RG190_DROME
ID RG190_DROME Reviewed; 1561 AA.
AC Q9VX32; Q8MRC6; Q95VZ5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Rho GTPase-activating protein 190;
DE AltName: Full=Rho GTPase-activating protein of 190 kDa;
GN Name=RhoGAPp190; ORFNames=CG32555;
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 [MRNA] (ISOFORM 2), FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=11672527; DOI=10.1016/s0092-8674(01)00522-0;
RA Billuart P., Winter C.G., Maresh A., Zhao X., Luo L.;
RT "Regulating axon branch stability: the role of p190 RhoGAP in repressing a
RT retraction signaling pathway.";
RL Cell 107:195-207(2001).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [5]
RP ACTIVITY REGULATION.
RX PubMed=17227793; DOI=10.1242/jcs.03341;
RA Williams M.J., Habayeb M.S., Hultmark D.;
RT "Reciprocal regulation of Rac1 and Rho1 in Drosophila circulating immune
RT surveillance cells.";
RL J. Cell Sci. 120:502-511(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973; SER-975; SER-985;
RP SER-988 AND SER-996, 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-activating protein (GAP) for RhoA/Rho1 that plays an
CC essential role in the stability of dorsal branches of mushroom body
CC (MB) neurons. The MB neurons are the center for olfactory learning and
CC memory. Acts by converting RhoA/Rho1 to an inactive GDP-bound state,
CC leading to repress the RhoA/Rho1-Drok-MRLC signaling pathway thereby
CC maintaining axon branch stability. {ECO:0000269|PubMed:11672527}.
CC -!- ACTIVITY REGULATION: Negatively regulated by integrin, bsk and
CC Src/Src64B. {ECO:0000269|PubMed:11672527, ECO:0000269|PubMed:17227793}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9VX32-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9VX32-2; Sequence=VSP_037211;
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DR EMBL; AF387518; AAL01872.1; -; mRNA.
DR EMBL; AE014298; AAF48748.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF48749.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09591.1; -; Genomic_DNA.
DR EMBL; AY121666; AAM51993.1; -; mRNA.
DR RefSeq; NP_001259656.1; NM_001272727.1. [Q9VX32-2]
DR RefSeq; NP_573231.2; NM_133003.3. [Q9VX32-1]
DR RefSeq; NP_728089.1; NM_167572.2. [Q9VX32-1]
DR RefSeq; NP_728090.1; NM_167573.2. [Q9VX32-1]
DR AlphaFoldDB; Q9VX32; -.
DR SMR; Q9VX32; -.
DR BioGRID; 59069; 14.
DR IntAct; Q9VX32; 1.
DR STRING; 7227.FBpp0305817; -.
DR iPTMnet; Q9VX32; -.
DR EnsemblMetazoa; FBtr0074481; FBpp0074255; FBgn0026375. [Q9VX32-1]
DR EnsemblMetazoa; FBtr0074482; FBpp0074256; FBgn0026375. [Q9VX32-1]
DR EnsemblMetazoa; FBtr0074483; FBpp0074257; FBgn0026375. [Q9VX32-1]
DR EnsemblMetazoa; FBtr0333659; FBpp0305815; FBgn0026375. [Q9VX32-2]
DR GeneID; 32743; -.
DR KEGG; dme:Dmel_CG32555; -.
DR UCSC; CG32555-RA; d. melanogaster. [Q9VX32-1]
DR CTD; 32743; -.
DR FlyBase; FBgn0026375; RhoGAPp190.
DR VEuPathDB; VectorBase:FBgn0026375; -.
DR eggNOG; KOG4271; Eukaryota.
DR InParanoid; Q9VX32; -.
DR PhylomeDB; Q9VX32; -.
DR Reactome; R-DME-350407; RHO1 GTPase cycle.
DR Reactome; R-DME-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-DME-8980692; RHOA GTPase cycle.
DR Reactome; R-DME-9013026; RHOB GTPase cycle.
DR Reactome; R-DME-9013106; RHOC 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 Reactome; R-DME-9035034; RHOF GTPase cycle.
DR SignaLink; Q9VX32; -.
DR BioGRID-ORCS; 32743; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32743; -.
DR PRO; PR:Q9VX32; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0026375; Expressed in brain and 29 other tissues.
DR ExpressionAtlas; Q9VX32; baseline and differential.
DR Genevisible; Q9VX32; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IGI:FlyBase.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0030215; F:semaphorin receptor binding; IPI:FlyBase.
DR GO; GO:0007415; P:defasciculation of motor neuron axon; IMP:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0045792; P:negative regulation of cell size; IMP:FlyBase.
DR GO; GO:0050770; P:regulation of axonogenesis; IGI:FlyBase.
DR GO; GO:0008361; P:regulation of cell size; IBA:GO_Central.
DR GO; GO:0007266; P:Rho protein signal transduction; IGI:FlyBase.
DR Gene3D; 1.10.10.440; -; 2.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002713; FF_domain.
DR InterPro; IPR036517; FF_domain_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039007; pG1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR032835; RhoGAP-FF1.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR045786; RhoGAP_pG1_pG2.
