ID B4G4T7_DROPE Unreviewed; 461 AA. AC B4G4T7; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 80. DE SubName: Full=GL23309 {ECO:0000313|EMBL:EDW24603.1}; GN Name=Dper\GL23309 {ECO:0000313|EMBL:EDW24603.1}; GN ORFNames=Dper_GL23309 {ECO:0000313|EMBL:EDW24603.1}; OS Drosophila persimilis (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7234 {ECO:0000313|Proteomes:UP000008744}; RN [1] {ECO:0000313|EMBL:EDW24603.1, ECO:0000313|Proteomes:UP000008744} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSH-3 / Tucson 14011-0111.49 RC {ECO:0000313|Proteomes:UP000008744}; 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). CC -!- SUBCELLULAR LOCATION: Cell projection, filopodium CC {ECO:0000256|ARBA:ARBA00004486}. Cell projection, lamellipodium CC {ECO:0000256|ARBA:ARBA00004510}. CC -!- SIMILARITY: Belongs to the ABI family. {ECO:0000256|ARBA:ARBA00010020}. 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; CH479179; EDW24603.1; -; Genomic_DNA. DR RefSeq; XP_002013617.1; XM_002013581.1. DR AlphaFoldDB; B4G4T7; -. DR SMR; B4G4T7; -. DR STRING; 7234.B4G4T7; -. DR EnsemblMetazoa; FBtr0188924; FBpp0187416; FBgn0160899. DR GeneID; 6588612; -. DR KEGG; dpe:6588612; -. DR eggNOG; KOG2546; Eukaryota. DR HOGENOM; CLU_035421_0_0_1; -. DR OMA; TDHYRSN; -. DR OrthoDB; 3028771at2759; -. DR PhylomeDB; B4G4T7; -. DR Proteomes; UP000008744; Unassembled WGS sequence. DR GO; GO:0045180; C:basal cortex; IEA:EnsemblMetazoa. DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell. DR GO; GO:0031258; C:lamellipodium membrane; IEA:EnsemblMetazoa. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:EnsemblMetazoa. DR GO; GO:0031209; C:SCAR complex; IEA:EnsemblMetazoa. DR GO; GO:0045296; F:cadherin binding; IEA:EnsemblMetazoa. DR GO; GO:0048846; P:axon extension involved in axon guidance; IEA:EnsemblMetazoa. DR GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:EnsemblMetazoa. DR GO; GO:0021955; P:central nervous system neuron axonogenesis; IEA:EnsemblMetazoa. DR GO; GO:0060269; P:centripetally migrating follicle cell migration; IEA:EnsemblMetazoa. DR GO; GO:0022416; P:chaeta development; IEA:EnsemblMetazoa. DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:EnsemblMetazoa. DR GO; GO:0042247; P:establishment of planar polarity of follicular epithelium; IEA:EnsemblMetazoa. DR GO; GO:0030032; P:lamellipodium assembly; IEA:EnsemblMetazoa. DR GO; GO:0016203; P:muscle attachment; IEA:EnsemblMetazoa. DR GO; GO:0007528; P:neuromuscular junction development; IEA:EnsemblMetazoa. DR GO; GO:0072499; P:photoreceptor cell axon guidance; IEA:EnsemblMetazoa. DR GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:EnsemblMetazoa. DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblMetazoa. DR GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:EnsemblMetazoa. DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:EnsemblMetazoa. DR GO; GO:0008360; P:regulation of cell shape; IEA:EnsemblMetazoa. DR CDD; cd11826; SH3_Abi; 1. DR Gene3D; 6.10.140.1620; -; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR028457; ABI. DR InterPro; IPR028455; ABI3_SH3. DR InterPro; IPR012849; Abl-interactor_HHR_dom. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR000727; T_SNARE_dom. DR PANTHER; PTHR10460:SF0; ABELSON INTERACTING PROTEIN, ISOFORM D; 1. DR PANTHER; PTHR10460; ABL INTERACTOR FAMILY MEMBER; 1. DR Pfam; PF07815; Abi_HHR; 1. DR Pfam; PF14604; SH3_9; 1. DR PRINTS; PR00499; P67PHOX. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50002; SH3; 1. DR PROSITE; PS50192; T_SNARE; 1. PE 3: Inferred from homology; KW Cell projection {ECO:0000256|ARBA:ARBA00023273}; KW Reference proteome {ECO:0000313|Proteomes:UP000008744}; KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE- KW ProRule:PRU00192}. FT DOMAIN 45..107 FT /note="T-SNARE coiled-coil homology" FT /evidence="ECO:0000259|PROSITE:PS50192" FT DOMAIN 403..461 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" FT REGION 156..281 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 293..324 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 349..393 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 156..175 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 177..191 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 192..217 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 245..264 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 297..322 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 461 AA; 50665 MW; 0003AAE38A3B24C4 CRC64; MDELASLIRT EIPDGRQSLR DSYTNLERVA DYCEDTYYRA DNKKGALEAT KNYTTQSLAS VAYQINTLAY SYMQLLELQA QQLSEMESQM NHIAQTVHIH KEKVARREIG VLTANKVSSR QFKIVAPINP EKPIKYVRKP IDYSILDEIG HGINSAQHQV RQKHRGSSHG SVQSLIPPSV GPPPTTKPPT PPQMSRAGNT GTLGKSVSNT GTLGKSSREY RTPPVVNPPQ VPSHYAPNYP IGHPKRMSTA SSSTTMTTTT MGGGAAGNER AAGYSALPMP PSQQIATHVN LPSAGMMQSL PPPPPTTYDD RSSMPPPPSP LTVSQHEMTE QSHIGMHTLG RNINRNHFSL NFARPGSQSP PLPPPPPPED EHQDFGRPRT STGPQLAPIV PEDQNLPGWV PKNFIEKVVA IYDYYADKDD ELSFQESSVL YVLKKNDDGW WEGVMDGVTG LFPGNYVEPC V //