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   24-JAN-2024, entry version 162.
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   PaxDb; 7227-FBpp0305817; -.
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   AGR; FB:FBgn0026375; -.
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-9013148; CDC42 GTPase cycle.
DR   Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR   Reactome; R-DME-9013405; RHOD GTPase cycle.
DR   Reactome; R-DME-9013406; RHOQ GTPase cycle.
DR   Reactome; R-DME-9013409; RHOJ GTPase cycle.
DR   Reactome; R-DME-9013423; RAC3 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 cell types or 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   CDD; cd22207; pseudoGTPaseD_p190RhoGAP; 1.
DR   CDD; cd04373; RhoGAP_p190; 1.
DR   Gene3D; 1.10.10.440; FF domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 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   PANTHER; PTHR46005; RHO GTPASE-ACTIVATING PROTEIN 190; 1.
DR   PANTHER; PTHR46005:SF4; RHO GTPASE-ACTIVATING PROTEIN 190; 1.
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; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//

ID   M9PHG0_DROME            Unreviewed;      1564 AA.
AC   M9PHG0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Rho GTPase activating protein p190, isoform D {ECO:0000313|EMBL:AGB95498.1};
GN   Name=RhoGAPp190 {ECO:0000313|EMBL:AGB95498.1,
GN   ECO:0000313|FlyBase:FBgn0026375};
GN   Synonyms=8267 {ECO:0000313|EMBL:AGB95498.1}, BcDNA:GH17919
GN   {ECO:0000313|EMBL:AGB95498.1}, BcDNA:GM05133
GN   {ECO:0000313|EMBL:AGB95498.1}, CG8240 {ECO:0000313|EMBL:AGB95498.1},
GN   CG8267 {ECO:0000313|EMBL:AGB95498.1}, D-p190
GN   {ECO:0000313|EMBL:AGB95498.1}, Dmel\CG32555
GN   {ECO:0000313|EMBL:AGB95498.1}, DRhoGAP {ECO:0000313|EMBL:AGB95498.1},
GN   mdcds_56566 {ECO:0000313|EMBL:AGB95498.1}, p190
GN   {ECO:0000313|EMBL:AGB95498.1}, p190 RhoGAP
GN   {ECO:0000313|EMBL:AGB95498.1}, p190-RhoGAP
GN   {ECO:0000313|EMBL:AGB95498.1}, p190RhoGAP
GN   {ECO:0000313|EMBL:AGB95498.1}, RhoGAP {ECO:0000313|EMBL:AGB95498.1},
GN   RhoGAP P190 {ECO:0000313|EMBL:AGB95498.1}, RhoGAP-16B12
GN   {ECO:0000313|EMBL:AGB95498.1};
GN   ORFNames=CG32555 {ECO:0000313|EMBL:AGB95498.1,
GN   ECO:0000313|FlyBase:FBgn0026375}, Dmel_CG32555
GN   {ECO:0000313|EMBL:AGB95498.1};
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 {ECO:0000313|EMBL:AGB95498.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AGB95498.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J., 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., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA   Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA   Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA   Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA   Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA   Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA   Zhu X., 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   [2] {ECO:0000313|EMBL:AGB95498.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT   euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [3] {ECO:0000313|EMBL:AGB95498.1, ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|EMBL:AGB95498.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA   Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin: a
RT   genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN   [5] {ECO:0000313|EMBL:AGB95498.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [6] {ECO:0000313|EMBL:AGB95498.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [7] {ECO:0000313|EMBL:AGB95498.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [8] {ECO:0000313|EMBL:AGB95498.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
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DR   EMBL; AE014298; AGB95498.1; -; Genomic_DNA.
DR   RefSeq; NP_001259656.1; NM_001272727.1.
DR   SMR; M9PHG0; -.
DR   EnsemblMetazoa; FBtr0333659; FBpp0305815; FBgn0026375.
DR   GeneID; 32743; -.
DR   AGR; FB:FBgn0026375; -.
DR   CTD; 32743; -.
