SH3G3_DROME
ID SH3G3_DROME Reviewed; 369 AA.
AC Q8T390; Q95V65; Q9VE25;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Endophilin-A;
DE AltName: Full=SH3 domain-containing GRB2-like protein;
GN Name=EndoA {ECO:0000312|FlyBase:FBgn0038659};
GN Synonyms=endo {ECO:0000303|PubMed:11955450};
GN ORFNames=CG14296 {ECO:0000312|FlyBase:FBgn0038659};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL24818.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, RNA EDITING OF POSITION 129, AND DISRUPTION PHENOTYPE.
RC STRAIN=Berkeley {ECO:0000269|PubMed:11955450};
RC TISSUE=Head {ECO:0000269|PubMed:11955450};
RX PubMed=11955450; DOI=10.1016/s0092-8674(02)00688-8;
RA Verstreken P., Kjaerulff O., Lloyd T.E., Atkinson R., Zhou Y.,
RA Meinertzhagen I.A., Bellen H.J.;
RT "Endophilin mutations block clathrin-mediated endocytosis but not
RT neurotransmitter release.";
RL Cell 109:101-112(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAD24682.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Berkeley {ECO:0000269|PubMed:11927550};
RC TISSUE=Head {ECO:0000312|EMBL:CAD24682.1};
RX PubMed=11927550; DOI=10.1093/emboj/21.7.1661;
RA Guichet A., Wucherpfennig T., Dudu V., Etter S., Wilsch-Brauniger M.,
RA Hellwig A., Gonzalez-Gaitan M., Huttner W.B., Schmidt A.A.;
RT "Essential role of endophilin A in synaptic vesicle budding at the
RT Drosophila neuromuscular junction.";
RL EMBO J. 21:1661-1672(2002).
RN [3] {ECO:0000312|EMBL:AAF55606.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAF55606.2}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAO25060.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND RNA EDITING OF POSITION 129.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO25060.1}; TISSUE=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP RNA EDITING OF POSITIONS 129 AND 137.
RX PubMed=17018572; DOI=10.1261/rna.254306;
RA Stapleton M., Carlson J.W., Celniker S.E.;
RT "RNA editing in Drosophila melanogaster: new targets and functional
RT consequences.";
RL RNA 12:1922-1932(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285; SER-289 AND SER-293, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Required presynaptically at the neuromuscular junction.
CC Implicated in synaptic vesicle endocytosis.
CC {ECO:0000269|PubMed:11927550, ECO:0000269|PubMed:11955450}.
CC -!- INTERACTION:
CC Q8T390; Q9VE96: l(3)05822; NbExp=3; IntAct=EBI-150782, EBI-156726;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11927550,
CC ECO:0000269|PubMed:11955450}. Membrane {ECO:0000269|PubMed:11927550,
CC ECO:0000269|PubMed:11955450}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11927550, ECO:0000269|PubMed:11955450}.
CC Note=Associated with internal membranes. Expressed presynaptically at
CC NMJs. {ECO:0000269|PubMed:11927550, ECO:0000269|PubMed:11955450}.
CC -!- TISSUE SPECIFICITY: Expression is abundant in central nervous system
CC (brain lobes and the ventral nerve cord) starting at embryonic stage 13
CC through to third instar larvae. Also expressed in photoreceptors in the
CC eye imaginal disks and the Bolwig organs of the peripheral nervous
CC system. {ECO:0000269|PubMed:11927550, ECO:0000269|PubMed:11955450}.
CC -!- RNA EDITING: Modified_positions=129 {ECO:0000269|PubMed:11955450,
CC ECO:0000269|PubMed:17018572, ECO:0000269|Ref.5}, 137
CC {ECO:0000269|PubMed:17018572}; Note=Partially edited. Target of Adar.
CC {ECO:0000269|PubMed:17018572};
CC -!- DISRUPTION PHENOTYPE: Dramatic impairment of clathrin-mediated
CC endocytosis, severe defects in motility and death at the early L2
CC larval stage. {ECO:0000269|PubMed:11955450}.
CC -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000255}.
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DR EMBL; AF426170; AAL24818.1; -; mRNA.
DR EMBL; AJ437141; CAD24682.1; -; mRNA.
DR EMBL; AE014297; AAF55606.2; -; Genomic_DNA.
DR EMBL; BT003300; AAO25060.1; -; mRNA.
DR RefSeq; NP_001262717.1; NM_001275788.1.
DR RefSeq; NP_620122.2; NM_138767.3.
DR RefSeq; NP_732383.1; NM_169838.2.
DR AlphaFoldDB; Q8T390; -.
DR SMR; Q8T390; -.
DR BioGRID; 67269; 15.
DR IntAct; Q8T390; 9.
DR STRING; 7227.FBpp0083112; -.
DR iPTMnet; Q8T390; -.
DR PaxDb; Q8T390; -.
DR PRIDE; Q8T390; -.
DR DNASU; 42265; -.
DR EnsemblMetazoa; FBtr0083698; FBpp0083112; FBgn0038659.
DR EnsemblMetazoa; FBtr0083699; FBpp0083113; FBgn0038659.
DR EnsemblMetazoa; FBtr0334522; FBpp0306589; FBgn0038659.
DR GeneID; 42265; -.
DR KEGG; dme:Dmel_CG14296; -.
DR CTD; 42265; -.
DR FlyBase; FBgn0038659; EndoA.
DR VEuPathDB; VectorBase:FBgn0038659; -.
DR eggNOG; KOG1118; Eukaryota.
DR GeneTree; ENSGT00940000157398; -.
DR HOGENOM; CLU_047887_0_0_1; -.
DR InParanoid; Q8T390; -.
DR OMA; QYLSETM; -.
DR OrthoDB; 788657at2759; -.
DR PhylomeDB; Q8T390; -.
DR Reactome; R-DME-177504; Retrograde neurotrophin signalling.
DR Reactome; R-DME-182971; EGFR downregulation.
DR Reactome; R-DME-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-DME-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-DME-437239; Recycling pathway of L1.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q8T390; -.
DR BioGRID-ORCS; 42265; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42265; -.
DR PRO; PR:Q8T390; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038659; Expressed in brain and 22 other tissues.
DR ExpressionAtlas; Q8T390; baseline and differential.
DR Genevisible; Q8T390; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:FlyBase.
DR GO; GO:0098793; C:presynapse; IBA:GO_Central.
DR GO; GO:0061174; C:type I terminal bouton; IDA:FlyBase.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IDA:FlyBase.
DR GO; GO:0005543; F:phospholipid binding; IDA:FlyBase.
DR GO; GO:0000045; P:autophagosome assembly; IMP:FlyBase.
DR GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
DR GO; GO:0150007; P:clathrin-dependent synaptic vesicle endocytosis; IMP:FlyBase.
DR GO; GO:0006897; P:endocytosis; IMP:FlyBase.
DR GO; GO:0097753; P:membrane bending; IDA:FlyBase.
DR GO; GO:0097749; P:membrane tubulation; IDA:FlyBase.
DR GO; GO:0097320; P:plasma membrane tubulation; IDA:FlyBase.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IMP:FlyBase.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:FlyBase.
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 Coiled coil; Cytoplasm; Endocytosis; Membrane; Phosphoprotein;
KW Reference proteome; RNA editing; SH3 domain.
FT CHAIN 1..369
FT /note="Endophilin-A"
FT /id="PRO_0000285838"
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"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VARIANT 129
FT /note="K -> R (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:11955450,
FT ECO:0000269|PubMed:17018572"
FT VARIANT 137
FT /note="K -> E (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:17018572"
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
