GenomeNet

Database: UniProt
Entry: B3NV58_DROER
LinkDB: B3NV58_DROER
Original site: B3NV58_DROER 
ID   B3NV58_DROER            Unreviewed;       492 AA.
AC   B3NV58;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 85.
DE   SubName: Full=Uncharacterized protein, isoform A {ECO:0000313|EMBL:EDV45906.1};
GN   Name=Dere\GG18490 {ECO:0000313|EMBL:EDV45906.1};
GN   ORFNames=Dere_GG18490 {ECO:0000313|EMBL:EDV45906.1};
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220 {ECO:0000313|EMBL:EDV45906.1};
RN   [1] {ECO:0000313|EMBL:EDV45906.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV45906.1};
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:EDV45906.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV45906.1};
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:EDV45906.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#14021-0224.01 {ECO:0000313|EMBL:EDV45906.1};
RG   FlyBase;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CH954180; EDV45906.1; -; Genomic_DNA.
DR   RefSeq; XP_001976979.1; XM_001976943.2.
DR   AlphaFoldDB; B3NV58; -.
DR   EnsemblMetazoa; FBtr0138544; FBpp0137036; FBgn0110703.
DR   GeneID; 6550924; -.
DR   KEGG; der:6550924; -.
DR   eggNOG; KOG1453; Eukaryota.
DR   HOGENOM; CLU_015883_0_0_1; -.
DR   OMA; HCKTIFA; -.
DR   OrthoDB; 5395569at2759; -.
DR   PhylomeDB; B3NV58; -.
DR   Proteomes; UP000008711; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048749; P:compound eye development; IEA:EnsemblMetazoa.
DR   GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:1903392; P:negative regulation of adherens junction organization; IEA:EnsemblMetazoa.
DR   GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IEA:EnsemblMetazoa.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:EnsemblMetazoa.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd20806; C1_CHN; 1.
DR   CDD; cd10352; SH2_a2chimerin_b2chimerin; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR035840; Chimaerin_SH2.
DR   InterPro; IPR017356; CHN1/CHN2.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   PANTHER; PTHR46075; CHIMERIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR46075:SF2; RHO GTPASE ACTIVATING PROTEIN AT 5A, ISOFORM A; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PIRSF; PIRSF038015; N-chimaerin; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          82..155
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          239..289
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          302..489
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..224
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  55004 MW;  A2BE43BF61A60CDD CRC64;
     MPRNTEAGAG SAVTGGVGGV GGAPEPSSPV QKVWKPELYK LQLEAPAPCP LRCQRTLPLP
     PAKSTAEAVE ANNLAGRLYG SEYHGLMGHL EAEQLLANAR DGSYFVRRSP QSDGYYTLSL
     RFNKRPKHYK LLYKPGVGHY LRGQDKRFDT VHDMVADGLI NFHMQLHASP IIQQINQQTK
     NCYQQSPYMT LNGRKLRALS NELGKANAKE SLPAEEKEQK QEEPPPPALD PMPLVYEKPH
     HFKVHNFKGL NWCEFCANFL WGFTAQGVKC EACGFVAHSK CSELVPPKCV PDLKRIRGVF
     GTDLTTMVQL ESHHQIPFVV RRCVEEVEAR GMLQEGIYRV SGFFDEIEAL KLALDREGEK
     TDMSETAYGN VNVIAGTLKL YLRLLPVPLI TFQAYPSFMA AGRTSNQAEQ RQLMAEAVRR
     LPPAHHSCLQ YMLEHLKRVA SHYAVNKMNE HNLATVFAPT LIATPQHMTN LTEEIFMLSS
     LITHCNTIFA PS
//
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