DR   FlyBase; FBgn0026375; RhoGAPp190.
DR   VEuPathDB; VectorBase:FBgn0026375; -.
DR   OrthoDB; 5405671at2759; -.
DR   BioGRID-ORCS; 32743; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 32743; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0026375; Expressed in brain and 29 other cell types or tissues.
DR   ExpressionAtlas; M9PHG0; baseline and differential.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd22207; pseudoGTPaseD_p190RhoGAP; 1.
DR   CDD; cd04373; RhoGAP_p190; 1.
DR   Gene3D; 1.10.10.440; FF domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 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   PANTHER; PTHR46005; RHO GTPASE-ACTIVATING PROTEIN 190; 1.
DR   PANTHER; PTHR46005:SF4; RHO GTPASE-ACTIVATING PROTEIN 190; 1.
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; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51676; FF; 3.
DR   PROSITE; PS51852; PG1; 1.
DR   PROSITE; PS51853; PG2; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:M9PHG0};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          365..419
FT                   /note="FF"
FT                   /evidence="ECO:0000259|PROSITE:PS51676"
FT   DOMAIN          426..480
FT                   /note="FF"
FT                   /evidence="ECO:0000259|PROSITE:PS51676"
FT   DOMAIN          482..547
FT                   /note="FF"
FT                   /evidence="ECO:0000259|PROSITE:PS51676"
FT   DOMAIN          592..765
FT                   /note="PG1 pseudoGTPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51852"
FT   DOMAIN          766..926
FT                   /note="PG2 pseudoGTPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51853"
FT   DOMAIN          1352..1555
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1054..1074
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1314..1349
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1564 AA;  179086 MW;  0830E9C6503FD327 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 SGPGEKKKPE
     PCVPEFMKSD KSPEYSMVPE LAGAGIFGAE NLPEYNMNQA KCLKDFEKLE KRRIKEETAR
     QRKLQEKEKE QEKKLKRKLK QNAKGLVESA EAQFGKLMIT SEQGEIPIFL NKCVEFIEKE
     GLDSEGIYRV PGSRAHVDML FQRFEEDTNT EIDALDIPVN AVATALKDFF SKRLPPLFSK
     DIIKELEEIA GSRGVGNSKL NVEVKTDRSC RLIALKSLLQ KLPPINFAIL KYIFQHFVHV
     SDNSKLNSMD SKNLAICWWP TLIPIDFTDM GHFEQLRPYL EDIVQTMIDQ FPYLFCGKDA
     FVMV
//

ID   M9PHV3_DROME            Unreviewed;      1621 AA.
AC   M9PHV3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Rho GTPase activating protein p190, isoform F {ECO:0000313|EMBL:AGB95500.1};
GN   Name=RhoGAPp190 {ECO:0000313|EMBL:AGB95500.1,
GN   ECO:0000313|FlyBase:FBgn0026375};
GN   Synonyms=8267 {ECO:0000313|EMBL:AGB95500.1}, BcDNA:GH17919
GN   {ECO:0000313|EMBL:AGB95500.1}, BcDNA:GM05133
GN   {ECO:0000313|EMBL:AGB95500.1}, CG8240 {ECO:0000313|EMBL:AGB95500.1},
GN   CG8267 {ECO:0000313|EMBL:AGB95500.1}, D-p190
GN   {ECO:0000313|EMBL:AGB95500.1}, Dmel\CG32555
GN   {ECO:0000313|EMBL:AGB95500.1}, DRhoGAP {ECO:0000313|EMBL:AGB95500.1},
GN   mdcds_56566 {ECO:0000313|EMBL:AGB95500.1}, p190
GN   {ECO:0000313|EMBL:AGB95500.1}, p190 RhoGAP
GN   {ECO:0000313|EMBL:AGB95500.1}, p190-RhoGAP
GN   {ECO:0000313|EMBL:AGB95500.1}, p190RhoGAP
GN   {ECO:0000313|EMBL:AGB95500.1}, RhoGAP {ECO:0000313|EMBL:AGB95500.1},
GN   RhoGAP P190 {ECO:0000313|EMBL:AGB95500.1}, RhoGAP-16B12
GN   {ECO:0000313|EMBL:AGB95500.1};
GN   ORFNames=CG32555 {ECO:0000313|EMBL:AGB95500.1,
GN   ECO:0000313|FlyBase:FBgn0026375}, Dmel_CG32555
GN   {ECO:0000313|EMBL:AGB95500.1};
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 {ECO:0000313|EMBL:AGB95500.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AGB95500.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J., 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., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA   Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA   Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA   Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA   Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA   Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA   Zhu X., 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   [2] {ECO:0000313|EMBL:AGB95500.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT   euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [3] {ECO:0000313|EMBL:AGB95500.1, ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|EMBL:AGB95500.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA   Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin: a
RT   genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN   [5] {ECO:0000313|EMBL:AGB95500.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [6] {ECO:0000313|EMBL:AGB95500.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [7] {ECO:0000313|EMBL:AGB95500.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [8] {ECO:0000313|EMBL:AGB95500.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014298; AGB95500.1; -; Genomic_DNA.
