RG92B_DROME
ID RG92B_DROME Reviewed; 740 AA.
AC Q9VDS5; Q8T3Q3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Rho GTPase-activating protein 92B;
GN Name=RhoGAP92B; ORFNames=CG4755;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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 [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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-593 AND THR-595, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469; SER-473; SER-715;
RP THR-721; SER-738 AND SER-739, AND 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: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. {ECO:0000250}.
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DR EMBL; AE014297; AAF55715.1; -; Genomic_DNA.
DR EMBL; AY094653; AAM11006.1; -; mRNA.
DR RefSeq; NP_001287417.1; NM_001300488.1.
DR RefSeq; NP_650844.1; NM_142587.3.
DR AlphaFoldDB; Q9VDS5; -.
DR SMR; Q9VDS5; -.
DR BioGRID; 67360; 44.
DR IntAct; Q9VDS5; 3.
DR STRING; 7227.FBpp0083230; -.
DR iPTMnet; Q9VDS5; -.
DR PaxDb; Q9VDS5; -.
DR PRIDE; Q9VDS5; -.
DR DNASU; 42371; -.
DR EnsemblMetazoa; FBtr0083821; FBpp0083230; FBgn0038747.
DR EnsemblMetazoa; FBtr0344354; FBpp0310730; FBgn0038747.
DR GeneID; 42371; -.
DR KEGG; dme:Dmel_CG4755; -.
DR UCSC; CG4755-RA; d. melanogaster.
DR CTD; 42371; -.
DR FlyBase; FBgn0038747; RhoGAP92B.
DR VEuPathDB; VectorBase:FBgn0038747; -.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00940000172069; -.
DR InParanoid; Q9VDS5; -.
DR OMA; IESPRYG; -.
DR OrthoDB; 1511935at2759; -.
DR PhylomeDB; Q9VDS5; -.
DR Reactome; R-DME-8980692; RHOA GTPase cycle.
DR Reactome; R-DME-9013148; CDC42 GTPase cycle.
DR Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR Reactome; R-DME-9013405; RHOD GTPase cycle.
DR SignaLink; Q9VDS5; -.
DR BioGRID-ORCS; 42371; 0 hits in 3 CRISPR screens.
DR ChiTaRS; RhoGAP92B; fly.
DR GenomeRNAi; 42371; -.
DR PRO; PR:Q9VDS5; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038747; Expressed in embryonic/larval hemocyte (Drosophila) and 29 other tissues.
DR ExpressionAtlas; Q9VDS5; baseline and differential.
DR Genevisible; Q9VDS5; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0005096; F:GTPase activator activity; IDA:FlyBase.
DR GO; GO:0005543; F:phospholipid binding; ISS:FlyBase.
DR GO; GO:0017124; F:SH3 domain binding; IPI:FlyBase.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IMP:FlyBase.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:1900144; P:positive regulation of BMP secretion; IMP:FlyBase.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:FlyBase.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0008104; P:protein localization; IMP:FlyBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:1990255; P:subsynaptic reticulum organization; IMP:FlyBase.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Coiled coil; GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..740
FT /note="Rho GTPase-activating protein 92B"
FT /id="PRO_0000347177"
FT DOMAIN 13..266
FT /note="BAR"
FT DOMAIN 251..448
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 49..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..577
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..740
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 595
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 721
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 512
FT /note="I -> T (in Ref. 3; AAM11006)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 740 AA; 83085 MW; 079421624F2F4817 CRC64;
MKRQFAKIKI AAENLSRSSK SDSKDSELEA IERQVDRYRD TIEKIVRKLP ALSGGGGSGS
GSSEEQDKRT KKNSHYKIAQ ALDESAKELP KDMPLQKVLA NCGELEKTMA ECIIESELET
EAKVVRRLKN ILDKEIQEIS TLKRNVSRTL QEYTSLKRSH EAAIRLEEPA AKVNHIKSQQ
EECELKLEKE RDAWAAQMLE LIAKEDEIVS CIRDYVLNQR NYHERALQHV NASLARIQDT
IQGTEKSRFG TSLKEHLTST NREISYIVEL CCCCLLEHGL EEEGLLRVGC ASTKLRRMKH
ALEAQHVKTP LPLDYQDPHV IGSILKLYLR ELPEPLLTYN LYKDFIRIAE RHSEAERKTE
IKAILTKLPK ENYANLRYLT RFLSIVQQRS ALNKMSSQNL AIVMSPNMLW PRIDKSSNAP
ADYIGQVNSS SAANIIVELL ISQWDYFFIG EVEFYLTLQK QKLFVEGKSK SNSSNENLDR
NDSEVMESPR YGTLRRQKAN APSPPTTNGN GIIMTTSQTS HRPHAKELFP QQTPEKQEKP
AKPPLPNLPQ FQSPAASQPT QTQLEPLPPP PVTPAKPVPM TRTQFFGLDN LPSPTADRKS
TDSIGSFKLK PDVPQKPLLP KRPTVLGVGV PKADGKSDDE GGTTPTQATI DNGNGSVRFK
TEHFLDKLRQ ENGETNGTRE VSSTTKENNH NHDPPATAAD QNQQQAQPQV TTPISPNSFQ
TPKRPTVPAP PPPTNWKSSD
