RHG05_MOUSE
ID RHG05_MOUSE Reviewed; 1501 AA.
AC P97393; E9Q0L8;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Rho GTPase-activating protein 5;
DE AltName: Full=Rho-type GTPase-activating protein 5;
DE AltName: Full=p190-B;
GN Name=Arhgap5; Synonyms=Rhogap5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ; TISSUE=Kidney;
RX PubMed=9838117; DOI=10.1016/s0167-4781(98)00207-3;
RA Burbelo P.D., Finegold A.A., Kozak C.A., Yamada Y., Takami H.;
RT "Cloning, genomic organization and chromosomal assignment of the mouse
RT p190-B gene.";
RL Biochim. Biophys. Acta 1443:203-210(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1149.
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1194; SER-1201 AND SER-1217,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: GTPase-activating protein for Rho family members.
CC {ECO:0000250|UniProtKB:Q13017}.
CC -!- SUBUNIT: May interact with RASA1/p120GAP.
CC {ECO:0000250|UniProtKB:Q13017}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13017}. Cell
CC membrane {ECO:0000250|UniProtKB:Q13017}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q13017}. Note=Also membrane-associated in a
CC fibrillar pattern that colocalizes with the alpha5-beta1 integrin
CC receptor (ITGA5/ITGB1) for fibronectin. {ECO:0000250|UniProtKB:Q13017}.
CC -!- TISSUE SPECIFICITY: Expressed in spinal cord, cerebellum, kidney,
CC testis and lung. {ECO:0000269|PubMed:9838117}.
CC -!- DOMAIN: The pG1 pseudoGTPase domain does not bind GTP.
CC {ECO:0000250|UniProtKB:Q13017}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK041016; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U67160; AAD12768.1; -; Genomic_DNA.
DR EMBL; AC114002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC155819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK041016; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T42724; T42724.
DR AlphaFoldDB; P97393; -.
DR BMRB; P97393; -.
DR SMR; P97393; -.
DR IntAct; P97393; 3.
DR MINT; P97393; -.
DR STRING; 10090.ENSMUSP00000106353; -.
DR iPTMnet; P97393; -.
DR PhosphoSitePlus; P97393; -.
DR EPD; P97393; -.
DR jPOST; P97393; -.
DR MaxQB; P97393; -.
DR PaxDb; P97393; -.
DR PeptideAtlas; P97393; -.
DR PRIDE; P97393; -.
DR ProteomicsDB; 253274; -.
DR MGI; MGI:1332637; Arhgap5.
DR eggNOG; KOG4271; Eukaryota.
DR InParanoid; P97393; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR ChiTaRS; Arhgap5; mouse.
DR PRO; PR:P97393; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P97393; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
DR GO; GO:0016477; P:cell migration; IMP:MGI.
DR GO; GO:0010631; P:epithelial cell migration; IMP:MGI.
DR GO; GO:0030879; P:mammary gland development; IMP:MGI.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:MGI.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:MGI.
DR GO; GO:0008361; P:regulation of cell size; IMP:MGI.
DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
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; PF01846; FF; 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; SM00441; FF; 4.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81698; SSF81698; 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 Cell membrane; Cytoplasm; GTPase activation; Membrane; Nitration;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1501
FT /note="Rho GTPase-activating protein 5"
FT /id="PRO_0000056703"
FT DOMAIN 267..325
FT /note="FF 1"
FT DOMAIN 366..420
FT /note="FF 2"
FT DOMAIN 427..481
FT /note="FF 3"
FT DOMAIN 482..548
FT /note="FF 4"
FT DOMAIN 590..763
FT /note="pG1 pseudoGTPase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01199"
FT DOMAIN 779..944
FT /note="pG2 pseudoGTPase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01200"
FT DOMAIN 1261..1448
