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SH3G3_DROER
ID   SH3G3_DROER             Reviewed;         369 AA.
AC   Q8I1I3; B3P397;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Endophilin-A;
DE   AltName: Full=SH3 domain-containing GRB2-like protein;
GN   Name=EndoA {ECO:0000250|UniProtKB:Q8T390}; ORFNames=GG23082;
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220;
RN   [1] {ECO:0000312|EMBL:AAO00984.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14021-0224.0 {ECO:0000312|EMBL:AAO00984.1};
RX   PubMed=12537575; DOI=10.1186/gb-2002-3-12-research0086;
RA   Bergman C.M., Pfeiffer B.D., Rincon-Limas D.E., Hoskins R.A., Gnirke A.,
RA   Mungall C.J., Wang A.M., Kronmiller B., Pacleb J.M., Park S., Stapleton M.,
RA   Wan K.H., George R.A., de Jong P.J., Botas J., Rubin G.M., Celniker S.E.;
RT   "Assessing the impact of comparative genomic sequence data on the
RT   functional annotation of the Drosophila genome.";
RL   Genome Biol. 3:RESEARCH0086.1-RESEARCH0086.20(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14021-0224.01;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Required presynaptically at the neuromuscular junction.
CC       Implicated in synaptic vesicle endocytosis.
CC       {ECO:0000250|UniProtKB:Q8T390}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8T390}.
CC       Membrane {ECO:0000250|UniProtKB:Q8T390}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q8T390}. Note=Associated with internal
CC       membranes. Expressed presynaptically at NMJs.
CC       {ECO:0000250|UniProtKB:Q8T390}.
CC   -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000255}.
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DR   EMBL; AY190935; AAO00984.1; -; Genomic_DNA.
DR   EMBL; CH954181; EDV48549.1; -; Genomic_DNA.
DR   RefSeq; XP_001979591.1; XM_001979555.2.
DR   AlphaFoldDB; Q8I1I3; -.
DR   SMR; Q8I1I3; -.
DR   STRING; 7220.FBpp0141628; -.
DR   EnsemblMetazoa; FBtr0143136; FBpp0141628; FBgn0064606.
DR   GeneID; 6553880; -.
DR   KEGG; der:6553880; -.
DR   eggNOG; KOG1118; Eukaryota.
DR   HOGENOM; CLU_047887_0_0_1; -.
DR   OMA; QYLSETM; -.
DR   OrthoDB; 788657at2759; -.
DR   PhylomeDB; Q8I1I3; -.
DR   Proteomes; UP000008711; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0061174; C:type I terminal bouton; IEA:EnsemblMetazoa.
DR   GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0005543; F:phospholipid binding; IEA:EnsemblMetazoa.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:EnsemblMetazoa.
DR   GO; GO:0009267; P:cellular response to starvation; IEA:EnsemblMetazoa.
DR   GO; GO:0150007; P:clathrin-dependent synaptic vesicle endocytosis; IEA:EnsemblMetazoa.
DR   GO; GO:0097753; P:membrane bending; IEA:EnsemblMetazoa.
DR   GO; GO:0097749; P:membrane tubulation; IEA:EnsemblMetazoa.
DR   GO; GO:0097320; P:plasma membrane tubulation; IEA:EnsemblMetazoa.
DR   GO; GO:0050803; P:regulation of synapse structure or activity; ISS:UniProtKB.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Endocytosis; Membrane; Phosphoprotein; SH3 domain.
FT   CHAIN           1..369
FT                   /note="Endophilin-A"
FT                   /id="PRO_0000285837"
FT   DOMAIN          18..248
FT                   /note="BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT   DOMAIN          305..364
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          266..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          227..247
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        275..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   369 AA;  41409 MW;  F6B82FAEA6FF31A9 CRC64;
     MAFAGLKKQI NKANQYMTEK MGGAEGTKLD MDFMEMERKT DVTVELVEEL QLKTKEFLQP
     NPTARAKMAA VKGISKLSGQ AKSNTYPQPE GLLAECMLTY GKKLGEDNSV FAQALVEFGE
     ALKQMADVKY SLDDNIKQNF LEPLHHMQTK DLKEVMHHRK KLQGRRLDFD CKRRRQAKDD
     EIRGAEDKFG ESLQLAQVGM FNLLENDTEH VSQLVTFAEA LYDFHSQCAD VLRGLQETLQ
     EKRSEAESRP RNEFVPKTLL DLNLDGGGGG LNEDGTPSHI SSSASPLPSP MRSPAKSMAV
     TPQRQQQPCC QALYDFEPEN PGELAFKEND IITLLNRVDD NWFEGAVNGR TGYFPQSYVQ
     VQVPLPNGN
 
 
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