DR   RefSeq; NP_001259658.1; NM_001272729.1.
DR   SMR; M9PHV3; -.
DR   EnsemblMetazoa; FBtr0333661; FBpp0305817; FBgn0026375.
DR   GeneID; 32743; -.
DR   AGR; FB:FBgn0026375; -.
DR   CTD; 32743; -.
DR   FlyBase; FBgn0026375; RhoGAPp190.
DR   VEuPathDB; VectorBase:FBgn0026375; -.
DR   OMA; MRNSFGG; -.
DR   OrthoDB; 5405671at2759; -.
DR   BioGRID-ORCS; 32743; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 32743; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0026375; Expressed in brain and 29 other cell types or tissues.
DR   ExpressionAtlas; M9PHV3; baseline and differential.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd22207; pseudoGTPaseD_p190RhoGAP; 1.
DR   CDD; cd04373; RhoGAP_p190; 1.
DR   Gene3D; 1.10.10.440; FF domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 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   PANTHER; PTHR46005; RHO GTPASE-ACTIVATING PROTEIN 190; 1.
DR   PANTHER; PTHR46005:SF4; RHO GTPASE-ACTIVATING PROTEIN 190; 1.
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; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51676; FF; 3.
DR   PROSITE; PS51852; PG1; 1.
DR   PROSITE; PS51853; PG2; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:M9PHV3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          365..419
FT                   /note="FF"
FT                   /evidence="ECO:0000259|PROSITE:PS51676"
FT   DOMAIN          426..480
FT                   /note="FF"
FT                   /evidence="ECO:0000259|PROSITE:PS51676"
FT   DOMAIN          482..547
FT                   /note="FF"
FT                   /evidence="ECO:0000259|PROSITE:PS51676"
FT   DOMAIN          592..765
FT                   /note="PG1 pseudoGTPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51852"
FT   DOMAIN          766..926
FT                   /note="PG2 pseudoGTPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51853"
FT   DOMAIN          1409..1612
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1110..1131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1371..1406
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1621 AA;  185228 MW;  55224B90738F393B 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 HQRFQIFPPP
     TTPPEPAPPD HQLITCTYKS QFVSASESSL EEITSDVSGS KDSLATHDAE WLEDKSDGRR
     NMNKNLIWNN FSGSTHAYTT GRRHIDSNLN KIRPKGPSQT LKVGEAPSRN CPAMSSSTFT
     LPTQQPGKLN MKNFQLVSDA VAKMNFTGSG SGSGSGSGSG STGLGLGLGS GSGCMGDSFL
     EPVDKDGKRY DHAQLDGEDE DSEELAEYEQ IYENEDCTES DSCASSTERR VRQQNAYYKA
     SKKPVAAKKQ KKKKVAIPVQ TPRVPPFGSY VSPPEIPLHY QRMAVGGSGP GEKKKPEPCV
     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
//

ID   M9PHY4_DROME            Unreviewed;      1579 AA.
