion during mitosis. Translocated to the mitochondrial membrane through O-GlcNAcylation and interaction with FIS1. Colocalized with MARCHF5 at mitochondrial membrane. Localizes to mitochondria at sites of division. Localizes to mitochondria following necrosis induction. Recruited to the mitochondrial outer membrane by interaction with MIEF1. Mitochondrial recruitment is inhibited by C11orf65/MFI (By similarity). Associated with peroxisomal membranes, partly recruited there by PEX11B. May also be associated with endoplasmic reticulum tubules and cytoplasmic vesicles and found to be perinuclear (PubMed:23792689). In some cell types, localizes to the Golgi complex (By similarity). Binds to phospholipid membranes (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8K1M6, ECO:0000269|PubMed:23792689}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5; Evidence={ECO:0000250|UniProtKB:O00429};
| null | null | null | null |
FUNCTION: Functions in mitochondrial and peroxisomal division (PubMed:11553726, PubMed:12499366, PubMed:12861026, PubMed:17301055, PubMed:18250306). Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism (PubMed:11553726). The specific recruitment at scission sites is mediated by membrane receptors like MFF, MIEF1 and MIEF2 for mitochondrial membranes (By similarity). While the recruitment by the membrane receptors is GTP-dependent, the following hydrolysis of GTP induces the dissociation from the receptors and allows DNM1L filaments to curl into closed rings that are probably sufficient to sever a double membrane (By similarity). Acts downstream of PINK1 to promote mitochondrial fission in a PRKN-dependent manner. Plays an important role in mitochondrial fission during mitosis (By similarity). Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage (By similarity). Required for normal brain development, including that of cerebellum (By similarity). Facilitates developmentally regulated apoptosis during neural tube formation (By similarity). Required for a normal rate of cytochrome c release and caspase activation during apoptosis; this requirement may depend upon the cell type and the physiological apoptotic cues (By similarity). Required for formation of endocytic vesicles (PubMed:18250306, PubMed:23792689). Proposed to regulate synaptic vesicle membrane dynamics through association with BCL2L1 isoform Bcl-X(L) which stimulates its GTPase activity in synaptic vesicles; the function may require its recruitment by MFF to clathrin-containing vesicles (PubMed:18250306, PubMed:23792689). Required for programmed necrosis execution (By similarity). Rhythmic control of its activity following phosphorylation at Ser-656 is essential for the circadian control of mitochondrial ATP production (By similarity). {ECO:0000250|UniProtKB:O00429, ECO:0000250|UniProtKB:Q8K1M6, ECO:0000269|PubMed:11553726, ECO:0000269|PubMed:12499366, ECO:0000269|PubMed:12861026, ECO:0000269|PubMed:17301055, ECO:0000269|PubMed:18250306, ECO:0000269|PubMed:23792689}.
|
Rattus norvegicus (Rat)
|
O35304
|
VACHT_MOUSE
|
MEPTAPTGQARAAATKLSEAVGAALQEPQRQRRLVLVIVCVALLLDNMLYMVIVPIVPDYIAHMRGGSESPTLISEVWEPTLPPPTLANASAYLANTSASPTAAGSARSILRPRYPTESEDVKIGVLFASKAILQLLVNPLSGPFIDRMSYDVPLLIGLGVMFASTVMFAFAEDYATFFAARSLQGLGSAFADTSGIAMIADKYPEEPERSRALGVALAFISFGSLVAPPFGGILYEFAGKRVPFLVLAAVSLFDALLLLAVAKPFSAAARARANLPVGTPIHRLMLDPYIAVVAGALTTCNIPLAFLEPTIATWMKHTMAASEWEMGMVWLPAFVPHVLGVYLTVRLAARYPHLQWLYGALGLAVIGVSSCVVPACRSFAPLVVSLCGLCFGIALVDTALLPTLAFLVDVRHVSVYGSVYAIADISYSVAYALGPIVAGHIVHSLGFEQLSLGMGLANLLYAPVLLLLRNVGLLTRSRSERDVLLDEPPQGLYDAVRLREVQGKDGGEPCSPPGPFDGCEDDYNYYSRS
| null | null |
acetylcholine transport [GO:0015870]; acetylcholine uptake [GO:0051630]; chemical synaptic transmission [GO:0007268]; neurotransmitter loading into synaptic vesicle [GO:0098700]; positive regulation of acetylcholine secretion, neurotransmission [GO:0014057]; positive regulation of long-term synaptic potentiation [GO:1900273]; positive regulation of neuromuscular junction development [GO:1904398]
|
AP-1 adaptor complex [GO:0030121]; AP-2 adaptor complex [GO:0030122]; axon [GO:0030424]; axon terminus [GO:0043679]; cholinergic synapse [GO:0098981]; cytoplasm [GO:0005737]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]; terminal bouton [GO:0043195]
|
acetylcholine transmembrane transporter activity [GO:0005277]; acetylcholine:proton antiporter activity [GO:0005278]; monoamine transmembrane transporter activity [GO:0008504]
|
PF07690;
|
1.20.1250.20;
|
Major facilitator superfamily, Vesicular transporter family
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q62666}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=acetylcholine(out) + 2 H(+)(in) = acetylcholine(in) + 2 H(+)(out); Xref=Rhea:RHEA:72891, ChEBI:CHEBI:15355, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q16572}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72892; Evidence={ECO:0000250|UniProtKB:Q16572}; CATALYTIC ACTIVITY: Reaction=choline(in) + 2 H(+)(out) = choline(out) + 2 H(+)(in); Xref=Rhea:RHEA:73819, ChEBI:CHEBI:15354, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q62666}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73820; Evidence={ECO:0000250|UniProtKB:Q62666}; CATALYTIC ACTIVITY: Reaction=2 H(+)(out) + serotonin(in) = 2 H(+)(in) + serotonin(out); Xref=Rhea:RHEA:73743, ChEBI:CHEBI:15378, ChEBI:CHEBI:350546; Evidence={ECO:0000250|UniProtKB:Q16572};
| null | null | null | null |
FUNCTION: Electrogenic antiporter that exchanges one cholinergic neurotransmitter, acetylcholine or choline, with two intravesicular protons across the membrane of synaptic vesicles. Uses the electrochemical proton gradient established by the V-type proton-pump ATPase to store neurotransmitters inside the vesicles prior to their release via exocytosis (By similarity). Determines cholinergic vesicular quantal size at presynaptic nerve terminals in developing neuro-muscular junctions with an impact on motor neuron differentiation and innervation pattern (By similarity) (PubMed:19635813). Part of forebrain cholinergic system, regulates hippocampal synapse transmissions that underlie spatial memory formation (PubMed:23045697). Can transport serotonin. {ECO:0000250|UniProtKB:Q16572, ECO:0000250|UniProtKB:Q62666, ECO:0000269|PubMed:19635813, ECO:0000269|PubMed:23045697}.
|
Mus musculus (Mouse)
|
O35305
|
TNR11_MOUSE
|
MAPRARRRRQLPAPLLALCVLLVPLQVTLQVTPPCTQERHYEHLGRCCSRCEPGKYLSSKCTPTSDSVCLPCGPDEYLDTWNEEDKCLLHKVCDAGKALVAVDPGNHTAPRRCACTAGYHWNSDCECCRRNTECAPGFGAQHPLQLNKDTVCTPCLLGFFSDVFSSTDKCKPWTNCTLLGKLEAHQGTTESDVVCSSSMTLRRPPKEAQAYLPSLIVLLLFISVVVVAAIIFGVYYRKGGKALTANLWNWVNDACSSLSGNKESSGDRCAGSHSATSSQQEVCEGILLMTREEKMVPEDGAGVCGPVCAAGGPWAEVRDSRTFTLVSEVETQGDLSRKIPTEDEYTDRPSQPSTGSLLLIQQGSKSIPPFQEPLEVGENDSLSQCFTGTESTVDSEGCDFTEPPSRTDSMPVSPEKHLTKEIEGDSCLPWVVSSNSTDGYTGSGNTPGEDHEPFPGSLKCGPLPQCAYSMGFPSEAAASMAEAGVRPQDRADERGASGSGSSPSDQPPASGNVTGNSNSTFISSGQVMNFKGDIIVVYVSQTSQEGPGSAEPESEPVGRPVQEETLAHRDSFAGTAPRFPDVCATGAGLQEQGAPRQKDGTSRPVQEQGGAQTSLHTQGSGQCAE
| null | null |
adaptive immune response [GO:0002250]; cellular response to zinc ion starvation [GO:0034224]; circadian temperature homeostasis [GO:0060086]; lymph node development [GO:0048535]; mammary gland alveolus development [GO:0060749]; multinuclear osteoclast differentiation [GO:0072674]; ossification [GO:0001503]; positive regulation of bone resorption [GO:0045780]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fever generation by positive regulation of prostaglandin secretion [GO:0071812]; positive regulation of osteoclast differentiation [GO:0045672]; response to ethanol [GO:0045471]; response to insulin [GO:0032868]; response to interleukin-1 [GO:0070555]; response to lipopolysaccharide [GO:0032496]; response to mechanical stimulus [GO:0009612]; response to organic cyclic compound [GO:0014070]; response to tumor necrosis factor [GO:0034612]; tumor necrosis factor-mediated signaling pathway [GO:0033209]
|
cell surface [GO:0009986]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; membrane raft [GO:0045121]
|
cytokine binding [GO:0019955]; metal ion binding [GO:0046872]; tumor necrosis factor receptor activity [GO:0005031]
|
PF18278;PF00020;
|
2.10.50.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Y6Q6}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:23478294}.
| null | null | null | null | null |
FUNCTION: Receptor for TNFSF11/RANKL/TRANCE/OPGL; essential for RANKL-mediated osteoclastogenesis (PubMed:20483727, PubMed:23478294, PubMed:9878548). Its interaction with EEIG1 promotes osteoclastogenesis via facilitating the transcription of NFATC1 and activation of PLCG2 (PubMed:23478294). Involved in the regulation of interactions between T-cells and dendritic cells (PubMed:9367155). {ECO:0000269|PubMed:20483727, ECO:0000269|PubMed:23478294, ECO:0000269|PubMed:9367155, ECO:0000269|PubMed:9878548}.
|
Mus musculus (Mouse)
|
O35309
|
NMI_MOUSE
|
MDADKDNIKQACDERSAEMDDMRGEQSMGLVHEIMSENKELDEEIKKLEAELQSDAREFQIKENVPEKKLKLTSVESPKDGCHFSNSSCSFQVSSQILYELQEGQALITFEKEEVAQNVISMGNHVVQMEGTPVKVSAHPVPLNTGVRFQVHVDISKMKINVTGIPDELSEEQTRDKLELSFCKSRNGGGEVESVDYDRKSRSAVITFVETGVVDKILKKKTYPLYMNQKCHSVAVSPCIERCLEKYQVFSAVSKKTVLLTGLEGIPVDEETGEDLLNIHFQRKNNGGGEVEVVKCSLDQSFAAYFKEEARETI
| null | null |
innate immune response [GO:0045087]; macrophage activation involved in immune response [GO:0002281]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of innate immune response [GO:0045824]; negative regulation of interferon-alpha production [GO:0032687]; negative regulation of interferon-beta production [GO:0032688]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; negative regulation of type I interferon production [GO:0032480]; positive regulation of inflammatory response [GO:0050729]; positive regulation of innate immune response [GO:0045089]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of protein K48-linked ubiquitination [GO:1902524]; protein K48-linked ubiquitination [GO:0070936]; response to virus [GO:0009615]; toll-like receptor 4 signaling pathway [GO:0034142]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
identical protein binding [GO:0042802]
|
PF07334;PF07292;
|
3.30.70.330;
|
NMI family
|
PTM: May be ubiquitinated. {ECO:0000250|UniProtKB:Q13287}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13287}. Nucleus {ECO:0000250|UniProtKB:Q13287}. Secreted {ECO:0000250|UniProtKB:Q13287}. Note=Cytoplasmic NMI localizes in punctate granular structures. Nuclear localization increased following IFN-alpha treatment. Extracelullar following secretion by macrophage. {ECO:0000250|UniProtKB:Q13287}.
| null | null | null | null | null |
FUNCTION: Acts as a signaling pathway regulator involved in innate immune system response (PubMed:23956435). In response to interleukin 2/IL2 and interferon IFN-gamma/IFNG, interacts with signal transducer and activator of transcription/STAT which activate the transcription of downstream genes involved in a multitude of signals for development and homeostasis (By similarity). Enhances the recruitment of CBP/p300 coactivators to STAT1 and STAT5, resulting in increased STAT1- and STAT5-dependent transcription (By similarity). In response to interferon IFN-alpha, associates in a complex with transcriptional regulator IFI35 to regulate immune response; the complex formation prevents proteasome-mediated degradation of IFI35 (By similarity). In complex with IFI35, negatively regulates nuclear factor NF-kappa-B signaling by inhibiting the nuclear translocation, activation and transcription of NF-kappa-B subunit p65/RELA, resulting in the inhibition of endothelial cell proliferation, migration and re-endothelialization of injured arteries (By similarity). Negatively regulates virus-triggered type I interferon/IFN production by inducing proteosome-dependent degradation of IRF7, a transcriptional regulator of type I IFN, thereby interfering with cellular antiviral responses (PubMed:23956435). Beside its role as an intracellular signaling pathway regulator, also functions extracellularly as damage-associated molecular patterns (DAMPs) to promote inflammation, when actively released by macrophage to the extracellular space during cell injury or pathogen invasion (By similarity). Macrophage-secreted NMI activates NF-kappa-B signaling in adjacent macrophages through Toll-like receptor 4/TLR4 binding and activation, thereby inducing NF-kappa-B translocation from the cytoplasm into the nucleus which promotes the release of pro-inflammatory cytokines (By similarity). {ECO:0000250|UniProtKB:Q13287, ECO:0000269|PubMed:23956435}.
