RHG01_MOUSE
ID RHG01_MOUSE Reviewed; 439 AA.
AC Q5FWK3; Q8C3X5; Q923D8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Rho GTPase-activating protein 1;
DE AltName: Full=Rho-type GTPase-activating protein 1;
GN Name=Arhgap1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 [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].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-65, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-50 AND SER-51, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 activator for the Rho, Rac and Cdc42 proteins,
CC converting them to the putatively inactive GDP-bound state. Cdc42 seems
CC to be the preferred substrate (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29,
CC VPS35 and SFN. Interacts with BNIPL (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR EMBL; AK084622; BAC39233.1; -; mRNA.
DR EMBL; AL691489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL714023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006592; AAH06592.1; -; mRNA.
DR EMBL; BC089306; AAH89306.1; -; mRNA.
DR CCDS; CCDS16437.1; -.
DR RefSeq; NP_001139374.1; NM_001145902.1.
DR RefSeq; NP_666236.3; NM_146124.4.
DR RefSeq; XP_006499307.1; XM_006499244.1.
DR RefSeq; XP_006499308.1; XM_006499245.3.
DR RefSeq; XP_006499309.1; XM_006499246.3.
DR RefSeq; XP_006499310.1; XM_006499247.2.
DR RefSeq; XP_006499311.1; XM_006499248.2.
DR RefSeq; XP_006499312.1; XM_006499249.2.
DR RefSeq; XP_006499313.1; XM_006499250.1.
DR RefSeq; XP_011237759.1; XM_011239457.1.
DR AlphaFoldDB; Q5FWK3; -.
DR SMR; Q5FWK3; -.
DR BioGRID; 230727; 47.
DR IntAct; Q5FWK3; 15.
DR STRING; 10090.ENSMUSP00000106963; -.
DR iPTMnet; Q5FWK3; -.
DR PhosphoSitePlus; Q5FWK3; -.
DR EPD; Q5FWK3; -.
DR jPOST; Q5FWK3; -.
DR MaxQB; Q5FWK3; -.
DR PaxDb; Q5FWK3; -.
DR PeptideAtlas; Q5FWK3; -.
DR PRIDE; Q5FWK3; -.
DR ProteomicsDB; 254864; -.
DR Antibodypedia; 1399; 245 antibodies from 30 providers.
DR DNASU; 228359; -.
DR Ensembl; ENSMUST00000090614; ENSMUSP00000088105; ENSMUSG00000027247.
DR Ensembl; ENSMUST00000111329; ENSMUSP00000106961; ENSMUSG00000027247.
DR Ensembl; ENSMUST00000111330; ENSMUSP00000106962; ENSMUSG00000027247.
DR GeneID; 228359; -.
DR KEGG; mmu:228359; -.
DR UCSC; uc008kwi.2; mouse.
DR CTD; 392; -.
DR MGI; MGI:2445003; Arhgap1.
DR VEuPathDB; HostDB:ENSMUSG00000027247; -.
DR eggNOG; KOG4406; Eukaryota.
DR GeneTree; ENSGT00940000160630; -.
DR HOGENOM; CLU_030214_1_0_1; -.
DR InParanoid; Q5FWK3; -.
DR OrthoDB; 1511935at2759; -.
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-9013404; RAC2 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-9696270; RND2 GTPase cycle.
DR BioGRID-ORCS; 228359; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Arhgap1; mouse.
DR PRO; PR:Q5FWK3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q5FWK3; protein.
DR Bgee; ENSMUSG00000027247; Expressed in yolk sac and 262 other tissues.
DR ExpressionAtlas; Q5FWK3; baseline and differential.
DR Genevisible; Q5FWK3; MM.
DR GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0097443; C:sorting endosome; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0016197; P:endosomal transport; ISO:MGI.
DR GO; GO:2001136; P:negative regulation of endocytic recycling; ISO:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:MGI.
DR GO; GO:0033572; P:transferrin transport; ISO:MGI.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; GTPase activation; Phosphoprotein;
KW Reference proteome; SH3-binding.
FT CHAIN 1..439
FT /note="Rho GTPase-activating protein 1"
FT /id="PRO_0000323607"
FT DOMAIN 63..218
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT DOMAIN 244..431
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 28..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 228..238
FT /note="SH3-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 30..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 282
FT /note="Involved in G-protein binding to GAPs"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q07960"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07960"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 65
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 80
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q07960"
FT CONFLICT 168
FT /note="K -> Q (in Ref. 1; BAC39233)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="D -> E (in Ref. 3; AAH06592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 50411 MW; D8FD1E14C6BE32D3 CRC64;
MDPLSELQDD LTLDDTSQAL NQLKLASIDE KNWPSDEMPD FPKSDDSKSS SPEPVTHLKW
DDPYYDIARH QIVEVAGDDK YGRKIIVFSA CRMPPSHQLD HSKLLGYLKH TLDQYVESDY
TLLYLHHGLT SDNKPSLSWL RDAYREFDRK YKKNIKALYI VHPTMFIKTL LILFKPLISF
KFGRKIFYVN YLSELSEHVK LEQLGIPRQV LKYDDFLKST QKSPATAPKP MPPRPPLPNQ
QFGVSLQHLQ EKSPGQDPIP IVLRETVAYL QAHALTTEGI FRRSANTQVV REVQQKYNMG
LPVDFDQYNE LHLPAVILKT FLRELPEPLL TFDLYPHVVG FLNIDESQRV EVTQQVLQTL
PEENYQVLHF LTAFLVQISA HCDQNKMTNT NLAVVFGPNL LWAKDAAITL KAINPINTFT
KFLLDHQGEL FPSTDAQGV