AC   M9PHY4;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Rho GTPase activating protein p190, isoform E {ECO:0000313|EMBL:AGB95499.1};
GN   Name=RhoGAPp190 {ECO:0000313|EMBL:AGB95499.1,
GN   ECO:0000313|FlyBase:FBgn0026375};
GN   Synonyms=8267 {ECO:0000313|EMBL:AGB95499.1}, BcDNA:GH17919
GN   {ECO:0000313|EMBL:AGB95499.1}, BcDNA:GM05133
GN   {ECO:0000313|EMBL:AGB95499.1}, CG8240 {ECO:0000313|EMBL:AGB95499.1},
GN   CG8267 {ECO:0000313|EMBL:AGB95499.1}, D-p190
GN   {ECO:0000313|EMBL:AGB95499.1}, Dmel\CG32555
GN   {ECO:0000313|EMBL:AGB95499.1}, DRhoGAP {ECO:0000313|EMBL:AGB95499.1},
GN   mdcds_56566 {ECO:0000313|EMBL:AGB95499.1}, p190
GN   {ECO:0000313|EMBL:AGB95499.1}, p190 RhoGAP
GN   {ECO:0000313|EMBL:AGB95499.1}, p190-RhoGAP
GN   {ECO:0000313|EMBL:AGB95499.1}, p190RhoGAP
GN   {ECO:0000313|EMBL:AGB95499.1}, RhoGAP {ECO:0000313|EMBL:AGB95499.1},
GN   RhoGAP P190 {ECO:0000313|EMBL:AGB95499.1}, RhoGAP-16B12
GN   {ECO:0000313|EMBL:AGB95499.1};
GN   ORFNames=CG32555 {ECO:0000313|EMBL:AGB95499.1,
GN   ECO:0000313|FlyBase:FBgn0026375}, Dmel_CG32555
GN   {ECO:0000313|EMBL:AGB95499.1};
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 {ECO:0000313|EMBL:AGB95499.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AGB95499.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J., 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., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA   Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA   Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA   Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA   Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA   Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA   Zhu X., 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   [2] {ECO:0000313|EMBL:AGB95499.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT   euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [3] {ECO:0000313|EMBL:AGB95499.1, ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|EMBL:AGB95499.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA   Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin: a
RT   genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN   [5] {ECO:0000313|EMBL:AGB95499.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [6] {ECO:0000313|EMBL:AGB95499.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [7] {ECO:0000313|EMBL:AGB95499.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [8] {ECO:0000313|EMBL:AGB95499.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014298; AGB95499.1; -; Genomic_DNA.
DR   RefSeq; NP_001259657.1; NM_001272728.1.
DR   SMR; M9PHY4; -.
DR   EnsemblMetazoa; FBtr0333660; FBpp0305816; FBgn0026375.
DR   GeneID; 32743; -.
DR   AGR; FB:FBgn0026375; -.
DR   CTD; 32743; -.
DR   FlyBase; FBgn0026375; RhoGAPp190.
DR   VEuPathDB; VectorBase:FBgn0026375; -.
DR   OrthoDB; 5405671at2759; -.
DR   BioGRID-ORCS; 32743; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 32743; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0026375; Expressed in brain and 29 other cell types or tissues.
DR   ExpressionAtlas; M9PHY4; baseline and differential.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd22207; pseudoGTPaseD_p190RhoGAP; 1.
DR   CDD; cd04373; RhoGAP_p190; 1.
DR   Gene3D; 1.10.10.440; FF domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 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   PANTHER; PTHR46005; RHO GTPASE-ACTIVATING PROTEIN 190; 1.
DR   PANTHER; PTHR46005:SF4; RHO GTPASE-ACTIVATING PROTEIN 190; 1.
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; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51676; FF; 3.
DR   PROSITE; PS51852; PG1; 1.