|
Mus musculus (Mouse)
|
O35310
|
HS3S1_MOUSE
|
MTLLLLGAVLLVAQPQLVHSHPAAPGPGLKQQELLRKVIILPEDTGEGTASNGSTQQLPQTIIIGVRKGGTRALLEMLSLHPDVAAAENEVHFFDWEEHYSQGLGWYLTQMPFSSPHQLTVEKTPAYFTSPKVPERIHSMNPTIRLLLILRDPSERVLSDYTQVLYNHLQKHKPYPPIEDLLMRDGRLNLDYKALNRSLYHAHMLNWLRFFPLGHIHIVDGDRLIRDPFPEIQKVERFLKLSPQINASNFYFNKTKGFYCLRDSGKDRCLHESKGRAHPQVDPKLLDKLHEYFHEPNKKFFKLVGRTFDWH
|
2.8.2.23
| null |
glycosaminoglycan biosynthetic process [GO:0006024]; heparan sulfate proteoglycan biosynthetic process [GO:0015012]
|
Golgi apparatus [GO:0005794]; Golgi lumen [GO:0005796]
|
[heparan sulfate]-glucosamine 3-sulfotransferase 1 activity [GO:0008467]
|
PF00685;
|
3.40.50.300;
|
Sulfotransferase 1 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus lumen {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = 3-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:15461, Rhea:RHEA-COMP:9830, Rhea:RHEA-COMP:9831, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388, ChEBI:CHEBI:70975; EC=2.8.2.23; Evidence={ECO:0000269|PubMed:15060080};
| null | null | null | null |
FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan (PubMed:15060080, PubMed:9346953). Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact) (PubMed:15060080, PubMed:9346953). This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site (PubMed:15060080, PubMed:9346953). {ECO:0000269|PubMed:15060080, ECO:0000269|PubMed:9346953}.
|
Mus musculus (Mouse)
|
O35312
|
GDF8_RAT
|
MIQKPQMYVYIYLFVLIAAGPVDLNEDSEREANVEKEGLCNACAWRQNTRYSRIEAIKIQILSKLRLETAPNISKDAIRQLLPRAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQADGKPKCCFFKFSSKIQYNKVVKAQLWIYLRAVKTPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMSPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS
| null | null |
cellular response to dexamethasone stimulus [GO:0071549]; cellular response to hypoxia [GO:0071456]; muscle cell cellular homeostasis [GO:0046716]; myoblast migration involved in skeletal muscle regeneration [GO:0014839]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of muscle hypertrophy [GO:0014741]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of myoblast proliferation [GO:2000818]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of satellite cell differentiation [GO:1902725]; negative regulation of skeletal muscle satellite cell proliferation [GO:1902723]; negative regulation of skeletal muscle tissue growth [GO:0048632]; ovulation cycle process [GO:0022602]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of macrophage chemotaxis [GO:0010759]; response to electrical stimulus [GO:0051602]; response to estrogen [GO:0043627]; response to ethanol [GO:0045471]; response to glucocorticoid [GO:0051384]; response to gravity [GO:0009629]; response to muscle activity [GO:0014850]; response to testosterone [GO:0033574]; skeletal muscle atrophy [GO:0014732]; skeletal muscle satellite cell differentiation [GO:0014816]; skeletal muscle tissue regeneration [GO:0043403]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102]
|
PF00019;PF00688;
|
2.60.120.970;2.10.90.10;
|
TGF-beta family
|
PTM: Synthesized as large precursor molecule that undergoes proteolytic cleavage to generate an N-terminal propeptide and a disulfide linked C-terminal dimer, which is the biologically active molecule. The circulating form consists of a latent complex of the C-terminal dimer and other proteins, including its propeptide, which maintain the C-terminal dimer in a latent, inactive state. Ligand activation requires additional cleavage of the prodomain by a tolloid-like metalloproteinase. {ECO:0000250|UniProtKB:O08689}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O08689}.
| null | null | null | null | null |
FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth. {ECO:0000250|UniProtKB:O08689}.
|
Rattus norvegicus (Rat)
|
O35314
|
SCG1_RAT
|
MQRAMLLGLLGAAALAAVISAPVDNRDHNEEMVTRCIIEVLSNALSKSSAPTITPECRQVLRKSGKEVKGEEKGENENSKFEVRLLRDPSDASVGRWASSREETGAPVEDSPGQAKVDNEEWTGGGGHSREAVDDQESLHPSNQQVSKEAKIRHSEERGGKEEEEEEGKIYPKGEHRGDAGEEKKHTEESGEKHNAFSNKRSEASAKKKEESVARAEAHFVELEKTHSREQSSQESGEETRRQEKPQELPDQDQSEEESEEGEEGEEGATSEVTKRRPRHHHWRSQSNKPSYEGRRPLSEERKHAAGESKDANVATANLGEKRGHHLAHYRASEEEPDYGEELRSYPGFQAPQGLQYQGRGSEEVRAPSPRSEESQEKEYKRNHPDSELESTANRHSEETEEERSYEGAKGRQHRGRGREPGAYPALDSRQEKRLLDEGHDPVHESPVDTAKRYPQSKWQEQEKNYLNYDEEGDQGRWWQQEEQLEPEESREEVSFPDRQYAPYPTTEKRKRLGALFNPYFDPLQWKNSDFEKKGNPDDSFLDDDGEDGNGVTMTEKNFFPEYNYDWWEKRPFSEDVNWGYEKRSFARAPHLDLKRQYDDGVAELDQLLHYRKKAAEFPDFYDSEEQMGPHQEAEDEKDRADQRVLTEEEKKELENLAAMDLELQKIAEKFSQRG
| null | null | null |
extracellular space [GO:0005615]; secretory granule [GO:0030141]
| null |
PF01271;
| null |
Chromogranin/secretogranin protein family
|
PTM: Extensively processed in glucagonoma tissue by limited proteolysis at conserved basic residues. Alternative processing are seen in different tissues. The proglucagon-converting enzymes present in transformed alpha-cells are likely candidates to be involved in tissue-specific processing.
|
SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine secretory granules. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Secretogranin-1 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides.
|
Rattus norvegicus (Rat)
|
O35316
|
SC6A6_MOUSE
|
MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEADGKPPQREKWSSKIDFVLSVAGGFVGLGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLEVIIGQYTSEGGITCWEKICPLFSGIGYASIVIVSLLNVYYIVILAWATYYLFHSFQKDLPWAHCNHSWNTPQCMEDTLRRNESHWVSLSTANFTSPVIEFWERNVLSLSSGIDNPGSLKWDLALCLLLVWLVCFFCIWKGVRSTGKVVYFTATFPFAMLLVLLVRGLTLPGAGEGIKFYLYPDISRLGDPQVWIDAGTQIFFSYAICLGAMTSLGSYNKYKYNSYRDCMLLGCLNSGTSFVSGFAIFSILGFMAQEQGVDIADVAESGPGLAFIAYPKAVTMMPLPTFWSILFFIMLLLLGLDSQFVEVEGQITSLVDLYPSFLRKGYRREIFIAILCSISYLLGLTMVTEGGMYVFQLFDYYAASGVCLLWVAFFECFVIAWIYGGDNLYDGIEDMIGYRPGPWMKYSWAVITPALCVGCFVFSLVKYVPLTYNKVYRYPDWAIGLGWGLALSSMLCIPLVIVILLCRTEGPLRVRIKYLITPREPNRWAVEREGATPFHSRVTLMNGALMKPSHVIVETMM
| null | null |
amino acid import across plasma membrane [GO:0089718]; amino acid transport [GO:0006865]; gamma-aminobutyric acid import [GO:0051939]; import across plasma membrane [GO:0098739]; modulation of chemical synaptic transmission [GO:0050804]; neurotransmitter transport [GO:0006836]; positive regulation of cell differentiation [GO:0045597]; sodium ion transmembrane transport [GO:0035725]; taurine transport [GO:0015734]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell projection [GO:0042995]; dendrite [GO:0030425]; GABA-ergic synapse [GO:0098982]; microvillus membrane [GO:0031528]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; plasma membrane protein complex [GO:0098797]; postsynaptic membrane [GO:0045211]
|
alanine transmembrane transporter activity [GO:0022858]; amino acid:sodium symporter activity [GO:0005283]; gamma-aminobutyric acid transmembrane transporter activity [GO:0015185]; gamma-aminobutyric acid:sodium:chloride symporter activity [GO:0005332]; taurine binding [GO:0030977]; taurine transmembrane transporter activity [GO:0005368]; taurine:sodium symporter activity [GO:0005369]
|
PF00209;
| null |
Sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family, SLC6A6 subfamily
|
PTM: Taurine transport activity is down-regulated upon Ser-322 phosphorylation. {ECO:0000250|UniProtKB:Q00589}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P31641}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=4-aminobutanoate(out) + chloride(out) + 2 Na(+)(out) = 4-aminobutanoate(in) + chloride(in) + 2 Na(+)(in); Xref=Rhea:RHEA:70687, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:59888; Evidence={ECO:0000269|PubMed:30270321, ECO:0000269|PubMed:9375654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70688; Evidence={ECO:0000305|PubMed:30270321}; CATALYTIC ACTIVITY: Reaction=chloride(out) + 2 Na(+)(out) + taurine(out) = chloride(in) + 2 Na(+)(in) + taurine(in); Xref=Rhea:RHEA:71223, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:1465453, ECO:0000269|PubMed:30270321, ECO:0000269|PubMed:9375654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71224; Evidence={ECO:0000269|PubMed:1465453}; CATALYTIC ACTIVITY: Reaction=beta-alanine(out) + chloride(out) + 2 Na(+)(out) = beta-alanine(in) + chloride(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71247, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57966; Evidence={ECO:0000269|PubMed:1465453, ECO:0000269|PubMed:9375654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71248; Evidence={ECO:0000305|PubMed:1465453}; CATALYTIC ACTIVITY: Reaction=chloride(out) + hypotaurine(out) + 2 Na(+)(out) = chloride(in) + hypotaurine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71243, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57853; Evidence={ECO:0000269|PubMed:30270321}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71244; Evidence={ECO:0000305|PubMed:30270321};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.5 uM for taurine {ECO:0000269|PubMed:1465453}; KM=13.2 uM for taurine {ECO:0000269|PubMed:9375654}; KM=10.7 uM for hypotaurine {ECO:0000269|PubMed:30270321}; KM=56 uM for beta-alanine {ECO:0000269|PubMed:1465453};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0 (for taurine transport). {ECO:0000269|PubMed:9375654};
| null |
FUNCTION: Mediates sodium- and chloride-dependent transport of taurine (PubMed:1465453, PubMed:30270321, PubMed:9375654). Can also mediate transport of hypotaurine, beta-alanine and gamma-aminobutyric acid (GABA) (PubMed:1465453, PubMed:30270321, PubMed:9375654). {ECO:0000269|PubMed:1465453, ECO:0000269|PubMed:30270321, ECO:0000269|PubMed:9375654}.
|
Mus musculus (Mouse)
|
O35317
|
PBX3_MOUSE
|
MDDQSRMLQTLAGVNLAGHSVQGGMALPPPPHGHEGADGDGRKQDIGDILHQIMTITDQSLDEAQAKKHALNCHRMKPALFSVLCEIKEKTGLSIRGAQEEDPPDPQLMRLDNMLLAEGVSGPEKGGGSAAAAAAAAASGGSSDNSIEHSDYRAKLTQIRQIYHTELEKYEQACNEFTTHVMNLLREQSRTRPISPKEIERMVGIIHRKFSSIQMQLKQSTCEAVMILRSRFLDARRKRRNFSKQATEILNEYFYSHLSNPYPSEEAKEELAKKCSITVSQVSNWFGNKRIRYKKNIGKFQEEANLYAAKTAVTAAHAVAAAVQNNQTNSPTTPNSGSSGSFNLPNSGDMFMNMQSLNGDSYQGSQVGANVQSQVDTLRHVINQTGGYSDGLGANSLYSPHNLNANGGWQDATTPSSVTSPTEGPGSVHSDTSN
| null | null |
adult locomotory behavior [GO:0008344]; animal organ morphogenesis [GO:0009887]; brain development [GO:0007420]; dorsal spinal cord development [GO:0021516]; embryonic organ development [GO:0048568]; eye development [GO:0001654]; neuron development [GO:0048666]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of respiratory gaseous exchange by nervous system process [GO:0002087]; regulation of transcription by RNA polymerase II [GO:0006357]; respiratory gaseous exchange by respiratory system [GO:0007585]
|
nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; 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;PF03792;
|
1.10.10.60;
|
TALE/PBX homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator that binds the sequence 5'-ATCAATCAA-3'. {ECO:0000250}.
