GenomeNet

Database: UniProt
Entry: RG190_DROME
LinkDB: RG190_DROME
Original site: 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   18-SEP-2019, entry version 144.
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;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND ACTIVITY
RP   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
RT   repressing a 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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic 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.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., 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
RT   immune 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
CC       an essential role in the stability of dorsal branches of mushroom
CC       body (MB) neurons. The MB neurons are the center for olfactory
CC       learning and memory. Acts by converting RhoA/Rho1 to an inactive
CC       GDP-bound state, leading to repress the RhoA/Rho1-Drok-MRLC
CC       signaling pathway thereby maintaining axon branch stability.
CC       {ECO:0000269|PubMed:11672527}.
CC   -!- ACTIVITY REGULATION: Negatively regulated by integrin, bsk and
CC       Src/Src64B. {ECO:0000269|PubMed:11672527,
CC       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;
CC         Note=No experimental confirmation available.;
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   SMR; Q9VX32; -.
DR   BioGrid; 59069; 14.
DR   IntAct; Q9VX32; 1.
DR   STRING; 7227.FBpp0305817; -.
DR   iPTMnet; Q9VX32; -.
DR   PRIDE; 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   InParanoid; Q9VX32; -.
DR   PhylomeDB; Q9VX32; -.
DR   Reactome; R-DME-194840; Rho GTPase cycle.
DR   Reactome; R-DME-350407; RHO1 GTPase cycle.
DR   Reactome; R-DME-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR   GenomeRNAi; 32743; -.
DR   PRO; PR:Q9VX32; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0026375; Expressed in 32 organ(s), highest expression level in brain.
DR   ExpressionAtlas; Q9VX32; differential.
DR   Genevisible; Q9VX32; DM.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0007266; P:Rho protein signal transduction; IGI:FlyBase.
DR   Gene3D; 1.10.10.440; -; 2.
DR   Gene3D; 1.10.555.10; -; 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; 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   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; Complete proteome;
KW   Developmental protein; GTPase activation; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN         1   1561       Rho GTPase-activating protein 190.
FT                                /FTId=PRO_0000372856.
FT   DOMAIN      252    320       FF 1.
FT   DOMAIN      365    419       FF 2.
FT   DOMAIN      426    480       FF 3.
FT   DOMAIN      482    547       FF 4.
FT   DOMAIN      592    765       pG1 pseudoGTPase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01199}.
FT   DOMAIN      766    926       pG2 pseudoGTPase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01200}.
FT   DOMAIN     1349   1552       Rho-GAP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00172}.
FT   COMPBIAS   1211   1217       Poly-Lys.
FT   MOD_RES     973    973       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     975    975       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     985    985       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     988    988       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     996    996       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   VAR_SEQ    1253   1254       PE -> PGEKK (in isoform 2).
FT                                {ECO:0000303|PubMed:11672527}.
FT                                /FTId=VSP_037211.
FT   CONFLICT    356    356       D -> G (in Ref. 4; AAM51993).
FT                                {ECO:0000305}.
FT   CONFLICT    505    505       N -> Y (in Ref. 4; AAM51993).
FT                                {ECO:0000305}.
FT   CONFLICT    580    580       K -> E (in Ref. 4; AAM51993).
FT                                {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
//
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