DR   PROSITE; PS51853; PG2; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:M9PHY4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          365..419
FT                   /note="FF"
FT                   /evidence="ECO:0000259|PROSITE:PS51676"
FT   DOMAIN          426..480
FT                   /note="FF"
FT                   /evidence="ECO:0000259|PROSITE:PS51676"
FT   DOMAIN          482..547
FT                   /note="FF"
FT                   /evidence="ECO:0000259|PROSITE:PS51676"
FT   DOMAIN          592..765
FT                   /note="PG1 pseudoGTPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51852"
FT   DOMAIN          766..926
FT                   /note="PG2 pseudoGTPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51853"
FT   DOMAIN          1367..1570
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          966..985
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1065..1089
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1329..1364
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1579 AA;  180572 MW;  37653289998EED6F 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 HQTDVSGSKD
     SLATHDAEWL EDKSDGRRNM NKNLIWNNFS GSTHAYTTGR RHIDSNLNKI RPKGPSQTLK
     VGEAPSRNCP AMSSSTFTLP TQQPGKLNMK NFQLVSDAVA KMNFTGSGSG SGSGSGSGST
     GLGLGLGSGS GCMGDSFLEP VDKDGKRYDH AQLDGEDEDS EELAEYEQIY ENEDCTESDS
     CASSTERRVR QQNAYYKASK KPVAAKKQKK KKVAIPVQTP RVPPFGSYVS PPEIPLHYQR
     MAVGGSGPGE KKKPEPCVPE FMKSDKSPEY SMVPELAGAG IFGAENLPEY NMNQAKCLKD
     FEKLEKRRIK EETARQRKLQ EKEKEQEKKL KRKLKQNAKG LVESAEAQFG KLMITSEQGE
     IPIFLNKCVE FIEKEGLDSE GIYRVPGSRA HVDMLFQRFE EDTNTEIDAL DIPVNAVATA
     LKDFFSKRLP PLFSKDIIKE LEEIAGSRGV GNSKLNVEVK TDRSCRLIAL KSLLQKLPPI
     NFAILKYIFQ HFVHVSDNSK LNSMDSKNLA ICWWPTLIPI DFTDMGHFEQ LRPYLEDIVQ
     TMIDQFPYLF CGKDAFVMV
//

ID   M9PJQ3_DROME            Unreviewed;      1398 AA.
AC   M9PJQ3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Rho GTPase activating protein p190, isoform G {ECO:0000313|EMBL:AGB95501.1};
GN   Name=RhoGAPp190 {ECO:0000313|EMBL:AGB95501.1,
GN   ECO:0000313|FlyBase:FBgn0026375};
GN   Synonyms=8267 {ECO:0000313|EMBL:AGB95501.1}, BcDNA:GH17919
GN   {ECO:0000313|EMBL:AGB95501.1}, BcDNA:GM05133
GN   {ECO:0000313|EMBL:AGB95501.1}, CG8240 {ECO:0000313|EMBL:AGB95501.1},
GN   CG8267 {ECO:0000313|EMBL:AGB95501.1}, D-p190
GN   {ECO:0000313|EMBL:AGB95501.1}, Dmel\CG32555
GN   {ECO:0000313|EMBL:AGB95501.1}, DRhoGAP {ECO:0000313|EMBL:AGB95501.1},
GN   mdcds_56566 {ECO:0000313|EMBL:AGB95501.1}, p190
GN   {ECO:0000313|EMBL:AGB95501.1}, p190 RhoGAP
GN   {ECO:0000313|EMBL:AGB95501.1}, p190-RhoGAP
GN   {ECO:0000313|EMBL:AGB95501.1}, p190RhoGAP
GN   {ECO:0000313|EMBL:AGB95501.1}, RhoGAP {ECO:0000313|EMBL:AGB95501.1},
GN   RhoGAP P190 {ECO:0000313|EMBL:AGB95501.1}, RhoGAP-16B12
GN   {ECO:0000313|EMBL:AGB95501.1};
GN   ORFNames=CG32555 {ECO:0000313|EMBL:AGB95501.1,
GN   ECO:0000313|FlyBase:FBgn0026375}, Dmel_CG32555
GN   {ECO:0000313|EMBL:AGB95501.1};
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 {ECO:0000313|EMBL:AGB95501.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AGB95501.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J., 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., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA   Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA   Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA   Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA   Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA   Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA   Zhu X., 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   [2] {ECO:0000313|EMBL:AGB95501.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT   euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [3] {ECO:0000313|EMBL:AGB95501.1, ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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] {ECO:0000313|EMBL:AGB95501.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA   Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin: a
RT   genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN   [5] {ECO:0000313|EMBL:AGB95501.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [6] {ECO:0000313|EMBL:AGB95501.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [7] {ECO:0000313|EMBL:AGB95501.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [8] {ECO:0000313|EMBL:AGB95501.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
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DR   EMBL; AE014298; AGB95501.1; -; Genomic_DNA.