|
Mus musculus (Mouse)
|
O35324
|
SH21B_MOUSE
|
MDLPYYHGCLTKRECEALLLKGGVDGNFLIRDSESVPGALCLCVSFKKLVYSYRIFREKHGYYRIETDAHTPRTIFPNLQELVSKYGKPGQGLVVHLSNPIMRNNLCQRGRRMELELNVYENTDEEYVDVLP
| null | null |
adaptive immune response [GO:0002250]; leukocyte activation involved in immune response [GO:0002366]; natural killer cell inhibitory signaling pathway [GO:0002769]; natural killer cell mediated cytotoxicity [GO:0042267]; negative regulation of bone resorption [GO:0045779]; negative regulation of natural killer cell mediated cytotoxicity [GO:0045953]; negative regulation of neutrophil differentiation [GO:0045659]; negative regulation of peptidyl-tyrosine phosphorylation [GO:0050732]; negative regulation of signal transduction [GO:0009968]; negative regulation of type II interferon production [GO:0032689]; positive regulation of B cell differentiation [GO:0045579]; positive regulation of innate immune response [GO:0045089]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]; positive regulation of natural killer cell mediated immunity [GO:0002717]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of signal transduction [GO:0009967]
|
cytosol [GO:0005829]
|
phosphotyrosine residue binding [GO:0001784]; signaling adaptor activity [GO:0035591]
|
PF00017;
|
3.30.505.10;
| null |
PTM: Phosphorylated on tyrosine residues; probably at Tyr-120 and/or Tyr-127. {ECO:0000269|PubMed:16127454}.
| null | null | null | null | null | null |
FUNCTION: Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family such as CD84, SLAMF1, LY9 and CD244. In SLAM signaling seems to cooperate with SH2D1A/SAP. Plays a role in regulation of effector functions of natural killer (NK) cells by controlling signal transduction through CD244/2B4. However, conflicting results are reported which may reflect the use of different strain backgrounds. Proposed to act as an inhibitor of CD244-mediated NK cell function including cytotoxicity and IFN-gamma production, the latter found also by triggering KLRA4 and KLRK1 next to CD244 (PubMed:16127454). Seems to positively regulate CD244- and CD84-dependent NK cell functions implicating CD244-mediated phosphorylation of VAV1. Activation of SLAMF7-mediated NK cell function does not effect receptor tyrosine phosphorylation but distal signaling (PubMed:19151721, PubMed:20962259, PubMed:24687958). In the context of NK cell-mediated cytotoxicity does not enhance conjugate formation with target cells but stimulates polarization of the microtubule-organizing center and cytotoxic granules toward the NK cell synapse (PubMed:24687958). Negatively regulates CD40-induced cytokine production in dendritic cells downstream of SLAM family receptors probably by inducing activation of the PI3K pathway to inhibit p38 MAPK and JNK activation (PubMed:26432891). {ECO:0000250|UniProtKB:O14796, ECO:0000269|PubMed:16127454, ECO:0000269|PubMed:19151721, ECO:0000269|PubMed:20962259, ECO:0000269|PubMed:24687958, ECO:0000269|PubMed:26432891}.
|
Mus musculus (Mouse)
|
O35326
|
SRSF5_MOUSE
|
MSGCRVFIGRLNPAAREKDVERFFKGYGRIRDIDLKRGFGFVEFEDPRDADDAVYELDGKELCSERVTIEHARARSRGGRGRGRYSDRFSSRRPRNDRRNAPPVRTENRLIVENLSSRVSWQDLKDFMRQAGEVTFADAHRPKLNEGVVEFASYGDLKNAIEKLSGKEINGRKIKLIEGSKRHRSRSRSRSRTRSSSRSRSRSRSRRSKSYSRSRSRSRSRSKSRSGSRSPVPEKSQKRGSSSRSKSPASVDRQRSRSRSRSRSVDSGN
| null | null |
mRNA splicing, via spliceosome [GO:0000398]; positive regulation of RNA splicing [GO:0033120]; response to insulin [GO:0032868]; response to wounding [GO:0009611]
|
cytoplasm [GO:0005737]; nuclear speck [GO:0016607]
|
mRNA binding [GO:0003729]; protein kinase B binding [GO:0043422]; RNA binding [GO:0003723]; RS domain binding [GO:0050733]
|
PF00076;
|
3.30.70.330;
|
Splicing factor SR family
|
PTM: Extensively phosphorylated on serine residues in the RS domain. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: May be required for progression through G1 and entry into S phase of cell growth. May play a regulatory role in pre-mRNA splicing. Autoregulates its own expression. Plays a role in constitutive splicing and can modulate the selection of alternative splice sites (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O35331
|
PDXK_RAT
|
MEGECRVLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLTSQELHALYEGLKANNVNKYDYVLTGYTRDKSFLGMVVDIVQELKQQNSRLVYVCDPVMGDKWNGEGSMYVPQDLLPVYREKVVPMADIITPNQFEAELLSGRKIHSQEEAFAVMDVLHRMGPDTVVITSSDLPSPKGSDYLMALGSQRMRKPDGSTVTQRIRMEMRKVDPVFVGTGDLFAAMLLAWTHKHPDNLKVACEKTVSAMQHVLQRTIRCAKAEAGEGQKPSPAQLELRMVQSRKDIEDPEIVVQATVL
|
2.7.1.35
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P82197}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O00764};
|
negative regulation of apoptotic process [GO:0043066]; phosphorylation [GO:0016310]; pyridoxal 5'-phosphate salvage [GO:0009443]; pyridoxal metabolic process [GO:0042817]; pyridoxal phosphate biosynthetic process [GO:0042823]; pyridoxal phosphate metabolic process [GO:0042822]; pyridoxamine metabolic process [GO:0042818]; response to amine [GO:0014075]; response to food [GO:0032094]; response to insecticide [GO:0017085]; response to progesterone [GO:0032570]; response to toxic substance [GO:0009636]; response to X-ray [GO:0010165]; response to xenobiotic stimulus [GO:0009410]
|
cytosol [GO:0005829]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; organic cyclic compound binding [GO:0097159]; phosphotransferase activity, alcohol group as acceptor [GO:0016773]; pyridoxal binding [GO:0070280]; pyridoxal kinase activity [GO:0008478]; small molecule binding [GO:0036094]
|
PF08543;
|
3.40.1190.20;
|
Pyridoxine kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O00764}.
|
CATALYTIC ACTIVITY: Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326; EC=2.7.1.35; Evidence={ECO:0000250|UniProtKB:O00764}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10225; Evidence={ECO:0000250|UniProtKB:O00764}; CATALYTIC ACTIVITY: Reaction=ATP + pyridoxamine = ADP + H(+) + pyridoxamine 5'-phosphate; Xref=Rhea:RHEA:25104, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57761, ChEBI:CHEBI:58451, ChEBI:CHEBI:456216; EC=2.7.1.35; Evidence={ECO:0000250|UniProtKB:O00764}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25105; Evidence={ECO:0000250|UniProtKB:O00764}; CATALYTIC ACTIVITY: Reaction=ATP + pyridoxine = ADP + H(+) + pyridoxine 5'-phosphate; Xref=Rhea:RHEA:25108, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709, ChEBI:CHEBI:30616, ChEBI:CHEBI:58589, ChEBI:CHEBI:456216; EC=2.7.1.35; Evidence={ECO:0000250|UniProtKB:O00764}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25109; Evidence={ECO:0000250|UniProtKB:O00764};
| null |
PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxal: step 1/1. {ECO:0000250|UniProtKB:O00764}.; PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxine 5'-phosphate from pyridoxine: step 1/1. {ECO:0000250|UniProtKB:O00764}.; PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxamine 5'-phosphate from pyridoxamine: step 1/1. {ECO:0000250|UniProtKB:O00764}.
| null | null |
FUNCTION: Catalyzes the phosphorylation of the dietary vitamin B6 vitamers pyridoxal (PL), pyridoxine (PN) and pyridoxamine (PM) to form pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), respectively (By similarity). PLP is the active form of vitamin B6, and acts as a cofactor for over 140 different enzymatic reactions (By similarity). {ECO:0000250|UniProtKB:O00764}.
|
Rattus norvegicus (Rat)
|
O35343
|
IMA3_MOUSE
|
MADNEKLDNQRLKNFKNKGRDLETMRRQRNEVVVELRKNKRDEHLLKRRNVPQEDICEDSDIDGDYRVQNTSLEAIVQNASSDNQGIQLSAVQAARKLLSSDRNPPIDDLIKSGILPILVHCLERDDNPSLQFEAAWALTNIASGTSEQTQAVVQSNAVPLFLRLLHSPHQNVCEQAVWALGNIIGDGPQCRDYVISLGVVKPLLSFISPSIPITFLRNVTWVMVNLCRHKDPPPPMETIQEILPALCVLIHHTDVNILVDTVWALSYLTDAGNEQIQMVIDSGIVPHLVPLLSHQEVKVQTAALRAVGNIVTGTDEQTQVVLNCDALSHFPALLTHPKEKINKEAVWFLSNITAGNQQQVQAVIDANLVPMIIHLLDKGDFGTQKEAAWAISNLTISGRKDQVAYLIQQNVIPPFCNLLTVKDAQVVQVVLDGLSNILKMAEDQAETIANLIEECGGLEKIEQLQNHENEDIYKLAYEIIDQFFSSDDIDEDPSLVPESVQGGTFGFNSSTNVPTEGFQF
| null | null |
NLS-bearing protein import into nucleus [GO:0006607]; protein import into nucleus [GO:0006606]; response to hydrogen peroxide [GO:0042542]
|
cytosol [GO:0005829]; male germ cell nucleus [GO:0001673]; NLS-dependent protein nuclear import complex [GO:0042564]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139]
|
PF00514;PF16186;PF01749;
|
1.20.5.690;1.25.10.10;
|
Importin alpha family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
|
Mus musculus (Mouse)
|
O35345
|
IMA7_MOUSE
|
METMASPGKDNYRMKSYKNNALNPEEMRRRREEEGIQLRKQKREQQLFKRRNVELINEEAAMFDSLLMDSYVSSTTGESVITREMVEMLFSDDSDLQLATTQKFRKLLSKEPSPPIDEVINTPGVVDRFVEFLKRNENCTLQFEAAWALTNIASGTSQQTKIVIEAGAVPIFIELLNSDFEDVQEQAVWALGNIAGDSSLCRDYVLNCSILNPLLTLLTKSTRLTMTRNAVWALSNLCRGKNPPPEFAKVSPCLPVLSRLLFSSDSDLLADACWALSYLSDGPNEKIQAVIDSGVCRRLVELLMHNDYKVASPALRAVGNIVTGDDIQTQVILNCSALPCLLHLLSSSKESIRKEACWTISNITAGNRAQIQAVIDANIFPVLIEILQKAEFRTRKEAAWAITNATSGGTPEQIRYLVSLGCIKPLCDLLTVMDSKIVQVALNGLENILRLGEQESKRSGSGVNPYCGLIEEAYGLDKIEFLQSHENQEIYQKAFDLIEHYFGVEDDDSSLAPQVDETQQQFIFQQPEAPMEGFQL
| null | null |
entry of viral genome into host nucleus through nuclear pore complex via importin [GO:0075506]; maternal process involved in female pregnancy [GO:0060135]; NLS-bearing protein import into nucleus [GO:0006607]; positive regulation of cytokine production involved in inflammatory response [GO:1900017]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of viral life cycle [GO:1903902]; protein import into nucleus [GO:0006606]; symbiont-mediated perturbation of host defenses [GO:0030682]; transcription by RNA polymerase II [GO:0006366]; viral genome replication [GO:0019079]
|
cytosol [GO:0005829]; host cell [GO:0043657]; NLS-dependent protein nuclear import complex [GO:0042564]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139]
|
PF00514;PF16186;PF01749;
|
1.20.5.690;1.25.10.10;
|
Importin alpha family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
|
Mus musculus (Mouse)
|
O35346
|
FAK1_RAT
|
MAAAYLDPNLNHTPSSSTKTHLGTGTERSPGAMERVLKVFHYFESSNEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQDIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFNQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGATQSFIIRPQKEGERALPSIPKLANNEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGVYLSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKVQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQISGYPGSHGIPAMAGSIYPGQASLLDQTELWNHRPQEMSMWQPSVEDSAALDLRGMGQVLPPHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSFQGPTGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLSNLSSISSPAESYNEGVKPWRLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPILPASTHREIEMAQKLLNSDLGELISKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH
|
2.7.10.2
| null |
angiogenesis [GO:0001525]; axonogenesis [GO:0007409]; blood vessel development [GO:0001568]; cell migration [GO:0016477]; cellular response to transforming growth factor beta stimulus [GO:0071560]; central nervous system neuron axonogenesis [GO:0021955]; endothelial cell migration [GO:0043542]; ephrin receptor signaling pathway [GO:0048013]; epidermal growth factor receptor signaling pathway [GO:0007173]; extracellular matrix organization [GO:0030198]; fat cell differentiation [GO:0045444]; growth hormone receptor signaling pathway [GO:0060396]; integrin-mediated signaling pathway [GO:0007229]; intracellular chloride ion homeostasis [GO:0030644]; JNK cascade [GO:0007254]; MAPK cascade [GO:0000165]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of anoikis [GO:2000811]; negative regulation of apoptotic process [GO:0043066]; negative regulation of autophagy [GO:0010507]; negative regulation of axonogenesis [GO:0050771]; negative regulation of cell migration [GO:0030336]; negative regulation of cell-cell adhesion [GO:0022408]; negative regulation of organ growth [GO:0046621]; negative regulation of synapse assembly [GO:0051964]; neuron migration [GO:0001764]; nuclear migration [GO:0007097]; organ growth [GO:0035265]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell growth [GO:0030307]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of fibroblast migration [GO:0010763]; positive regulation of glial cell proliferation [GO:0060252]; positive regulation of macrophage chemotaxis [GO:0010759]; positive regulation of macrophage proliferation [GO:0120041]; positive regulation of phagocytosis [GO:0050766]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of synaptic transmission [GO:0050806]; positive regulation of ubiquitin-dependent protein catabolic process [GO:2000060]; positive regulation of wound healing [GO:0090303]; protein autophosphorylation [GO:0046777]; regulation of cell adhesion [GO:0030155]; regulation of cell adhesion mediated by integrin [GO:0033628]; regulation of cell population proliferation [GO:0042127]; regulation of cell shape [GO:0008360]; regulation of epithelial cell migration [GO:0010632]; regulation of focal adhesion assembly [GO:0051893]; regulation of modification of postsynaptic actin cytoskeleton [GO:1905274]; regulation of osteoblast differentiation [GO:0045667]; regulation of protein phosphorylation [GO:0001932]; regulation of substrate adhesion-dependent cell spreading [GO:1900024]; response to arsenic-containing substance [GO:0046685]; response to estradiol [GO:0032355]; response to glucose [GO:0009749]; response to mechanical stimulus [GO:0009612]; response to organic cyclic compound [GO:0014070]; response to organic substance [GO:0010033]; response to organonitrogen compound [GO:0010243]; response to xenobiotic stimulus [GO:0009410]; signal complex assembly [GO:0007172]; transforming growth factor beta receptor signaling pathway [GO:0007179]; vasculogenesis [GO:0001570]; vasodilation [GO:0042311]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell cortex [GO:0005938]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; intercalated disc [GO:0014704]; lamellipodium [GO:0030027]; nuclear body [GO:0016604]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; sarcolemma [GO:0042383]; stress fiber [GO:0001725]
|
actin binding [GO:0003779]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; JUN kinase binding [GO:0008432]; molecular function activator activity [GO:0140677]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphatase binding [GO:0019902]; phosphatidylinositol 3-kinase binding [GO:0043548]; protein kinase binding [GO:0019901]; protein phosphatase binding [GO:0019903]; protein tyrosine kinase activity [GO:0004713]; protein tyrosine phosphatase activity [GO:0004725]; protein-containing complex binding [GO:0044877]; SH2 domain binding [GO:0042169]
|
PF21477;PF00373;PF18038;PF03623;PF07714;
|
1.20.80.10;1.20.120.330;2.30.29.30;1.20.5.540;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, FAK subfamily
|
PTM: Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 and at additional tyrosine residues. FGR promotes phosphorylation at Tyr-397 and Tyr-576. FER promotes phosphorylation at Tyr-577, Tyr-861 and Tyr-928, even when cells are not adherent. Tyr-397, Tyr-576 and Ser-722 are phosphorylated only when cells are adherent. Phosphorylation at Tyr-397 is important for interaction with BMX, PIK3R1 and SHC1. Phosphorylation at Tyr-928 is important for interaction with GRB2. Dephosphorylated by PTPN11; PTPN11 is recruited to PTK2 via EPHA2 (tyrosine phosphorylated). Microtubule-induced dephosphorylation at Tyr-397 is crucial for the induction of focal adhesion disassembly; this dephosphorylation could be catalyzed by PTPN11 and regulated by ZFYVE21 (By similarity). Phosphorylation on tyrosine residues is enhanced by NTN1 (By similarity). {ECO:0000250|UniProtKB:P34152}.; PTM: Sumoylated; this enhances autophosphorylation. {ECO:0000269|PubMed:12732587, ECO:0000269|PubMed:14500712, ECO:0000269|PubMed:16373587}.
