SH3G3_DROVI
ID SH3G3_DROVI Reviewed; 369 AA.
AC Q8I190; B4MC14;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Endophilin-A;
DE AltName: Full=SH3 domain-containing GRB2-like protein;
GN Name=EndoA {ECO:0000250|UniProtKB:Q8T390}; ORFNames=GJ14546;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1] {ECO:0000312|EMBL:AAO01081.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1001.10 {ECO:0000312|EMBL:AAO01081.1};
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 15010-1051.87;
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; AY190955; AAO01081.1; -; Genomic_DNA.
DR EMBL; CH940656; EDW58635.1; -; Genomic_DNA.
DR RefSeq; XP_002058667.1; XM_002058631.2.
DR RefSeq; XP_015024958.1; XM_015169472.1.
DR RefSeq; XP_015024959.1; XM_015169473.1.
DR RefSeq; XP_015024960.1; XM_015169474.1.
DR RefSeq; XP_015024961.1; XM_015169475.1.
DR AlphaFoldDB; Q8I190; -.
DR SMR; Q8I190; -.
DR STRING; 7244.FBpp0228963; -.
DR EnsemblMetazoa; FBtr0230471; FBpp0228963; FBgn0086436.
DR EnsemblMetazoa; FBtr0433697; FBpp0390816; FBgn0086436.
DR EnsemblMetazoa; FBtr0434069; FBpp0391160; FBgn0086436.
DR EnsemblMetazoa; FBtr0439285; FBpp0395970; FBgn0086436.
DR EnsemblMetazoa; FBtr0439486; FBpp0396154; FBgn0086436.
DR GeneID; 6635107; -.
DR KEGG; dvi:6635107; -.
DR eggNOG; KOG1118; Eukaryota.
DR HOGENOM; CLU_047887_0_0_1; -.
DR InParanoid; Q8I190; -.
DR OMA; QYLSETM; -.
DR OrthoDB; 788657at2759; -.
DR PhylomeDB; Q8I190; -.
DR Proteomes; UP000008792; 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;
KW Reference proteome; SH3 domain.
FT CHAIN 1..369
FT /note="Endophilin-A"
FT /id="PRO_0000285840"
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 275..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 227..249
FT /evidence="ECO:0000255"
FT COMPBIAS 276..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 41302 MW; 13083EBAFB655526 CRC64;
MAFAGLKKQI NKANQYVTEK MGGAEGTKLD LDFMDMERKT DVTVELVEEL QLKTKEFLQP
NPTARAKMAA VKGISKLSGQ AKSNTYPQPE GLLAECMLTY GKKLGEDNSV FAQALVEFGE
ALKQMADVKY SLDDNIKQNF LEPLHHMQTK DLKEVMHHRK KLQGRRLDFD CKRRRQAKDD
EIRGAEDKFA ESLQLAQVGM FNLLENDTEH VSQLVTFAEA LYDFHSQCAD VLRGLQETLQ
EKRAEAESRP RNEFVPKTLL DLNLDGGGGG LIDDGTPSHI SSSASPLPSP MRSPAKSMAV
TPNRQQQPCC QALYDFDPEN PGELGFKEND IITLLNRVDD NWYEGAVNGR TGYFPQSYVQ
VQVPLPNGN
