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SH3GH_CAEEL
ID   SH3GH_CAEEL             Reviewed;         381 AA.
AC   B1V8A0; A5A8Q9; A5A8R0; O61843; Q6TM46;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Endophilin-A homolog {ECO:0000305|PubMed:14622579};
DE   AltName: Full=Endophilin-1 homolog {ECO:0000305|PubMed:14622579};
DE   AltName: Full=Uncoordinated protein 57 {ECO:0000312|WormBase:T04D1.3d};
GN   Name=unc-57 {ECO:0000312|WormBase:T04D1.3d};
GN   ORFNames=T04D1.3 {ECO:0000312|WormBase:T04D1.3d};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|EMBL:AAQ96373.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=14622579; DOI=10.1016/s0896-6273(03)00667-6;
RA   Schuske K.R., Richmond J.E., Matthies D.S., Davis W.S., Runz S., Rube D.A.,
RA   van der Bliek A.M., Jorgensen E.M.;
RT   "Endophilin is required for synaptic vesicle endocytosis by localizing
RT   synaptojanin.";
RL   Neuron 40:749-762(2003).
RN   [2] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=17928447; DOI=10.1523/jneurosci.1941-07.2007;
RA   Parker J.A., Metzler M., Georgiou J., Mage M., Roder J.C., Rose A.M.,
RA   Hayden M.R., Neri C.;
RT   "Huntingtin-interacting protein 1 influences worm and mouse presynaptic
RT   function and protects Caenorhabditis elegans neurons against mutant
RT   polyglutamine toxicity.";
RL   J. Neurosci. 27:11056-11064(2007).
RN   [4] {ECO:0000305}
RP   SUBCELLULAR LOCATION.
RX   PubMed=18094048; DOI=10.1091/mbc.e07-07-0719;
RA   Marza E., Long T., Saiardi A., Sumakovic M., Eimer S., Hall D.H.,
RA   Lesa G.M.;
RT   "Polyunsaturated fatty acids influence synaptojanin localization to
RT   regulate synaptic vesicle recycling.";
RL   Mol. Biol. Cell 19:833-842(2008).
RN   [5] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 1-MET--PRO-26
RP   AND ALA-66.
RX   PubMed=21029864; DOI=10.1016/j.cell.2010.09.024;
RA   Bai J., Hu Z., Dittman J.S., Pym E.C., Kaplan J.M.;
RT   "Endophilin functions as a membrane-bending molecule and is delivered to
RT   endocytic zones by exocytosis.";
RL   Cell 143:430-441(2010).
RN   [6] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=22157748; DOI=10.1038/emboj.2011.447;
RA   Troulinaki K., Tavernarakis N.;
RT   "Endocytosis and intracellular trafficking contribute to necrotic
RT   neurodegeneration in C. elegans.";
RL   EMBO J. 31:654-666(2012).
CC   -!- FUNCTION: Involved in synaptic vesicle (SV) recycling in neurons
CC       probably by regulating clathrin-mediated endocytosis (PubMed:14622579,
CC       PubMed:21029864). By controlling SV endocytosis, regulates the rate of
CC       excitatory postsynaptic currents (EPSCs) at neuromuscular junctions and
CC       thus locomotion (PubMed:21029864). In a similar manner, involved in
CC       necrotic neuronal cell death induced by abnormal hyperactivation of ion
CC       channels (PubMed:22157748). Plays a minor role in responses to
CC       mechanical stimuli (PubMed:17928447). Plays a minor role in unc-
CC       26/synaptojanin localization to synapses (PubMed:14622579).
CC       {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:17928447,
CC       ECO:0000269|PubMed:21029864, ECO:0000269|PubMed:22157748}.
CC   -!- SUBUNIT: May form a homodimer (via the BAR domain).
CC       {ECO:0000303|PubMed:21029864}.
CC   -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:14622579,
CC       ECO:0000269|PubMed:18094048, ECO:0000269|PubMed:21029864}. Cytoplasmic
CC       vesicle, secretory vesicle, synaptic vesicle
CC       {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:21029864}. Membrane
CC       {ECO:0000305|PubMed:21029864}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:21029864}. Note=Localizes to neuromuscular
CC       junctions. Co-localizes with snb-1/synaptobrevin and rab-3 but not dyn-
CC       1 and apt-4 (PubMed:14622579, PubMed:21029864). Exocytosis promotes
CC       dissociation from synaptic vesicles (PubMed:21029864).