|
SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q00944}. Cell membrane {ECO:0000250|UniProtKB:Q00944}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q00944}; Cytoplasmic side {ECO:0000250|UniProtKB:Q00944}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q00944}. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12732587}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus {ECO:0000269|PubMed:12732587, ECO:0000269|PubMed:14500712, ECO:0000269|PubMed:16373587}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q05397}. Cytoplasm {ECO:0000269|PubMed:16373587}. Note=Constituent of focal adhesions. Detected at microtubules. {ECO:0000250|UniProtKB:P34152}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Phosphorylates NEDD9 following integrin stimulation (By similarity). Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. {ECO:0000250|UniProtKB:P34152, ECO:0000250|UniProtKB:Q05397, ECO:0000269|PubMed:15494733}.; FUNCTION: [Isoform 2]: Does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription (By similarity). {ECO:0000250|UniProtKB:Q05397}.
|
Rattus norvegicus (Rat)
|
O35350
|
CAN1_MOUSE
|
MTEELITPVYCTGVSAQVQKKRDKELGLGRHENAIKYLGQDYETLRARCLQSGVLFQDEAFPPVSHSLGFKELGPHSSKTYGIKWKRPTELMSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNETILHRVVPYGQSFQDGYAGIFHFQLWQFGEWVDVVIDDLLPTKDGKLVFVHSAQGNEFWSALLEKAYAKVNGSYEALSGGCTSEAFEDFTGGVTEWYDLQKAPSDLYQIILKALERGSLLGCSINISDIRDLEAITFKNLVRGHAYSVTGAKQVTYQGQRVNLIRMRNPWGEVEWKGPWSDSSYEWNKVDPYEREQLRVKMEDGEFWMSFRDFIREFTKLEICNLTPDALKSRTLRNWNTTFYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLEEVDDADDYDNRESGCSFLLALMQKHRRRERRFGRDMETIGFAVYQVPRELAGQPVHLKRDFFLANASRAQSEHFINLREVSNRIRLPPGEYIVVPSTFEPNKEGDFLLRFFSEKKAGTQELDDQIQANLPDEKVLSEEEIDDNFKTLFSKLAGDDMEISVKELQTILNRIISKHKDLRTNGFSLESCRSMVNLMDRDGNGKLGLVEFNILWNRIRNYLTIFRKFDLDKSGSMSAYEMRMAIEAAGFKLNKKLHELIITRYSEPDLAVDFDNFVCCLVRLETMFRFFKLLDTDLDGVVTFDLFKWLQLTMFA
|
3.4.22.52
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P07384}; Note=Binds 4 Ca(2+) ions. {ECO:0000250|UniProtKB:P07384};
|
cellular response to hydrogen peroxide [GO:0070301]; mammary gland involution [GO:0060056]; negative regulation of actin filament polymerization [GO:0030837]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; positive regulation of leukocyte tethering or rolling [GO:1903238]; positive regulation of vascular permeability [GO:0043117]; protein autoprocessing [GO:0016540]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]; receptor catabolic process [GO:0032801]; regulation of catalytic activity [GO:0050790]; response to angiotensin [GO:1990776]; self proteolysis [GO:0097264]
|
calpain complex [GO:0110158]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; lysosome [GO:0005764]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; cytoskeletal protein binding [GO:0008092]; enzyme binding [GO:0019899]
|
PF01067;PF13833;PF00648;
|
2.60.120.380;3.90.70.10;1.10.238.10;
|
Peptidase C2 family
|
PTM: Undergoes calcium-induced successive autoproteolytic cleavages that generate a membrane-bound 78 kDa active form and an intracellular 75 kDa active form. Calpastatin reduces with high efficiency the transition from 78 kDa to 75 kDa calpain forms (By similarity). {ECO:0000250|UniProtKB:P07384}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07384}. Cell membrane {ECO:0000250|UniProtKB:P07384}. Note=Translocates to the plasma membrane upon Ca(2+) binding. {ECO:0000250|UniProtKB:P07384}.
|
CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.52; Evidence={ECO:0000250|UniProtKB:P07384};
| null | null | null | null |
FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves CTBP1 at 'Asn-375', 'Gly-388' and 'His-410'. Cleaves and activates caspase-7 (CASP7). {ECO:0000250|UniProtKB:P07384}.
|
Mus musculus (Mouse)
|
O35375
|
NRP2_MOUSE
|
MDMFPLTWVFLALYFSGHEVRSQQDPPCGGRLNSKDAGYITSPGYPQDYPSHQNCEWIVYAPEPNQKIVLNFNPHFEIEKHDCKYDFIEIRDGDSESADLLGKHCGNIAPPTIISSGSVLYIKFTSDYARQGAGFSLRYEIFKTGSEDCSKNFTSPNGTIESPGFPEKYPHNLDCTFTILAKPRMEIILQFLTFDLEHDPLQVGEGDCKYDWLDIWDGIPHVGPLIGKYCGTKTPSKLRSSTGILSLTFHTDMAVAKDGFSARYYLIHQEPPENFQCNVPLGMESGRIANEQISASSTFSDGRWTPQQSRLHGDDNGWTPNLDSNKEYLQVDLRFLTMLTAIATQGAISRETQKGYYVKSYKLEVSTNGEDWMVYRHGKNHKIFQANNDATEVVLNKLHMPLLTRFIRIRPQTWHLGIALRLELFGCRVTDAPCSNMLGMLSGLIADTQISASSTREYLWSPSAARLVSSRSGWFPRNPQAQPGEEWLQVDLGTPKTVKGVIIQGARGGDSITAVEARAFVRKFKVSYSLNGKDWEYIQDPRTQQTKLFEGNMHYDTPDIRRFDPVPAQYVRVYPERWSPAGIGMRLEVLGCDWTDSKPTVETLGPTVKSEETTTPYPMDEDATECGENCSFEDDKDLQLPSGFNCNFDFPEETCGWVYDHAKWLRSTWISSANPNDRTFPDDKNFLKLQSDGRREGQYGRLISPPVHLPRSPVCMEFQYQAMGGHGVALQVVREASQESKLLWVIREDQGSEWKHGRIILPSYDMEYQIVFEGVIGKGRSGEISIDDIRISTDVPLENCMEPISAFAGEDFKVDIPETHGGEGYEDEIDDEYEGDWSNSSSSTSGAGDPSSGKEKSWLYTLDPILITIIAMSSLGVLLGATCAGLLLYCTCSYSGLSSRSCTTLENYNFELYDGLKHKVKINHQKCCSEA
| null | null |
angiogenesis [GO:0001525]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; cellular response to leukemia inhibitory factor [GO:1990830]; dorsal root ganglion morphogenesis [GO:1904835]; facial nerve structural organization [GO:0021612]; facioacoustic ganglion development [GO:1903375]; gonadotrophin-releasing hormone neuronal migration to the hypothalamus [GO:0021828]; heart development [GO:0007507]; negative chemotaxis [GO:0050919]; nerve development [GO:0021675]; neural crest cell migration involved in autonomic nervous system development [GO:1901166]; neuron migration [GO:0001764]; outflow tract septum morphogenesis [GO:0003148]; regulation of postsynapse organization [GO:0099175]; semaphorin-plexin signaling pathway [GO:0071526]; sensory neuron axon guidance [GO:0097374]; sympathetic ganglion development [GO:0061549]; sympathetic neuron projection extension [GO:0097490]; sympathetic neuron projection guidance [GO:0097491]; trigeminal ganglion development [GO:0061551]; trunk neural crest cell migration [GO:0036484]; ventral trunk neural crest cell migration [GO:0036486]; vestibulocochlear nerve structural organization [GO:0021649]
|
axon [GO:0030424]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]
|
heparin binding [GO:0008201]; metal ion binding [GO:0046872]; semaphorin receptor activity [GO:0017154]; vascular endothelial growth factor receptor activity [GO:0005021]
|
PF00431;PF11980;PF00754;PF00629;
|
2.60.120.200;2.60.120.260;2.60.120.290;
|
Neuropilin family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O60462}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O60462}.
| null | null | null | null | null |
FUNCTION: High affinity receptor for semaphorins 3C, 3F, VEGF-165 and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF.
