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Database: UniProt
Entry: B4JT02_DROGR
LinkDB: B4JT02_DROGR
Original site: B4JT02_DROGR 
ID   B4JT02_DROGR            Unreviewed;       775 AA.
AC   B4JT02;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=GH16728 {ECO:0000313|EMBL:EDV94892.1};
GN   Name=Dgri\GH16728 {ECO:0000313|EMBL:EDV94892.1};
GN   ORFNames=Dgri_GH16728 {ECO:0000313|EMBL:EDV94892.1};
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222 {ECO:0000313|Proteomes:UP000001070};
RN   [1] {ECO:0000313|EMBL:EDV94892.1, ECO:0000313|Proteomes:UP000001070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00 {ECO:0000313|Proteomes:UP000001070};
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).
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DR   EMBL; CH916373; EDV94892.1; -; Genomic_DNA.
DR   RefSeq; XP_001994156.1; XM_001994120.1.
DR   AlphaFoldDB; B4JT02; -.
DR   STRING; 7222.B4JT02; -.
DR   EnsemblMetazoa; FBtr0152142; FBpp0150634; FBgn0124199.
DR   GeneID; 6567927; -.
DR   KEGG; dgr:6567927; -.
DR   eggNOG; KOG4270; Eukaryota.
DR   HOGENOM; CLU_022281_0_0_1; -.
DR   InParanoid; B4JT02; -.
DR   OMA; WDYFFEG; -.
DR   OrthoDB; 7959at2759; -.
DR   PhylomeDB; B4JT02; -.
DR   Proteomes; UP000001070; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0031594; C:neuromuscular junction; IEA:EnsemblMetazoa.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:EnsemblMetazoa.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:EnsemblMetazoa.
DR   GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:EnsemblMetazoa.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IEA:EnsemblMetazoa.
DR   GO; GO:1900144; P:positive regulation of BMP secretion; IEA:EnsemblMetazoa.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IEA:EnsemblMetazoa.
DR   GO; GO:0008104; P:protein localization; IEA:EnsemblMetazoa.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:1990255; P:subsynaptic reticulum organization; IEA:EnsemblMetazoa.
DR   CDD; cd07595; BAR_RhoGAP_Rich-like; 1.
DR   CDD; cd04386; RhoGAP_nadrin; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR047165; RHG17/44/SH3BP1-like.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR14130; 3BP-1 RELATED RHOGAP; 1.
DR   PANTHER; PTHR14130:SF14; RHO GTPASE-ACTIVATING PROTEIN 92B; 1.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001070}.
FT   DOMAIN          252..449
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          469..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          744..775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          126..153
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        476..492
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..521
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        540..555
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..610
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        758..775
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   775 AA;  87033 MW;  B0FB2A995846D27C CRC64;
     MKKQIAKIRI AAENLRSTKS DCKDSELETI EKQVDRYRDT IEKIVRKLPA LSSSGSSNNG
     IITTEEHDKR IKKNSHFKIA QALDESAKEL PRDMPLQKVL ANCGELEKTI AECSIESELE
     TETKVVRRLK NILDKEIQEI STLKRNVSRT LQEYTSLKKS YEASKRNEEP ASKLNHIKSQ
     QEECEVKLEK ERDAWAAQML ELIAKEDEIV NCIRDYVLNQ RNYHERALQH VNESLARIQD
     TIQSTEKTRF GTSLKDHLTS THRDISYIVE LCCCCLLEHG LEEEGLLRVG CASTKLRRMK
     HALEAQHVKT PLPLEYQDPH VIGSILKLYL RELPEPLLTY ALYKDFVRIA ELHTEAERKT
     AIKAVMGKLP KENYANLRYL TRFLALMQQS AVHNKMSSQN LAIVMSPNML WPRIDKSSNA
     PADYMGQVNS SSAANIIVEL LISQWDYFFD GEVEFYQTLQ RHKLFVEGKA KSNSSNENLN
     KHDSEVIESP RYGTLRRQKP NAPSPPTKLE ATTNGGGSNH SISHRPHAKE LFPQQQPTQQ
     PEDKHDKHEK QEKPAKPPLP ALVQLQQPAT YTQLEALSPP PVTPAKPVPM TRTQFFGLDN
     LPSPTADRKS IDSIGSFRLK PDVPQKPQLP KRPIVLAITS GGGPGSGSGP KGESKSDDEA
     TRLPQAHIDN GNGSVRYTTE KFLDKIRQEH CDTNGTREEA AMATAGITAT ATTATTTAAG
     SREENHNNTE QQPQQCLVIA EQITPTTPIS PNSFQTPKRP TVPAPPPPTI RKQAD
//
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