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 975..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1247
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 550
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13017"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13017"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13017"
FT MOD_RES 951
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13017"
FT MOD_RES 968
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13017"
FT MOD_RES 1115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13017"
FT MOD_RES 1194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 71..72
FT /note="HF -> SL (in Ref. 1; AAD12768)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="I -> N (in Ref. 1; AAD12768)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="R -> H (in Ref. 1; AAD12768)"
FT /evidence="ECO:0000305"
FT CONFLICT 348..349
FT /note="TL -> SV (in Ref. 1; AAD12768)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="N -> K (in Ref. 1; AAD12768)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="I -> F (in Ref. 1; AAD12768)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="Missing (in Ref. 1; AAD12768)"
FT /evidence="ECO:0000305"
FT CONFLICT 787
FT /note="G -> A (in Ref. 1; AAD12768)"
FT /evidence="ECO:0000305"
FT CONFLICT 793
FT /note="D -> H (in Ref. 1; AAD12768)"
FT /evidence="ECO:0000305"
FT CONFLICT 849
FT /note="H -> T (in Ref. 1; AAD12768)"
FT /evidence="ECO:0000305"
FT CONFLICT 1079..1081
FT /note="LAH -> FG (in Ref. 1; AAD12768)"
FT /evidence="ECO:0000305"
FT CONFLICT 1092
FT /note="V -> A (in Ref. 1; AAD12768)"
FT /evidence="ECO:0000305"
FT CONFLICT 1140
FT /note="D -> DR (in Ref. 1; AAD12768)"
FT /evidence="ECO:0000305"
FT CONFLICT 1153
FT /note="I -> T (in Ref. 1; AAD12768)"
FT /evidence="ECO:0000305"
FT CONFLICT 1185
FT /note="K -> KP (in Ref. 1; AAD12768)"
FT /evidence="ECO:0000305"
FT CONFLICT 1413..1415
FT /note="WPT -> GQP (in Ref. 1; AAD12768)"
FT /evidence="ECO:0000305"
FT CONFLICT 1463
FT /note="P -> Q (in Ref. 1; AAD12768)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1501 AA; 172113 MW; C2E14661E838548D CRC64;
MMAKNKEPRP PSYTVSVVGL SGTEKDKGNC GVGKSCLCNR FVRSKADEYY PEHTSVLSTI
DFGGRVVNND HFLYWGDITQ NGEDGVECKI HVIEQTEFID DQTFLPHRST NLQPYIKRAA
ASKLQSAEKL MYICTDQLGL EQDFEQKQMP EGKLNVDGFL LCIDVSQGCN RKFDDQLKFV
NNLFVQLSKS KKPVIIAATK CDECVDHYLR EVQAFASNKK NLLVVETSAR FNVNIETCFT
ALVQMLDKTR GKPKIIPYLD AYKTQRQLVV TATDKFEKLV QTVRDYHATW KTVSNKLKNH
PDYEEYINLE GTRKARNTFS KHIEQLKQEH IRKRREEYIS TLPRAFNTLL PDLEEIEHLN
WLEALKLMEK RADFQLCFVV LEKTPWDETD HIDKINDRRI PFDLLSTLEA EKVYQNHVQH
LISEKRRIEM KEKFKKTLEK IQFISPGQPW EEVMCFVMED EAFKYITEAD SKEVYGRHQR
EIVEKAKEEF QEMLFEHSEL FYDLDLNATP SSDKMSEIHT VLSEEPRYKA LQKLAPDRES
LLLKHIGFVY HPTKETCLSG QYCTDIKVEN LLATSLLEMD HNRVRLYHDS TNIDKVNLFI
LGKDGLAQEL ANEIRTQSTD DEYALDGKIY ELDLRPVDAK SPYILSQLWT AAFKPHGCFC
VFNSIESLSF IGEFIGKIRT EASQIRKDKY MTNLPFTLIL ANQRDSISKN LPILRHQGQQ
LANKLQCPFV DVPTGTYPRK FNESQIKQAL RGVLESVKHN LDVVSPVPIN KDVSEADLRI
VMCAMCGDPF SVDLILSPFL DSHSCSAAQA GQNNSLMLDK IIGEKRRRIQ ITILSYHSSI
GVRKDELVHG YILVYSAKRK ASMGMLRAFL SEVQDTIPVQ LVAVTDSQAD FFENEAIKEL
MTEGEHIATE ITAKFTALYS LSQYHRQTEV FTLFFSDVLE KKNMIENSYL SDNTRESTHQ
SEDVFLPSPR DCFPYNNYPD SDDDTEAPPP YSPIGDDVQL LPTPSDRSRY RLDLEGNEYP
VHSTPNCHDH ERNHKVPPPI KPKPVVPKTN VKKLDPNLLK TIEAGIGKNP RKQTSRVPLA
HPEDMDSSDN YVEPLDTIFK QKGYSDEIYV VPDDSQNRII KIRNSFVNNT QGDEENGFSD
PQKVMESVGL QNININLKLC LVKPSHTTEE HTQMQAMMRL SLLPKKRKGR HRGSEEDPLL
SPVETWKGGI DNPAITSDQE VDDKKIKKKT HKVKEDKKQK KKTKTFNPPT RRNWESNYFG
MPLQDLVTAE KPIPLFVEKC VEFIEDTGLC TEGLYRVSGN KTDQDNIQKQ FDQDHNINLA
SMEVTVNAVA GALKAFFADL PDPLIPYSLH PELLEAAKIP DKTERFHALK EIVKKFHPVN
YDVFRYVITH LNRVSQQNKI NLMTADNLSI CFWPTLMRPD FENREFLSTT KIHQSVVETF
IQQCQFFFYN GEIVETANTV APPPTSNPGQ LVESMVPLQL PPPLQPQLIQ PQLQTDPLGI
I