|
Mus musculus (Mouse)
|
O35379
|
MRP1_MOUSE
|
MALRSFCSADGSDPLWDWNVTWHTSNPDFTKCFQNTVLTWVPCFYLWSCFPLYFFYLSRHDRGYIQMTHLNKTKTALGFFLWIICWADLFYSFWERSQGVLRAPVLLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALLCALAILRSKIISALKKDAHVDVFRDSTFYLYFTLVLVQLVLSCFSDCSPLFSETVHDRNPCPESSASFLSRITFWWITGMMVHGYRQPLESSDLWSLNKEDTSEEVVPVLVNNWKKECDKSRKQPVRIVYAPPKDPSKPKGSSQLDVNEEVEALIVKSPHKDREPSLFKVLYKTFGPYFLMSFLYKALHDLMMFAGPKILELIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVFVTVDERNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRSIKSGEGNSITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNDSLRENILFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLRTYANAEQDLASEDDSVSGSGKESKPVENGMLVTDTVGKHLQRHLSNSSSHSGDTSQQHSSIAELQKAGAKEETWKLMEADKAQTGQVQLSVYWNYMKAIGLFITFLSIFLFLCNHVSALASNYWLSLWTDDPPVVNGTQANRNFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSTWPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSMAKDAGLV
|
7.6.2.2; 7.6.2.3
| null |
astrocyte differentiation [GO:0048708]; cell chemotaxis [GO:0060326]; cellular response to amyloid-beta [GO:1904646]; cobalamin transport [GO:0015889]; cyclic nucleotide transport [GO:0070729]; export across plasma membrane [GO:0140115]; glial cell differentiation [GO:0010001]; glutathione transmembrane transport [GO:0034775]; leukotriene transport [GO:0071716]; long-chain fatty acid import across plasma membrane [GO:0015911]; phospholipid efflux [GO:0033700]; phospholipid translocation [GO:0045332]; positive regulation of cell migration [GO:0030335]; positive regulation of inflammatory response [GO:0050729]; regulation of cellular response to drug [GO:2001038]; response to oxidative stress [GO:0006979]; response to xenobiotic stimulus [GO:0009410]; sphingolipid translocation [GO:0099039]; transepithelial transport [GO:0070633]; transmembrane transport [GO:0055085]; xenobiotic detoxification by transmembrane export across the plasma membrane [GO:1990961]; xenobiotic transport [GO:0042908]; xenobiotic transport across blood-brain barrier [GO:1990962]
|
apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; lateral plasma membrane [GO:0016328]; plasma membrane [GO:0005886]
|
ABC-type glutathione S-conjugate transporter activity [GO:0015431]; ABC-type transporter activity [GO:0140359]; ABC-type vitamin B12 transporter activity [GO:0015420]; ABC-type xenobiotic transporter activity [GO:0008559]; amide transmembrane transporter activity [GO:0042887]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled lipid transmembrane transporter activity [GO:0034040]; carboxylic acid transmembrane transporter activity [GO:0046943]; efflux transmembrane transporter activity [GO:0015562]; glutathione transmembrane transporter activity [GO:0034634]; long-chain fatty acid transporter activity [GO:0005324]; xenobiotic transmembrane transporter activity [GO:0042910]
|
PF00664;PF00005;
|
1.20.1560.10;3.40.50.300;
|
ABC transporter superfamily, ABCC family, Conjugate transporter (TC 3.A.1.208) subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000269|PubMed:9359705}; CATALYTIC ACTIVITY: Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-substituted glutathione(out) + H(+) + phosphate; Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779, ChEBI:CHEBI:456216; EC=7.6.2.3; Evidence={ECO:0000269|PubMed:9359705}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122; Evidence={ECO:0000269|PubMed:9359705}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57973, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:9281595, ECO:0000269|PubMed:9359705}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964; Evidence={ECO:0000269|PubMed:9281595}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + sphing-4-enine 1-phosphate(in) = ADP + H(+) + phosphate + sphing-4-enine 1-phosphate(out); Xref=Rhea:RHEA:38951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:60119, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P33527}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38952; Evidence={ECO:0000250|UniProtKB:P33527}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O = 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60128, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:82961, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P33527}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129; Evidence={ECO:0000250|UniProtKB:P33527}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + vincristine(in) = ADP + H(+) + phosphate + vincristine(out); Xref=Rhea:RHEA:60160, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143658, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:9281595}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60161; Evidence={ECO:0000269|PubMed:9281595}; CATALYTIC ACTIVITY: Reaction=ATP + daunorubicin(in) + H2O = ADP + daunorubicin(out) + H(+) + phosphate; Xref=Rhea:RHEA:33147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64677, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P33527}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33148; Evidence={ECO:0000250|UniProtKB:P33527}; CATALYTIC ACTIVITY: Reaction=2',3'-cGAMP(in) + ATP + H2O = 2',3'-cGAMP(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:74887, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143093, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:36070769};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=60 nM for leukotriene C4 {ECO:0000269|PubMed:9281595}; KM=3.3 nM for S-(2,4-dinitrophenyl)glutathione {ECO:0000269|PubMed:9359705}; Vmax=350 pmol/min/mg enzyme for leukotriene C4 transport {ECO:0000269|PubMed:9281595};
| null | null | null |
FUNCTION: Mediates export of organic anions and drugs from the cytoplasm. Mediates ATP-dependent transport of glutathione and glutathione conjugates, leukotriene C4, estradiol-17-beta-o-glucuronide, methotrexate, antiviral drugs and other xenobiotics. Confers resistance to anticancer drugs by decreasing accumulation of drug in cells, and by mediating ATP- and GSH-dependent drug export (PubMed:9281595, PubMed:9359705). Hydrolyzes ATP with low efficiency. Catalyzes the export of sphingosine 1-phosphate from mast cells independently of their degranulation (By similarity). Participates in inflammatory response by allowing export of leukotriene C4 from leukotriene C4-synthezing cells (PubMed:9359705). Mediates ATP-dependent, GSH-independent cyclic GMP-AMP (cGAMP) export (PubMed:36070769). Thus, by limiting intracellular cGAMP concentrations negatively regulates the cGAS-STING pathway (PubMed:36070769). {ECO:0000250|UniProtKB:P33527, ECO:0000269|PubMed:36070769, ECO:0000269|PubMed:9281595, ECO:0000269|PubMed:9359705}.
|
Mus musculus (Mouse)
|
O35381
|
AN32A_MOUSE
|
MEMDKRIYLELRNRTPSDVKELVLDNCKSIEGKIEGLTDEFEELEFLSTINVGLTSISNLPKLNKLKKLELSENRISGDLEVLAEKCPNLKHLNLSGNKIKDLSTIEPLKKLENLKSLDLFNCEVTNLNAYRENVFKLLPQVMYLDGYDRDNKEAPDSDVEGYVEDDDEEDEDEEEYDEYAQLVEDEEEEDEEEEGEEEDVSGEEEEDEEGYNDGEVDDEEDEEEAGEEEGSQKRKREPDDEGEEDD
| null | null |
nucleocytoplasmic transport [GO:0006913]; regulation of apoptotic process [GO:0042981]
|
cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
histone binding [GO:0042393]
|
PF14580;
|
3.80.10.10;
|
ANP32 family
|
PTM: Phosphorylated on serine residues, at least in part by casein kinase 2/CK2. {ECO:0000250|UniProtKB:P39687}.; PTM: Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12807913}. Cytoplasm {ECO:0000269|PubMed:12807913}. Endoplasmic reticulum {ECO:0000250}. Note=Shuttles between nucleus and cytoplasm. Translocates to the cytoplasm during the process of neuritogenesis.
| null | null | null | null | null |
FUNCTION: Multifunctional protein that is involved in the regulation of many processes including tumor suppression, apoptosis, cell cycle progression or transcription. Promotes apoptosis by favouring the activation of caspase-9/CASP9 and allowing apoptosome formation. In addition, plays a role in the modulation of histone acetylation and transcription as part of the INHAT (inhibitor of histone acetyltransferases) complex. Inhibits the histone-acetyltranferase activity of EP300/CREBBP (CREB-binding protein) and EP300/CREBBP-associated factor by histone masking. Preferentially binds to unmodified histone H3 and sterically inhibiting its acetylation and phosphorylation leading to cell growth inhibition (PubMed:29467488). Participates in other biochemical processes such as regulation of mRNA nuclear-to-cytoplasmic translocation and stability by its association with ELAVL1 (Hu-antigen R). Plays a role in E4F1-mediated transcriptional repression as well as inhibition of protein phosphatase 2A (By similarity) (PubMed:17557114, PubMed:29467488). {ECO:0000250|UniProtKB:P39687, ECO:0000269|PubMed:17557114, ECO:0000269|PubMed:29467488}.
|
Mus musculus (Mouse)
|
O35382
|
EXOC4_MOUSE
|
MAAEAAGGKYRSTVSKSKDPSGLLISVIRTLSTSDDVEDRENEKGRLEEAYEKCDRDLDELIVQHYTELTTAIRTYQSITERITNSRNKIKQVKENLLSCKMLLHCKRDELRKLWIEGIEHKHVLNLLDEIENIKQVPQKLEQCMASKHYLSATDMLVSAVESLEGPLLQVEGLSDLRLELHSKKMNLHLVLIEELHRHLYIKSTSRVVQRNKEKGKMSSHGKDPSPGPLIDVSNIPTPRKFLDASQYSAAGGSSVREMNLQDVKEDLECDPEENSTLFMGILIQGLARLKKIPETVKAIKERLEQELKQIVKRSTTQVADSAYQRGESLTVDNQPRLLLELLELLFDKFNAVATAHSVVLGYLQDSVGTQLTQQEEIKLYDMADVWVKIQDVLQMLLTEYLDMKNTRTASEPSAQLSYASTGREFAAFFAKKKPQRPKNSLFKFESSSHAISMSAYLREQRRELYSRSGELQGGPDDNLIEGGGTKFVCKPGARNITVIFHPLLRFIQEIEHALGLGPAKQCPLREFLTVYIKSIFLNQVLAEINKEIEGVTKTSDPLKILANADTMKVLGVQRPLLQSTIIVEKTVQDLMNLMHDLSAYSDQFLNMVCVKLQEYKDTCSTAYRGIVQSEEKLVISASWAKDDDISRLLKSLPNWTNMAQPKQLRPKREEEEDFIRAAFGKESEVLIGNLGDKLIPPQDILRDVSDLKALANMHESLEWLAGRTKSAFSNLSTSQMLSPAQESHVNMDLPPVSEQIMQTLSELAKTFQDMADRCLLVLHLEVRVHCFHYLIPLAKEGNYAIVANVESMDYDPLVVKLNKDISAMEEAMSASLQQHKFQYIFEGLGHLISCILINGAQYFRRISESGIKKMCRNIFVLQQNLTNITMSREADLDFARQYYEMLYNTADELLNLVVDQGVKYTELEYIHALTLLHRSQTGVGDQTTQNTRLQRLKEIICEQAAIKQATKDKKITTV
| null | null |
chemical synaptic transmission [GO:0007268]; establishment of cell polarity [GO:0030010]; exocytosis [GO:0006887]; Golgi to plasma membrane transport [GO:0006893]; Golgi to transport vesicle transport [GO:0055108]; membrane biogenesis [GO:0044091]; membrane fission [GO:0090148]; mitotic cytokinesis [GO:0000281]; oligodendrocyte differentiation [GO:0048709]; paraxial mesoderm formation [GO:0048341]; positive regulation of calcium-mediated signaling [GO:0050850]; protein targeting to membrane [GO:0006612]; protein transmembrane transport [GO:0071806]; regulation of protein transport [GO:0051223]; vesicle docking involved in exocytosis [GO:0006904]; vesicle tethering involved in exocytosis [GO:0090522]
|
cell leading edge [GO:0031252]; centrosome [GO:0005813]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; exocyst [GO:0000145]; Flemming body [GO:0090543]; growth cone [GO:0030426]; growth cone membrane [GO:0032584]; microvillus [GO:0005902]; myelin sheath abaxonal region [GO:0035748]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic density, intracellular component [GO:0099092]; protein-containing complex [GO:0032991]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]
|
ionotropic glutamate receptor binding [GO:0035255]; PDZ domain binding [GO:0030165]; protein-containing complex binding [GO:0044877]
|
PF20652;PF04048;
| null |
SEC8 family
| null |
SUBCELLULAR LOCATION: Midbody, Midbody ring {ECO:0000250|UniProtKB:Q96A65}. Cell projection {ECO:0000250|UniProtKB:Q62824}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96A65}. Note=Colocalizes with CNTRL/centriolin at the midbody ring (By similarity). Localizes at the leading edge of migrating cells (By similarity). {ECO:0000250|UniProtKB:Q62824, ECO:0000250|UniProtKB:Q96A65}.
| null | null | null | null | null |
FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250|UniProtKB:Q62824}.
|
Mus musculus (Mouse)
|
O35385
|
PPE2_MOUSE
|
MGSSSSTQHHFAFQNAEKAFKAAALIQRWYRRYMARLEMRRRCTWNIFQSIEYAGQQDQVKLHEFFSYLVDHFTPSSHHERDFLNRMFTEERFAQDVETEEGGDFESIEVPDSYTGPRLSFPLLPDHATALVEAFRLRQQLHARYVLNLLYETRKHLAQLPNINRVSTCYSEEVTVCGDLHGQLDDLIFIFYKNGLPSPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYKIHGKKILRTLQDVFCWLPLATLVDEKVLVLHGGVSDKTDLELLAKLDRHKIVSTMRCKTRKESENREEQKRKDNQTSSGQKPTPWFLPQSRSLPSSPFHLGSGFKAYKAGRSCSIPCGSPNSKELSRRGQVRRSVDLELEQCRQQAGFLGIREKGESLPLAPDADCVADGGGVLEPTPEEWKQVVDILWSDPAAQEGCKANAVRGGGCYFGPDVTERLMEKYKLQLLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPALTPHIVQYQANKATHRLTMRQRISRVEESALRALRQKLFAHSSDLLVEFRKRDPDESGVITLSDWATAVESVLHLGLPWRMLRPQLVNSSADNVLEYRSWLDSLAKEQLSRENIQSSLLEKLYRNRSNLETIFRIIDSDHSGFISLDEFRQTWKLFSSHMSIDITDDGICDLARSIDFNKDGHIDINEFLEAFRLVEQSCLEGHASACLQSTDTAESGHSSPGPC
|
3.1.3.16
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250};
|
detection of stimulus involved in sensory perception [GO:0050906]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; visual perception [GO:0007601]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
calcium ion binding [GO:0005509]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; iron ion binding [GO:0005506]; manganese ion binding [GO:0030145]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]
|
PF13499;PF00149;PF08321;
|
3.60.21.10;1.10.238.10;
|
PPP phosphatase family
| null | null |
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16;
| null | null | null | null |
FUNCTION: May play a role in phototransduction. May dephosphorylate photoactivated rhodopsin. May function as a calcium sensing regulator of ionic currents, energy production or synaptic transmission.