DR   RefSeq; NP_001259659.1; NM_001272730.1.
DR   SMR; M9PJQ3; -.
DR   EnsemblMetazoa; FBtr0333662; FBpp0305818; FBgn0026375.
DR   GeneID; 32743; -.
DR   AGR; FB:FBgn0026375; -.
DR   CTD; 32743; -.
DR   FlyBase; FBgn0026375; RhoGAPp190.
DR   VEuPathDB; VectorBase:FBgn0026375; -.
DR   HOGENOM; CLU_004268_0_0_1; -.
DR   OrthoDB; 5405671at2759; -.
DR   BioGRID-ORCS; 32743; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 32743; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0026375; Expressed in brain and 29 other cell types or tissues.
DR   ExpressionAtlas; M9PJQ3; baseline and differential.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd22207; pseudoGTPaseD_p190RhoGAP; 1.
DR   CDD; cd04373; RhoGAP_p190; 1.
DR   Gene3D; 1.10.10.440; FF domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 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   PANTHER; PTHR46005; RHO GTPASE-ACTIVATING PROTEIN 190; 1.
DR   PANTHER; PTHR46005:SF4; RHO GTPASE-ACTIVATING PROTEIN 190; 1.
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; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51676; FF; 3.
DR   PROSITE; PS51852; PG1; 1.
DR   PROSITE; PS51853; PG2; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:M9PJQ3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          365..419
FT                   /note="FF"
FT                   /evidence="ECO:0000259|PROSITE:PS51676"
FT   DOMAIN          426..480
FT                   /note="FF"
FT                   /evidence="ECO:0000259|PROSITE:PS51676"
FT   DOMAIN          482..547
FT                   /note="FF"
FT                   /evidence="ECO:0000259|PROSITE:PS51676"
FT   DOMAIN          592..765
FT                   /note="PG1 pseudoGTPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51852"
FT   DOMAIN          766..926
FT                   /note="PG2 pseudoGTPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51853"
FT   DOMAIN          1186..1389
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   COILED          1148..1183
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1398 AA;  161231 MW;  7E0E8460FE04E304 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 HQNCTESDSC
     ASSTERRVRQ QNAYYKASKK PVAAKKQKKK KVAIPVQTPR VPPFGSYVSP PEIPLHYQRM
     AVGGSGPGEK KKPEPCVPEF MKSDKSPEYS MVPELAGAGI FGAENLPEYN MNQAKCLKDF
     EKLEKRRIKE ETARQRKLQE KEKEQEKKLK RKLKQNAKGL VESAEAQFGK LMITSEQGEI
     PIFLNKCVEF IEKEGLDSEG IYRVPGSRAH VDMLFQRFEE DTNTEIDALD IPVNAVATAL
     KDFFSKRLPP LFSKDIIKEL EEIAGSRGVG NSKLNVEVKT DRSCRLIALK SLLQKLPPIN
     FAILKYIFQH FVHVSDNSKL NSMDSKNLAI CWWPTLIPID FTDMGHFEQL RPYLEDIVQT
     MIDQFPYLFC GKDAFVMV
//