CC       {ECO:0000269|PubMed:14622579, ECO:0000269|PubMed:21029864}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=d {ECO:0000312|WormBase:T04D1.3d};
CC         IsoId=B1V8A0-1; Sequence=Displayed;
CC       Name=a {ECO:0000312|WormBase:T04D1.3a};
CC         IsoId=B1V8A0-2; Sequence=VSP_058674, VSP_058675;
CC       Name=b {ECO:0000312|WormBase:T04D1.3b};
CC         IsoId=B1V8A0-3; Sequence=VSP_058673, VSP_058675;
CC       Name=c {ECO:0000312|WormBase:T04D1.3c};
CC         IsoId=B1V8A0-4; Sequence=VSP_058675;
CC   -!- TISSUE SPECIFICITY: Expressed in neurons and posterior intestine.
CC       {ECO:0000269|PubMed:14622579}.
CC   -!- DOMAIN: An N-terminal amphipathic helix, the BAR domain and a second
CC       amphipathic helix inserted into helix 1 of the BAR domain (N-BAR
CC       domain) induce membrane curvature and bind curved membranes. The BAR
CC       domain dimer forms a rigid crescent shaped bundle of helices with the
CC       pair of second amphipathic helices protruding towards the membrane-
CC       binding surface (By similarity). Essential for synaptic vesicle
CC       endocytosis (PubMed:21029864). Plays a role in unc-57 localization to
CC       synaptic vesicles (PubMed:21029864). Dimerization and membrane-bending
CC       activity are required neither for binding to synaptic vesicles nor for
CC       unbinding following synaptic vesicle exocytosis (PubMed:21029864).
CC       {ECO:0000250|UniProtKB:Q99962, ECO:0000269|PubMed:21029864}.
CC   -!- DOMAIN: The SH3 domain is required for unc-26/synaptojanin localization
CC       to synapses but is dispensable for endocytosis and unc-57 targeting to
CC       synaptic vesicles. {ECO:0000269|PubMed:21029864}.
CC   -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000305}.
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DR   EMBL; AY394006; AAQ96373.1; -; mRNA.
DR   EMBL; BX284601; CCD61260.1; -; Genomic_DNA.
DR   EMBL; BX284601; CCD61261.1; -; Genomic_DNA.
DR   EMBL; BX284601; CCD61262.1; -; Genomic_DNA.
DR   EMBL; BX284601; CCD61263.1; -; Genomic_DNA.
DR   PIR; T33150; T33150.
DR   RefSeq; NP_001040680.1; NM_001047215.3. [B1V8A0-2]
DR   RefSeq; NP_001040681.1; NM_001047216.1. [B1V8A0-3]
DR   RefSeq; NP_001122512.1; NM_001129040.2. [B1V8A0-4]
DR   RefSeq; NP_001122513.1; NM_001129041.2. [B1V8A0-1]
DR   AlphaFoldDB; B1V8A0; -.
DR   SMR; B1V8A0; -.
DR   DIP; DIP-25104N; -.
DR   IntAct; B1V8A0; 45.
DR   STRING; 6239.T04D1.3d; -.
DR   EPD; B1V8A0; -.
DR   PaxDb; B1V8A0; -.
DR   PRIDE; B1V8A0; -.
DR   EnsemblMetazoa; T04D1.3a.1; T04D1.3a.1; WBGene00006791. [B1V8A0-2]
DR   EnsemblMetazoa; T04D1.3b.1; T04D1.3b.1; WBGene00006791. [B1V8A0-3]
DR   EnsemblMetazoa; T04D1.3c.1; T04D1.3c.1; WBGene00006791. [B1V8A0-4]
DR   EnsemblMetazoa; T04D1.3d.1; T04D1.3d.1; WBGene00006791. [B1V8A0-1]
DR   GeneID; 172078; -.
DR   KEGG; cel:CELE_T04D1.3; -.
DR   UCSC; T04D1.3d; c. elegans.
DR   CTD; 172078; -.