|
Mus musculus (Mouse)
|
O35386
|
PAHX_MOUSE
|
MNLTRAGARLQVLLGHLGRPSAPTIVAQPVSGLASPASFQPEQFQYTLDNNVLTLEQRKFYEENGFLVIKNLVSDDDIQRFRAEFERICREEVKPPGIVIMRDVALAKQDYMPSDRMVSKIQDFQEDEELFRYCLLPEILKYVECFTGPNIMALHGMLINKPPDVGKKTSRHPLHQDLHYFPFRPSNLIVCAWTAMEHIDRNNGCLVVLPGTHKGTLKPHDYPKWEGGVNKMYHGIQDYDPNSPRVHLVMEKGDTVFFHPLLIHGSGRNKTQGFRKAISCHFGSSDCQCIDVSGTSQENIAREVVEMAEKKYGFQGVMDFKDTWIFRSRLVKGERINI
|
1.14.11.18
|
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:O14832}; COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:O14832}; COFACTOR: Name=ATP; Xref=ChEBI:CHEBI:30616; Evidence={ECO:0000250|UniProtKB:O14832}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O14832};
|
2-oxobutyrate catabolic process [GO:0019606]; 2-oxoglutarate metabolic process [GO:0006103]; fatty acid alpha-oxidation [GO:0001561]; isoprenoid metabolic process [GO:0006720]; methyl-branched fatty acid metabolic process [GO:0097089]
|
9+0 non-motile cilium [GO:0097731]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]
|
catalytic activity [GO:0003824]; ferrous iron binding [GO:0008198]; L-ascorbic acid binding [GO:0031418]; phytanoyl-CoA dioxygenase activity [GO:0048244]
|
PF05721;
|
2.60.120.620;
|
PhyH family
| null |
SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:O14832}.
|
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + phytanoyl-CoA = 2-hydroxyphytanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:16065, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57334, ChEBI:CHEBI:57391; EC=1.14.11.18; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16066; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 3-methylhexadecanoyl-CoA + O2 = 2-hydroxy-3-methylhexadecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:44000, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:58784, ChEBI:CHEBI:83969; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44001; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + hexadecanoyl-CoA + O2 = 2-hydroxyhexadecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54596, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57379, ChEBI:CHEBI:74115; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54597; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + octanoyl-CoA = 2-hydroxyoctanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54600, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57386, ChEBI:CHEBI:138290; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54601; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + decanoyl-CoA + O2 = 2-hydroxydecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54604, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:61430, ChEBI:CHEBI:138292; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54605; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 3-methylbutanoyl-CoA + O2 = 2-hydroxy-3-methylbutanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54612, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57345, ChEBI:CHEBI:138296; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54613; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + heptadecanoyl-CoA + O2 = 2-hydroxyheptadecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54616, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:74307, ChEBI:CHEBI:138297; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54617; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + eicosanoyl-CoA + O2 = 2-hydroxyeicosanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54620, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57380, ChEBI:CHEBI:138298; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54621; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + octadecanoyl-CoA = 2-hydroxyoctadecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54624, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57394, ChEBI:CHEBI:74116; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54625; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + dodecanoyl-CoA + O2 = 2-hydroxydodecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54628, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57375, ChEBI:CHEBI:138299; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54629; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + tetradecanoyl-CoA = 2-hydroxytetradecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54632, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57385, ChEBI:CHEBI:138300; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54633; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + hexanoyl-CoA + O2 = 2-hydroxyhexanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55172, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:62620, ChEBI:CHEBI:138630; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55173; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + butanoyl-CoA + O2 = 2-hydroxybutanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55176, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57371, ChEBI:CHEBI:138628; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55177; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 3-methylnonanoyl-CoA + O2 = 2-hydroxy-3-methylnonanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55180, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:138633, ChEBI:CHEBI:138634; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55181; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 3-methylundecanoyl-CoA + O2 = 2-hydroxy-3-methylundecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55184, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:84183, ChEBI:CHEBI:138632; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55185; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 3-methyldodecanoyl-CoA + O2 = 2-hydroxy-3-methyldodecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55192, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:138636, ChEBI:CHEBI:138637; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55193; Evidence={ECO:0000250|UniProtKB:O14832};
| null |
PATHWAY: Lipid metabolism; fatty acid metabolism.
| null | null |
FUNCTION: Catalyzes the 2-hydroxylation of not only racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono-branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon atoms) (By similarity). Does not hydroxylate long and very long straight chain acyl-CoAs or 2-methyl-and 4-methyl-branched acyl-CoAs (By similarity). {ECO:0000250|UniProtKB:O14832}.
|
Mus musculus (Mouse)
|
O35387
|
HAX1_MOUSE
|
MSVFDLFRGFFGFPGPRSHRDPFFGGMTRDDDDDDDDDDEAEEDRGAWGRESYAFDGSQPPEEFGFSFSPRGGMRFHGNFGFDDLVRDFNSIFSEMGAWTLPSHSPELPGPESETPGERLREGQTLRDSMLKYPDSHQPRIFEGVLESHAKPESPKPAPDWGSQGPFHRLDDTWPVSPHSRAKEDKDLDSQVSQEGLGPLLQPQPKSYFKSISVTKITKPDGTVEERRTVVDSEGRRETTVTHQEAHDSSRSDPDSQRSSALDDPFSILDLLLGRWFRSR
| null | null |
cell surface receptor signaling pathway [GO:0007166]; granulocyte colony-stimulating factor signaling pathway [GO:0038158]; negative regulation of apoptotic process [GO:0043066]; positive regulation of granulocyte differentiation [GO:0030854]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of actin filament polymerization [GO:0030833]
|
actin cytoskeleton [GO:0015629]; apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; lamellipodium [GO:0030027]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]; P-body [GO:0000932]; sarcoplasmic reticulum [GO:0016529]; transcription regulator complex [GO:0005667]
|
interleukin-1 binding [GO:0019966]; protein domain specific binding [GO:0019904]; signaling adaptor activity [GO:0035591]
| null | null |
HAX1 family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:16814492, ECO:0000269|PubMed:26915802}. Endoplasmic reticulum {ECO:0000269|PubMed:10760273}. Nucleus membrane {ECO:0000305|PubMed:16814492}. Cytoplasmic vesicle {ECO:0000269|PubMed:10760273, ECO:0000269|PubMed:16814492}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:O00165}. Cell membrane {ECO:0000250|UniProtKB:O00165}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00165}; Cytoplasmic side {ECO:0000250|UniProtKB:O00165}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q7TSE9}. Cytoplasm, P-body {ECO:0000250|UniProtKB:O00165}. Cytoplasm {ECO:0000250|UniProtKB:O00165}. Nucleus {ECO:0000250|UniProtKB:O00165}. Note=Predominantly cytoplasmic. Also detected in the nucleus when nuclear export is inhibited (in vitro). {ECO:0000250|UniProtKB:O00165}.
| null | null | null | null | null |
FUNCTION: Recruits the Arp2/3 complex to the cell cortex and regulates reorganization of the cortical actin cytoskeleton via its interaction with KCNC3 and the Arp2/3 complex. Slows down the rate of inactivation of KCNC3 channels. Promotes GNA13-mediated cell migration. Involved in the clathrin-mediated endocytosis pathway. May be involved in internalization of ABC transporters such as ABCB11. May inhibit CASP9 and CASP3. Promotes cell survival. May regulate intracellular calcium pools. {ECO:0000250|UniProtKB:O00165}.
|
Mus musculus (Mouse)
|
O35393
|
EFNB3_MOUSE
|
MGAPHFGPGGVQVGALLLLGFAGLVSGLSLEPVYWNSANKRFQAEGGYVLYPQIGDRLDLLCPRARPPGPHSSPSYEFYKLYLVEGAQGRRCEAPPAPNLLLTCDRPDLDLRFTIKFQEYSPNLWGHEFRSHHDYYIIATSDGTREGLESLQGGVCLTRGMKVLLRVGQSPRGGAVPRKPVSEMPMERDRGAAHSAEPGRDTIPGDPSSNATSRGAEGPLPPPSMPAVAGAAGGMALLLLGVAGAGGAMCWRRRRAKPSESRHPGPGSFGRGGSLGLGGGGGMGPREAEPGELGIALRGGGTADPPFCPHYEKVSGDYGHPVYIVQDGPPQSPPNIYYKV
| null | null |
adult walking behavior [GO:0007628]; axon choice point recognition [GO:0016198]; axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; negative regulation of axonogenesis [GO:0050771]; positive regulation of presynapse assembly [GO:1905608]; positive regulation of synaptic transmission [GO:0050806]; T cell costimulation [GO:0031295]; trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission [GO:0099557]
|
glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynaptic membrane [GO:0042734]
|
ephrin receptor binding [GO:0046875]
|
PF00812;
|
2.60.40.420;
|
Ephrin family
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. May play a pivotal role in forebrain function. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons. {ECO:0000269|PubMed:10704386}.
|
Mus musculus (Mouse)
|
O35394
|
PRAF1_RAT
|
MAAQKDQQKDAEVEGLSATTLLPKLIPSGAGREWLERRRATIRPWGTFVDQQRFSRPRNVGELCQRLVRNVEYYQSNYVFVFLGLILYCVVTSPMLLVALAVFFGACYILYLRTLQSKLVLFGREVSPAHQYALAGGVSFPFFWLAGAGSAVFWVLGATLVLIGSHAAFHQIEPADGEELQMEPV
| null | null |
vesicle-mediated transport [GO:0016192]
|
endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; plasma membrane [GO:0005886]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]
|
GTPase binding [GO:0051020]; identical protein binding [GO:0042802]; proline-rich region binding [GO:0070064]; protein-macromolecule adaptor activity [GO:0030674]
|
PF03208;
| null |
PRA1 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10751420}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:10751420}. Golgi apparatus {ECO:0000269|PubMed:10751420, ECO:0000269|PubMed:11096102, ECO:0000269|PubMed:12107180}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:10707984}. Note=According to some authors, it is an integral membrane protein, while others showed that it is cytoplasmic and membrane-associated to Golgi (PubMed:10751420, PubMed:12107180, PubMed:11096102) and synaptic vesicles (PubMed:10707984). {ECO:0000269|PubMed:10707984, ECO:0000269|PubMed:10751420, ECO:0000269|PubMed:11096102, ECO:0000269|PubMed:12107180}.
| null | null | null | null | null |
FUNCTION: General Rab protein regulator required for vesicle formation from the Golgi complex. May control vesicle docking and fusion by mediating the action of Rab GTPases to the SNARE complexes. In addition it inhibits the removal of Rab GTPases from the membrane by GDI1. {ECO:0000269|PubMed:10751420, ECO:0000269|PubMed:12107180, ECO:0000269|PubMed:9341137}.
|
Rattus norvegicus (Rat)
|
O35397
|
CASP6_RAT
|
MTETDGFYRSREVLDPAEQYKMDHKRRGTALIFNHERFFWHLALPERRGTNADRDNPTRRFSELGFEVKCFNDLRAEELLLKIHEVSTSSHVDADCFLCVFLSHGEGNHIYAYDAKIEIQTLTGLFKGDKCQSLVGKPKIFIIQACRGSQHDVPLVPLDVVDHQTDKLDDNVTQVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLSEMLARHGSSLEFTELLTLVNRKVSQRRVDFCKDPGAIGKKQVPCFASMLTKKLHFCPKPSK
|
3.4.22.59
| null |
activation of innate immune response [GO:0002218]; acute inflammatory response to non-antigenic stimulus [GO:0002525]; axonal fasciculation [GO:0007413]; cellular response to staurosporine [GO:0072734]; epithelial cell differentiation [GO:0030855]; hepatocyte apoptotic process [GO:0097284]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; lens development in camera-type eye [GO:0002088]; positive regulation of apoptotic process [GO:0043065]; positive regulation of necroptotic process [GO:0060545]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of retinal cell programmed cell death [GO:0046670]; protein autoprocessing [GO:0016540]; proteolysis [GO:0006508]; pyroptosis [GO:0070269]; regulation of programmed cell death [GO:0043067]; response to cytokine [GO:0034097]; response to estradiol [GO:0032355]; response to gamma radiation [GO:0010332]; response to glucose [GO:0009749]; response to hydrogen peroxide [GO:0042542]; response to iron ion [GO:0010039]; response to metal ion [GO:0010038]; response to organic substance [GO:0010033]; response to organonitrogen compound [GO:0010243]; response to testosterone [GO:0033574]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]
|
cysteine-type endopeptidase activity [GO:0004197]; cysteine-type endopeptidase activity involved in apoptotic process [GO:0097153]; cysteine-type endopeptidase activity involved in execution phase of apoptosis [GO:0097200]; endopeptidase activity [GO:0004175]; identical protein binding [GO:0042802]
|
PF00656;
|
3.40.50.1460;
|
Peptidase C14A family
|
PTM: Phosphorylated by NUAK1; phosphorylation inhibits self-activation. Phosphorylation at Ser-240 by AMP-activated protein kinase (PRKAA1 or PRKAA2) inhibits autocleavage, preventing caspase activation, thereby preventing hepatocyte apoptosis. {ECO:0000250|UniProtKB:P55212}.; PTM: Palmitoylation by ZDHHC17 blocks dimerization and subsequent activation, leading to inhibit the cysteine protease activity. {ECO:0000250|UniProtKB:P55212}.; PTM: Can be cleaved and activated by different caspases, depending on the context. Cleaved and activated by caspase-8 (CASP8) and subsequently by caspase-3 (CASP3). Can also undergo autoactivation by mediating autocleavage at Asp-162 and Asp-176, while it is not able to cleave its N-terminal disordered prodomain. Cleaved and activated by CASP1, possibly in the context of inflammation. {ECO:0000250|UniProtKB:P55212}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P55212}. Nucleus {ECO:0000250|UniProtKB:P55212}.
