ID A0A0Q9WCP0_DROVI Unreviewed; 369 AA. AC A0A0Q9WCP0; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-OCT-2020, entry version 36. DE RecName: Full=Endophilin-A {ECO:0000256|ARBA:ARBA00018286}; DE AltName: Full=SH3 domain-containing GRB2-like protein {ECO:0000256|ARBA:ARBA00017039}; GN Name=Dvir\endoA {ECO:0000313|EMBL:KRF78373.1}; GN ORFNames=Dvir_GJ14546 {ECO:0000313|EMBL:KRF78373.1}; OS Drosophila virilis (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila. OX NCBI_TaxID=7244 {ECO:0000313|EMBL:KRF78373.1, ECO:0000313|Proteomes:UP000008792}; RN [1] {ECO:0000313|EMBL:KRF78373.1, ECO:0000313|Proteomes:UP000008792} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:KRF78373.1}, and Tucson RC 15010-1051.87 {ECO:0000313|Proteomes:UP000008792}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 Genomes Consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A., RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B., RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M., RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R., RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P., RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J., RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K., RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L., RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G., RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B., RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J., RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R., RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E., RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K., RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H., RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F., RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M., RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L., RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M., RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G., RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R., RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D., RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A., RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J., RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A., RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T., RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B., RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W., RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W., RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L., RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J., RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D., RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P., RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A., RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M., RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K., RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J., RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A., RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R., RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L., RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C., RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L., RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F., RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T., RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J., RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S., RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I., RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). RN [2] {ECO:0000313|EMBL:KRF78373.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:KRF78373.1}; RX PubMed=18057021; DOI=10.1093/bioinformatics/btm542; RA Zimin A.V., Smith D.R., Sutton G., Yorke J.A.; RT "Assembly reconciliation."; RL Bioinformatics 24:42-45(2008). RN [3] {ECO:0000313|EMBL:KRF78373.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:KRF78373.1}; RG FlyBase; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Required presynaptically at the neuromuscular junction. CC Implicated in synaptic vesicle endocytosis. CC {ECO:0000256|ARBA:ARBA00003037}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. CC -!- SIMILARITY: Belongs to the endophilin family. CC {ECO:0000256|ARBA:ARBA00006697}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CH940656; KRF78372.1; -; Genomic_DNA. DR EMBL; CH940656; KRF78373.1; -; Genomic_DNA. DR EMBL; CH940656; KRF78374.1; -; Genomic_DNA. DR EMBL; CH940656; KRF78375.1; -; 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 SMR; A0A0Q9WCP0; -. 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 KO; K11247; -. DR OMA; PYPQTEG; -. DR OrthoDB; 788657at2759; -. DR Proteomes; UP000008792; Unassembled WGS sequence. 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; IEA:EnsemblMetazoa. 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; IEA:EnsemblMetazoa. 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 {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils}; KW Endocytosis {ECO:0000256|ARBA:ARBA00022583}; KW Reference proteome {ECO:0000313|Proteomes:UP000008792}; KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE- KW ProRule:PRU00192}. FT DOMAIN 18..248 FT /note="BAR" FT /evidence="ECO:0000259|PROSITE:PS51021" FT DOMAIN 305..364 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" FT REGION 275..297 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 229..249 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 276..297 FT /note="Polar" 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 //