DR   WormBase; T04D1.3a; CE37042; WBGene00006791; unc-57. [B1V8A0-2]
DR   WormBase; T04D1.3b; CE39765; WBGene00006791; unc-57. [B1V8A0-3]
DR   WormBase; T04D1.3c; CE41009; WBGene00006791; unc-57. [B1V8A0-4]
DR   WormBase; T04D1.3d; CE42509; WBGene00006791; unc-57. [B1V8A0-1]
DR   eggNOG; KOG1118; Eukaryota.
DR   GeneTree; ENSGT00940000157398; -.
DR   InParanoid; B1V8A0; -.
DR   OMA; QYLSETM; -.
DR   OrthoDB; 788657at2759; -.
DR   PhylomeDB; B1V8A0; -.
DR   Reactome; R-CEL-182971; EGFR downregulation.
DR   Reactome; R-CEL-432720; Lysosome Vesicle Biogenesis.
DR   Reactome; R-CEL-432722; Golgi Associated Vesicle Biogenesis.
DR   Reactome; R-CEL-437239; Recycling pathway of L1.
DR   Reactome; R-CEL-6807004; Negative regulation of MET activity.
DR   Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR   SignaLink; B1V8A0; -.
DR   PRO; PR:B1V8A0; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00006791; Expressed in larva and 4 other tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:WormBase.
DR   GO; GO:0098793; C:presynapse; IBA:GO_Central.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:WormBase.
DR   GO; GO:0010940; P:positive regulation of necrotic cell death; IGI:WormBase.
DR   GO; GO:0012501; P:programmed cell death; IEA:UniProtKB-KW.
DR   GO; GO:0016191; P:synaptic vesicle uncoating; IBA:GO_Central.
DR   CDD; cd11803; SH3_Endophilin_A; 1.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR028501; Endophilin-A.
DR   InterPro; IPR035824; Endophilin_A_SH3.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR14167:SF45; PTHR14167:SF45; 1.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00721; BAR; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   PROSITE; PS51021; BAR; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasmic vesicle; Endocytosis;
KW   Membrane; Necrosis; Reference proteome; SH3 domain; Synapse.
FT   CHAIN           1..381
FT                   /note="Endophilin-A homolog"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000438523"
FT   DOMAIN          18..247
FT                   /note="BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT   DOMAIN          320..379
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          1..21
FT                   /note="Membrane-binding amphipathic helix"
FT                   /evidence="ECO:0000250|UniProtKB:Q99962"
FT   REGION          246..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          170..238
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        261..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..317
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..277
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_058673"
FT   VAR_SEQ         269..270
FT                   /note="Missing (in isoform a)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_058674"
FT   VAR_SEQ         288..289
FT                   /note="Missing (in isoform a, isoform b and isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_058675"
FT   MUTAGEN         1..26
FT                   /note="Missing: Locomotion is almost completely impaired.
FT                   Severe reduction in synaptic vesicle endocytosis and in the
FT                   rate of excitatory postsynaptic currents (EPSCs) at
FT                   neuromuscular junctions."
FT                   /evidence="ECO:0000269|PubMed:21029864"
FT   MUTAGEN         66
FT                   /note="A->W: May increase membrane-binding activity in
FT                   vitro. Does not affect its localization to synaptic
FT                   vesicles."
FT                   /evidence="ECO:0000269|PubMed:21029864"
FT   CONFLICT        217
FT                   /note="I -> T (in Ref. 1; AAQ96373)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   381 AA;  42856 MW;  3F6A96595F837422 CRC64;
     MSLSGLRKQF NKANQYLSET MGAAEPTKLD DVFNEMEKNV DTTYNLITDL VAGTNEYLQP
     NPATRAKMAT QVALSKVRGT TKTSPYPQTE GMLADVMQKY GQQLGDNSDL GKSLNDAAET
     YRQMADIKYQ MEDNVKQNFL DPLTHLQNNE LKDVNHHRTK LKGRRLDYDC KKRQQRRDDE
     MIQAEEKLEE SKRLAEMSMF NVLSNDVEQI SQLRALIEAQ LDFHRQTAQC LENLQQQLGH
     RIKDAAARPR EEHVPLSVLA NESRTPRSSF RSPAPSDMSH NSTAAAAFKM PPQNGGGITQ
     APPSYQGPPP GGLPPPLSQQ QKPQCRALFD FDAQSEGELD FKEGTLIELV SQIDENWYEG
     RVNGKTGLFP VTYVQVLVPL K
 
 
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