|
CATALYTIC ACTIVITY: Reaction=Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|-.; EC=3.4.22.59; Evidence={ECO:0000250|UniProtKB:P55212};
| null | null | null | null |
FUNCTION: Cysteine protease that plays essential roles in programmed cell death, axonal degeneration, development and innate immunity (By similarity). Acts as a non-canonical executioner caspase during apoptosis: localizes in the nucleus and cleaves the nuclear structural protein NUMA1 and lamin A/LMNA thereby inducing nuclear shrinkage and fragmentation. Lamin-A/LMNA cleavage is required for chromatin condensation and nuclear disassembly during apoptotic execution (By similarity). Acts as a regulator of liver damage by promoting hepatocyte apoptosis: in absence of phosphorylation by AMP-activated protein kinase (AMPK), catalyzes cleavage of BID, leading to cytochrome c release, thereby participating in nonalcoholic steatohepatitis. Cleaves PARK7/DJ-1 in cells undergoing apoptosis (By similarity). Involved in intrinsic apoptosis by mediating cleavage of RIPK1. Furthermore, cleaves many transcription factors such as NF-kappa-B and cAMP response element-binding protein/CREBBP (By similarity). Cleaves phospholipid scramblase proteins XKR4 and XKR9. In addition to apoptosis, involved in different forms of programmed cell death. Plays an essential role in defense against viruses by acting as a central mediator of the ZBP1-mediated pyroptosis, apoptosis, and necroptosis (PANoptosis), independently of its cysteine protease activity. PANoptosis is a unique inflammatory programmed cell death, which provides a molecular scaffold that allows the interactions and activation of machinery required for inflammasome/pyroptosis, apoptosis and necroptosis. Mechanistically, interacts with RIPK3 and enhances the interaction between RIPK3 and ZBP1, leading to ZBP1-mediated inflammasome activation and cell death. Plays an essential role in axon degeneration during axon pruning which is the remodeling of axons during neurogenesis but not apoptosis. Regulates B-cell programs both during early development and after antigen stimulation (By similarity). {ECO:0000250|UniProtKB:O08738, ECO:0000250|UniProtKB:P55212}.
|
Rattus norvegicus (Rat)
|
O35400
|
ST2B1_MOUSE
|
MDGPQPRALWSSSEKNVSEMSWNFGGEYFRYKGIPFPVGMYSPESLSLAENTSNVRDDDIFIVTYPKSGTNWMIEIVCLILKDGDPSWIRSEPIWQRAPWCETIISAFNVLDRPSPRIMSSHLPIELFTKAFFSSKAKVIYVGRNPRDVVVSLYYYSKIAGQLKDPGTPDQFLQNFLKGEVQFGSWFDHIKGWIRMQNQENFLFITYEELQQDLRGSVQRICEFLGRPLGEEALSSVVAHSAFAAMKANTMSNYSLLPASLLDHRQGEFLRKGISGDWKNHFTVAQSEAFDSVYREQMHGVQRFPWDTSEEDSSPDGQPDPEPSPSPASDDPNPGSSQ
|
2.8.2.2
| null |
cholesterol metabolic process [GO:0008203]; sulfate assimilation [GO:0000103]; sulfation [GO:0051923]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]
|
cholesterol sulfotransferase activity [GO:0051922]; sulfotransferase activity [GO:0008146]
|
PF00685;
|
3.40.50.300;
|
Sulfotransferase 1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O00204}. Microsome {ECO:0000250|UniProtKB:O00204}. Nucleus {ECO:0000250|UniProtKB:O00204}.
|
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate + H(+); Xref=Rhea:RHEA:22552, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:83414; EC=2.8.2.2; Evidence={ECO:0000269|PubMed:12639899}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + pregnenolone = adenosine 3',5'-bisphosphate + H(+) + pregnenolone sulfate; Xref=Rhea:RHEA:52356, ChEBI:CHEBI:15378, ChEBI:CHEBI:16581, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:133000; Evidence={ECO:0000269|PubMed:12639899}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 3beta-hydroxyandrost-5-en-17-one = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate + H(+); Xref=Rhea:RHEA:51216, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689, ChEBI:CHEBI:57905, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; Evidence={ECO:0000269|PubMed:12639899, ECO:0000269|PubMed:9647753}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + cholesterol = adenosine 3',5'-bisphosphate + cholesterol sulfate + H(+); Xref=Rhea:RHEA:52368, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136579; Evidence={ECO:0000269|PubMed:12639899};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.88 uM for cholesterol (isoform 2) {ECO:0000269|PubMed:12639899}; KM=17.7 uM for pregnenolone (isoform 2) {ECO:0000269|PubMed:12639899}; KM=0.87 uM for cholesterol (isoform 1) {ECO:0000269|PubMed:12639899}; KM=16.7 uM for pregnenolone (isoform 1) {ECO:0000269|PubMed:12639899}; KM=19.7 uM for 3beta-hydroxyandrost-5-en-17-one (DHEA)(isoform 1) {ECO:0000269|PubMed:12639899};
| null | null | null |
FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation. Preferentially sulfonates cholesterol (PubMed:12639899). Catalyzes sulfation of the 3beta-hydroxyl groups of steroids, such as, pregnenolone and dehydroepiandrosterone (DHEA). Cholesterol sulfation is approximately 10-fold higher than for pregnenolone and 20-fold higher than for DHEA (PubMed:12639899). Plays a role in epidermal cholesterol metabolism and in the regulation of epidermal proliferation and differentiation (By similarity). {ECO:0000250|UniProtKB:O00204, ECO:0000269|PubMed:12639899}.; FUNCTION: [Isoform 2]: Strongly sulfonates pregnenolone, however is capable to sulfonate cholesterol with a high degree of efficiency. DHEA is a relatively poor substrate. {ECO:0000269|PubMed:12639899}.
|
Mus musculus (Mouse)
|
O35405
|
PLD3_MOUSE
|
MKPKLMYQELKVPVEEPAGELPLNEIEAWKAAEKKARWVLLVLILAVVGFGALMTQLFLWEYGDLHLFGPNQRPAPCYDPCEAVLVESIPEGLEFPNATTSNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDTHTQEPSAQQGEEVLQQLQALAPRGVKVRIAVSKPNGPLADLQSLLQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCSCLARDLTKIFEAYWFLGQAGSSIPSTWPRSFDTRYNQETPMEICLNGTPALAYLASAPPPLCPSGRTPDLKALLNVVDSARSFIYIAVMNYLPTMEFSHPRRFWPAIDDGLRRAAYERGVKVRLLISCWGHSDPSMRSFLLSLAALHDNHTHSDIQVKLFVVPTDESQARIPYARVNHNKYMVTERASYIGTSNWSGSYFTETAGTSLLVTQNGHGGLRSQLEAVFLRDWESPYSHDLDTSANSVGNACRLL
|
3.1.16.1
| null |
inflammatory response [GO:0006954]; innate immune response [GO:0045087]; myotube differentiation [GO:0014902]; regulation of cytokine production involved in inflammatory response [GO:1900015]
|
early endosome membrane [GO:0031901]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]
|
phospholipase D activity [GO:0004630]; single-stranded DNA 5'-3' DNA exonuclease activity [GO:0045145]
|
PF13918;
|
3.30.870.10;
|
Phospholipase D family
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8IV08}.; PTM: Proteolytically processed to a soluble form that is stable within endosomes and lysosomes. During transport through the secretory pathway becomes proteolysed by cysteine proteases, thereby releasing a stable soluble lysosomal lumenal polypeptide, whereas the transmembrane-bound fragment is rapidly degraded. Its transport route to lysosomes involves ubiquitination and the ESCRT complex. {ECO:0000250|UniProtKB:Q8IV08}.; PTM: Ubiquitinated. Ubiquitination mediates sorting into lysosomes. {ECO:0000250|UniProtKB:Q8IV08}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8IV08}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8IV08}. Lysosome lumen {ECO:0000250|UniProtKB:Q8IV08}. Early endosome membrane {ECO:0000250|UniProtKB:Q8IV08}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8IV08}. Late endosome membrane {ECO:0000269|PubMed:28128235}; Single-pass type II membrane protein {ECO:0000269|PubMed:28128235}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8IV08}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8IV08}. Endosome membrane {ECO:0000250|UniProtKB:Q8IV08}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8IV08}. Note=Localizes to ER-associated vesicles in differentiating myotubes. The soluble form in lysosome arises by proteolytic processing of the membrane-bound form. {ECO:0000250|UniProtKB:Q8IV08}.
|
CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.; EC=3.1.16.1; Evidence={ECO:0000269|PubMed:30111894};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-5. {ECO:0000269|PubMed:30111894};
| null |
FUNCTION: 5'->3' DNA exonuclease which digests single-stranded DNA (ssDNA) (PubMed:30111894). Regulates inflammatory cytokine responses via the degradation of nucleic acids, by reducing the concentration of ssDNA able to stimulate TLR9, a nucleotide-sensing receptor in collaboration with PLD4 (PubMed:30111894). May be important in myotube formation. Plays a role in lysosomal homeostasis. Involved in the regulation of endosomal protein sorting (By similarity). {ECO:0000250|UniProtKB:Q8IV08, ECO:0000269|PubMed:30111894}.
|
Mus musculus (Mouse)
|
O35409
|
FOLH1_MOUSE
|
MWNALQDRDSAEVLGHRQRWLRVGTLVLALTGTFLIGFLFGWFIKPSNEATGNVSHSGMKKEFLHELKAENIKKFLYNFTRTPHLAGTQNNFELAKQIHDQWKEFGLDLVELSHYDVLLSYPNKTHPNYISIINEDGNEIFKTSLSEQPPPGYENISDVVPPYSAFSPQGTPEGDLVYVNYARTEDFFKLEREMKISCSGKIVIARYGKVFRGNMVKNAQLAGAKGMILYSDPADYFVPAVKSYPDGWNLPGGGVQRGNVLNLNGAGDPLTPGYPANEHAYRHELTNAVGLPSIPVHPIGYDDAQKLLEHMGGPAPPDSSWKGGLKVPYNVGPGFAGNFSTQKVKMHIHSYTKVTRIYNVIGTLKGALEPDRYVILGGHRDAWVFGGIDPQSGAAVVHEIVRSFGTLKKKGRRPRRTILFASWDAEEFGLLGSTEWAEEHSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVYNLTKELQSPDEGFEGKSLYDSWKEKSPSPEFIGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWKTNKVSSYPLYHSVYETYELVVKFYDPTFKYHLTVAQVRGAMVFELANSIVLPFDCQSYAVALKKYADTIYNISMKHPQEMKAYMISFDSLFSAVNNFTDVASKFNQRLQELDKSNPILLRIMNDQLMYLERAFIDPLGLPGRPFYRHIIYAPSSHNKYAGESFPGIYDALFDISSKVNASKAWNEVKRQISIATFTVQAAAETLREVA
|
3.4.17.21
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit. Required for NAALADase activity.;
|
folic acid-containing compound metabolic process [GO:0006760]; positive regulation of apoptotic process [GO:0043065]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]
|
cell surface [GO:0009986]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
Ac-Asp-Glu binding [GO:1904492]; carboxypeptidase activity [GO:0004180]; dipeptidase activity [GO:0016805]; metal ion binding [GO:0046872]; metallocarboxypeptidase activity [GO:0004181]; peptidase activity [GO:0008233]; tetrahydrofolyl-poly(glutamate) polymer binding [GO:1904493]
|
PF02225;PF04389;PF04253;
|
3.50.30.30;1.20.930.40;3.40.630.10;
|
Peptidase M28 family, M28B subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q04609}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q04609}.
|
CATALYTIC ACTIVITY: Reaction=Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.; EC=3.4.17.21;
| null | null | null | null |
FUNCTION: Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides (By similarity). In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. {ECO:0000250}.; FUNCTION: Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC. {ECO:0000250}.