DR InterPro; IPR039006; RhoGAP_pG2.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF16512; RhoGAP-FF1; 1.
DR Pfam; PF19518; RhoGAP_pG1_pG2; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51676; FF; 4.
DR PROSITE; PS51852; PG1; 1.
DR PROSITE; PS51853; PG2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Developmental protein;
KW GTPase activation; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1561
FT /note="Rho GTPase-activating protein 190"
FT /id="PRO_0000372856"
FT DOMAIN 252..320
FT /note="FF 1"
FT DOMAIN 365..419
FT /note="FF 2"
FT DOMAIN 426..480
FT /note="FF 3"
FT DOMAIN 482..547
FT /note="FF 4"
FT DOMAIN 592..765
FT /note="pG1 pseudoGTPase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01199"
FT DOMAIN 766..926
FT /note="pG2 pseudoGTPase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01200"
FT DOMAIN 1349..1552
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1054..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 975
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 985
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 988
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 996
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1253..1254
FT /note="PE -> PGEKK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11672527"
FT /id="VSP_037211"
FT CONFLICT 356
FT /note="D -> G (in Ref. 4; AAM51993)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="N -> Y (in Ref. 4; AAM51993)"
FT /evidence="ECO:0000305"
FT CONFLICT 580
FT /note="K -> E (in Ref. 4; AAM51993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1561 AA; 178772 MW; 9E28A17B6AF9E308 CRC64;
MRQFNISVIG LSGTEKDRGQ VGVGKSCLCN RFMRPMADDY FIDHISVLSQ SDFSGRIVNN
DHFLYWGDVR KTTEEGVEYQ FNIIEQTEFM DDSTFQAFKV GKMDPYSKRC TATKVFSAEK
LMYICKNQLG IEKEYEQKVM PDGRLSIDGF VVVFDVSPVP NRSVEKQVEF VQNVIATILK
NKKPLVLVTT KNDDAYELYV REAEKISQRK DYKSTVQLIE TSAHESINID LAFLLLAQMI
DKVKNRVKII SYQESAKSRK ELLDTRSEAV TRLIRNQITD YHVLWSQGSK MLSQYREWNE
FLNIFGHEAG QKLFRRHMKK LRDDHLNKKL HQYLDKFALA LEYLLPDIGA LNISDDDAWE
CARNYLQNHI EFEQYFFECP QASWTELVDM DEAEDEARIP FDVLETSEAE TVFRNYLNSV
QQDKKKIGWK QQFKMLLEES GFVTPGKQLS EVRVLFMGRE CFEALSEHDC QQIYDIHQDD
IIEKSKQNFV ELLLEHAQYF LQFKNVDNIT QEDVRQITDV IQEDSRYKML DRLDQERRLM
LVQHLRFIHC PIRDHCPFFY NCVDSLIEEV LSDKSASNHK TPSGGGWKSS GSGSDRTLNL
LIVGSEHLAS DLLNDIRICT GSKGEYIYEN QTYYLNYRIA NGDMEAFKAI DVYSSGLICV
YSNQQSFETL KDNLERTLLC NLELEDKFEN LPIVLVYQPQ DLKENEVEYL RNEGMRLSEM
LHCDFIDHTQ NHQKYVYDIL NIVILSLKLT EMKSYEPYPS NHTDLRILCC IFCGDQYDIE
NIVQPLVEES TLVKANEHSI IVDVFIGDAK RRVEFILSSY HGTSQYRDEL IHGYIYFYST
KRRSSLANLS ILAAQNANIP LQIIAVTESG GVNAFFNSDI CQFLITEGNA VADRFKGSFM
TFSADQYVKF AFYNPFLKTA WDNKYEVENL HVEESITLDS GEGTLENSVN QMPRPPPRHE
SYMLSNTLGT DGSGSENYEM APTRSLNSLN EERDISLDEI YDDNEKPKHL HQKWLEDKSD
GRRNMNKNLI WNNFSGSTHA YTTGRRHIDS NLNKIRPKGP SQTLKVGEAP SRNCPAMSSS
TFTLPTQQPG KLNMKNFQLV SDAVAKMNFT GSGSGSGSGS GSGSTGLGLG LGSGSGCMGD
SFLEPVDKDG KRYDHAQLDG EDEDSEELAE YEQIYENEDC TESDSCASST ERRVRQQNAY
YKASKKPVAA KKQKKKKVAI PVQTPRVPPF GSYVSPPEIP LHYQRMAVGG SGPEKPEPCV
PEFMKSDKSP EYSMVPELAG AGIFGAENLP EYNMNQAKCL KDFEKLEKRR IKEETARQRK
LQEKEKEQEK KLKRKLKQNA KGLVESAEAQ FGKLMITSEQ GEIPIFLNKC VEFIEKEGLD
SEGIYRVPGS RAHVDMLFQR FEEDTNTEID ALDIPVNAVA TALKDFFSKR LPPLFSKDII
KELEEIAGSR GVGNSKLNVE VKTDRSCRLI ALKSLLQKLP PINFAILKYI FQHFVHVSDN
SKLNSMDSKN LAICWWPTLI PIDFTDMGHF EQLRPYLEDI VQTMIDQFPY LFCGKDAFVM
V