|
Mus musculus (Mouse)
|
O35412
|
SI1L1_RAT
|
MTSLKRSQTERPVTADRASVVSTDGTPKVHTDDFYMRRFRSQNGSLGSSVMAAVGPPRSEGPHHITSTPGVPKMGVRARIADWPPRKENVKESSRSSQEIETSSCLESLSSKGSPVSQGSSVSLNSNDSAMLKSIQNTLKNKTGPAESMDSRFLMPEAYPSSPRKALRRIRQRSNSDITISELDVDSFDECISPTYKSGPSLHREYGSTSSIDKQGTSGESFFGLLKGYKDDRADRGPTPTKLSDFLITGGGKGSGFSLDVIDGPISQRENLRLFKEREKPLKRRSKSETGDSSIFRKLRNAKGEELGKSSDLEDNRSEDSVRPWTCPKCFAHYDVQSILFDLNEAIMNRHNVIKRRNTTTGASAAAVASLVSGPLSHSTSFSSPMGSTEDFNSKGSLGMDQGDDKSNELVMSCPYFRNEIGGEGERKISLSKSNSGSFSGCESTSFESALSSHCTNAGVAVLEVPKESLMLHLDRVRRYTVEHVDLGAYYYRKCFYQKEHWNYFGADENLGPVAVSIRREKPEDMKENGSPYNYRIIFRTSELMTLRGSVLEDAIPSTAKHSTARGLPLKEVLEHVIPELNVQCLRLAFNTPKVTEQLMKLDEQGLNYQQKVGIMYCKAGQSTEEEMYNTPKVTEQFMKLDEQGLNYQQKVGIMYCKAGQSTEEEMYNNESAGPAFEEFLQLLGERVRLKGFEKYRAQLDTKTDSTGTHSLYTTYKDYEIMFHVSTMLPYTPNNKQQLLRKRHIGNDIVTIVFQEPGAQPFSPKNIRSHFQHVFVIVRAHNPCTESVCYSVAVTRSRDVPSFGPPIPKGVTFPKSNVFRDFLLAKVINAENAAHKSEKFRAMATRTRQEYLKDLAEKNVTNTPIDPSGKFPFISLASKKKEKSKPYPGAELSSMGAIVWAVRAKDYNKAMEFDCLLGISNEFIVLIEQETKSVVFNCSCRDVIGWTSSDSSLKIFYERGECISVESFMSSEDIKEIVKRLQFVSKGCESVEMTLRRNGLGQLGFHVNYEGIVADVEPYGYAWQAGLKQGSRLVEICKVAVATLSHEQMIDLLRTSVTVKVVIIPPHDDCTPRRSCSETYRMPVMEYKMNEGVSYEYKFPFRSNNKWQRNAGKGAHSPQVPLQLQSPMISRVNAGKGDGKMPLPERAANIPRSISSDGRPLERRLSPGSDIYVTVSSMALARSQCRNSPSNLSSSSETGSGGGTYRQKSMPEGFGVSRRSPASIDRQNTQSDIGGSGKSTPSWQRSEDSLADQMEPTCHLPAVSKVLPAFRESPSGRLMRQDPVVHLSPNKQGHSDSHYSSHSSSNTLSSNASSAHSDEKWYDGDRTESDLNSYNYLQGTSADSGIDTASYGLSHGSTASLGASTSSPRSGPGKEKVAPLWHSSSEVLSLADRTLETEGHGMDRKTESSLSLDIHSKSQGGSSPLTRENSTFSINDATSHTSTMSSRHSASPVVFSSARSSPKEELHPTTSSQLAPSFSSSSSSSSGPRTFYPRQGATSKYLIGWKKPEGTINSVGFMDTRKRHQSDGNEIAHTRLRASTRDLRASPKPTSKSTIEEDLKKLIDLESPTPESQKNFKFHGLSSPQSPFPSTPTSRRALHRTLSDESIYSSQREHFFTSRASLLDQALPNDVFFSSTYPSLPKSLPLRRPSYTLGMKSLHGEFFASDSSLTDIQETRRQPIPDPGLMPLPDTASDLDWSNLVDAAKAYEVQRASFFAASDENHRPLSAASNSDQLEEQALVQMKSYSSSKDSSPTLASKVDQLEGMLKMLREDLKKEKEDKAHLQAEVEHLREDNLRLQEESQNASDKLKKFTEWVFNTIDMS
| null | null |
actin cytoskeleton organization [GO:0030036]; activation of GTPase activity [GO:0090630]; ephrin receptor signaling pathway [GO:0048013]; postsynaptic actin cytoskeleton organization [GO:0098974]; regulation of axonogenesis [GO:0050770]; regulation of dendrite morphogenesis [GO:0048814]; regulation of dendritic spine morphogenesis [GO:0061001]; regulation of GTPase activity [GO:0043087]; regulation of postsynaptic density assembly [GO:0099151]; regulation of small GTPase mediated signal transduction [GO:0051056]; regulation of synaptic plasticity [GO:0048167]
|
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; postsynapse [GO:0098794]; postsynaptic density [GO:0014069]; protein-containing complex [GO:0032991]
|
actin filament binding [GO:0051015]; ephrin receptor binding [GO:0046875]; GTPase activator activity [GO:0005096]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877]; ubiquitin protein ligase binding [GO:0031625]
|
PF00595;PF21022;PF02145;PF11881;
|
2.30.42.10;3.30.1120.160;3.40.50.11210;
| null |
PTM: Ubiquitinated and degraded by the SCF(BTRC) following phosphorylation by PLK2.; PTM: Phosphorylated at Ser-1367 by CDK5, creating a docking site for the POLO box domains of PLK2. Subsequently, PLK2 binds and phosphorylates SIPA1L1, leading to ubiquitination and degradation by the proteasome. {ECO:0000269|PubMed:18498738}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Postsynaptic density. Synapse, synaptosome. Note=Associated with the actin cytoskeleton. Detected at synapses and dendritic spines of cultured hippocampal neurons.
| null | null | null | null | null |
FUNCTION: Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F-actin. Contributes to the regulation of dendritic spine morphogenesis. {ECO:0000269|PubMed:11502259}.
|
Rattus norvegicus (Rat)
|
O35413
|
SRBS2_RAT
|
MNTDSGGCARKRAAMSVTLTSVKRVQSSPNLLAAGRESHSPDSAWRSYNGRNPETLNGDATYSSLAAKGFRSVRPNLQDKKSPTQSHITINGNSGGAVSPVSYYQRPFSPSAYSLPASLNSSIIMPHGRSLDSAETYSQHAQSLDGTMGSSIPLYRSSEEEKRVTVIKAPHYPGIGPVDESGIPTAIRTTVDRPKDWYKTMFKQIHMVHKPDEDTDMYNTPYTYNAGLYNSPYSAQSHPAAKTQTYRPLSKSHSDNGTDAFKEATSPVPPPHVPPRPRDQSSTEKHDWDPPDRKVDTRKFRSEPRSIFEYEPGKSSILQHERPVSVYQSSIDRSLERPSSSASMAGDFRKRRKSEPAVGPPRGLGDHSSSRTSPGRADLPGSSSTFTTSFISSSPSSPSRAQGGDDSKMCPPLCSYSGLNGSPSSELECCGAYRRHLDVPQDSQRAITFKNGWQMARQNAEIWSSTEEAVSPKIKSRSCDDLLNDDCGSFPDPKTKSESMGSLLCDEGSKESDPMTWTSPYIPEVCGNSRSRLKHRSAHNAPGFLKMYKKMHRINRKDLMNSEVICSVKSRILQYEKEQQHRGLLHGWSQSSTEEVPRDVVPTRISEFEKLIQKSKSMPNLGDEMLSPVTLEPPQNGLCPKRRFSIESLLEEETQVRHPSQGQRSCKSNTLVPIHIEVTSDEQPRTHMEFSDSDQDGVVSDHSDNVHVERSSFCSESDFDHFSFTSSESFYGSSHHHHHHHHHHGHFISSCKGRCPASYTRFTTMLKHERAKHENIDRPRRQDMDPGLSKLAFLVSPVPFRRKKVLTPQKQTEQAKCKASVVEALDSALKDICDQIKAEKRRGSLPDNSILHRLISELLPQIPKRNSSLNALKRSPMHQPFHPLPQDGAIHCPLYQNDCGRMPHSASFPDVDTTSSYHAQDYGSVLSLQDHESPRSYSSTLTDLGRSVSRERRGTPEKEVKLPAKAVYDFKAQTSKELSFKKGDTVYILRKIDQNWYEGEHHGRVGIFPISYVEKLTPPEKAQPARPPPPVQPGEIGEAIAKYNFNADTNVELSLRKGDRIILLKRVDQNWYEGKIPGTNRQGIFPVSYVEVVKRNTKGSEDYPDPPLPHSYSSDRIYSLSSNKPQRPVFSHENIQGGGEPFQALYNYTPRNEDELELRESDVVDVMEKCDDGWFVGTSRRTKFFGTFPGNYVKRL
| null | null |
acetylcholine receptor signaling pathway [GO:0095500]; cell growth involved in cardiac muscle cell development [GO:0061049]; Notch signaling pathway [GO:0007219]; regulation of skeletal muscle acetylcholine-gated channel clustering [GO:1904393]
|
apical plasma membrane [GO:0016324]; dendrite [GO:0030425]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; synapse [GO:0045202]
|
protein domain specific binding [GO:0019904]
|
PF00018;PF14604;PF02208;
|
2.30.30.40;
| null |
PTM: Ubiquitinated by CBL. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10521485, ECO:0000269|PubMed:15128873, ECO:0000269|PubMed:15659545, ECO:0000269|PubMed:16125169}. Apical cell membrane {ECO:0000250|UniProtKB:O94875}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:O94875}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O94875}. Note=Detected in the stress fibers, synaptosomal cytosol, postsynaptic density fraction, Z-disks and intercalated. The CBL/PTK2B/ARGBP2 complex is recruited to lipid rafts following growth factor stimulation. In pancreatic acinar cells, localized preferentially to the apical membrane. Colocalized with vinculin and filamentous actin at focal adhesions and lamellipodia of pancreatic cells. {ECO:0000250|UniProtKB:O94875}.
| null | null | null | null | null |
FUNCTION: Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1 (By similarity). May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (By similarity). Isoform 2 increases water and sodium absorption in the intestine and gall-bladder. {ECO:0000250, ECO:0000250|UniProtKB:O94875, ECO:0000269|PubMed:10521485}.
|
Rattus norvegicus (Rat)
|
O35417
|
PDYN_MOUSE
|
MAWSRLMLAACLLVMPSNVMADCLSLCSLCAVRIQDGPRPINPLICSLECQDLVPPSEEWETCRGFSSFLTLTVSGLRGKDDLEDEVALEEGISAHAKLLEPVLKELEKSRLLTSVPEEKFRGLSSSFGNGKESELAGADRMNDEAAQGRTVHFNEEDLRKQAKRYGGFLRKYPKRSSEMARDEDGGQDGDQVGHEDLYKRYGGFLRRIRPKLKWDNQKRYGGFLRRQFKVVTRSQENPNTYSEDLDV
| null | null |
chemical synaptic transmission [GO:0007268]; neuropeptide signaling pathway [GO:0007218]; sensory perception [GO:0007600]
|
axon terminus [GO:0043679]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; dense core granule [GO:0031045]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; neuronal cell body [GO:0043025]; neuronal dense core vesicle lumen [GO:0099013]; plasma membrane [GO:0005886]; synaptic vesicle [GO:0008021]
|
neuropeptide hormone activity [GO:0005184]; opioid peptide activity [GO:0001515]; opioid receptor binding [GO:0031628]
|
PF01160;
| null |
Opioid neuropeptide precursor family
|
PTM: The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity). {ECO:0000250}.; FUNCTION: Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opioid activity, it is 700 times more potent than Leu-enkephalin (By similarity). {ECO:0000250}.; FUNCTION: Leumorphin has a typical opioid activity and may have anti-apoptotic effect. {ECO:0000250}.
|
Mus musculus (Mouse)
|
O35423
|
AGT1_MOUSE
|
MFRMLAKASVTLGSRAAGWVRTMGSYQLLVPPPEALSKPLSVPTRLLLGPGPSNLAPRVLAAGSLRMIGHMQKEMLQIMEEIKQGIQYVFQTRNPLTLVVSGSGHCAMETALFNLLEPGDSFLTGTNGIWGMRAAEIADRIGARVHQMIKKPGEHYTLQEVEEGLAQHKPVLLFLVHGESSTGVVQPLDGFGELCHRYQCLLLVDSVASLGGVPIYMDQQGIDIMYSSSQKVLNAPPGISLISFNDKAKYKVYSRKTKPVSFYTDITYLAKLWGCEGETRVIHHTTPVTSLYCLRESLALIAEQGLENCWRRHREATAHLHKHLQEMGLKFFVKDPEIRLPTITTVTVPAGYNWRDIVSYVLDHFSIEISGGLGPTEERVLRIGLLGYNATTENVDRVAEALREALQHCPKNKL
|
2.6.1.44; 2.6.1.51
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P21549};
|
glycine biosynthetic process, by transamination of glyoxylate [GO:0019265]; glyoxylate catabolic process [GO:0009436]; glyoxylate metabolic process [GO:0046487]; L-alanine catabolic process [GO:0042853]; L-cysteine catabolic process [GO:0019448]; L-serine metabolic process [GO:0006563]; Notch signaling pathway [GO:0007219]; oxalic acid secretion [GO:0046724]; pyruvate biosynthetic process [GO:0042866]; response to cAMP [GO:0051591]; response to glucocorticoid [GO:0051384]
|
mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]
|
alanine-glyoxylate transaminase activity [GO:0008453]; amino acid binding [GO:0016597]; protein homodimerization activity [GO:0042803]; protein self-association [GO:0043621]; pyridoxal phosphate binding [GO:0030170]; serine-pyruvate transaminase activity [GO:0004760]
|
PF00266;
|
3.90.1150.10;3.40.640.10;
|
Class-V pyridoxal-phosphate-dependent aminotransferase family
| null |
SUBCELLULAR LOCATION: [Isoform Peroxisomal]: Peroxisome {ECO:0000250|UniProtKB:P21549}.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion matrix {ECO:0000250|UniProtKB:P09139}.
|
CATALYTIC ACTIVITY: [Isoform Mitochondrial]: Reaction=L-serine + pyruvate = 3-hydroxypyruvate + L-alanine; Xref=Rhea:RHEA:22852, ChEBI:CHEBI:15361, ChEBI:CHEBI:17180, ChEBI:CHEBI:33384, ChEBI:CHEBI:57972; EC=2.6.1.51; Evidence={ECO:0000250|UniProtKB:P09139}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22853; Evidence={ECO:0000250|UniProtKB:P09139}; CATALYTIC ACTIVITY: [Isoform Peroxisomal]: Reaction=glyoxylate + L-alanine = glycine + pyruvate; Xref=Rhea:RHEA:24248, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:57972; EC=2.6.1.44; Evidence={ECO:0000250|UniProtKB:P21549}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24249; Evidence={ECO:0000250|UniProtKB:P21549};
| null | null | null | null |
FUNCTION: [Isoform Peroxisomal]: Catalyzes the transamination of glyoxylate to glycine and contributes to the glyoxylate detoxification. {ECO:0000250|UniProtKB:P21549}.; FUNCTION: [Isoform Mitochondrial]: Catalyzes the transamination between L-serine and pyruvate and weakly contributes to gluconeogenesis from the L-serine metabolism. {ECO:0000250|UniProtKB:P09139}.
|
Mus musculus (Mouse)
|
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