RHG27_MOUSE
ID RHG27_MOUSE Reviewed; 869 AA.
AC A2AB59; Q3V366; Q4V9V5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Rho GTPase-activating protein 27;
DE AltName: Full=CIN85-associated multi-domain-containing Rho GTPase-activating protein 1;
DE AltName: Full=Rho-type GTPase-activating protein 27;
GN Name=Arhgap27; Synonyms=Camgap1;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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] OF 749-869.
RC STRAIN=Czech II; TISSUE=Lung;
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 TISSUE SPECIFICITY.
RX PubMed=15147912; DOI=10.1016/j.febslet.2004.03.101;
RA Sakakibara T., Nemoto Y., Nukiwa T., Takeshima H.;
RT "Identification and characterization of a novel Rho GTPase activating
RT protein implicated in receptor-mediated endocytosis.";
RL FEBS Lett. 566:294-300(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-28 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-350; SER-459;
RP SER-462; THR-464; SER-469; SER-632 AND SER-636, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT TYR-28 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
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: Rho GTPase-activating protein which may be involved in
CC clathrin-mediated endocytosis. GTPase activators for the Rho-type
CC GTPases act by converting them to an inactive GDP-bound state. Has
CC activity toward CDC42 and RAC1 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SH3KBP1/CIN85. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2AB59-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AB59-2; Sequence=VSP_031057;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney, lung,
CC small intestine and thymus. {ECO:0000269|PubMed:15147912}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH96671.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK046763; BAE20660.1; -; mRNA.
DR EMBL; AL662804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL772325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096671; AAH96671.1; ALT_INIT; mRNA.
DR CCDS; CCDS25517.1; -. [A2AB59-2]
DR CCDS; CCDS56815.1; -. [A2AB59-1]
DR RefSeq; NP_001192165.1; NM_001205236.1. [A2AB59-1]
DR RefSeq; NP_598476.2; NM_133715.5. [A2AB59-2]
DR AlphaFoldDB; A2AB59; -.
DR SMR; A2AB59; -.
DR STRING; 10090.ENSMUSP00000039427; -.
DR iPTMnet; A2AB59; -.
DR PhosphoSitePlus; A2AB59; -.
DR EPD; A2AB59; -.
DR jPOST; A2AB59; -.
DR MaxQB; A2AB59; -.
DR PaxDb; A2AB59; -.
DR PeptideAtlas; A2AB59; -.
DR PRIDE; A2AB59; -.
DR ProteomicsDB; 254965; -. [A2AB59-1]
DR ProteomicsDB; 254966; -. [A2AB59-2]
DR Antibodypedia; 49843; 144 antibodies from 23 providers.
DR Ensembl; ENSMUST00000041385; ENSMUSP00000039427; ENSMUSG00000034255. [A2AB59-2]
DR Ensembl; ENSMUST00000107024; ENSMUSP00000102639; ENSMUSG00000034255. [A2AB59-1]
DR GeneID; 544817; -.
DR KEGG; mmu:544817; -.
DR UCSC; uc007luc.2; mouse. [A2AB59-1]
DR UCSC; uc007lud.2; mouse. [A2AB59-2]
DR CTD; 201176; -.
DR MGI; MGI:1916903; Arhgap27.
DR VEuPathDB; HostDB:ENSMUSG00000034255; -.
DR eggNOG; KOG1450; Eukaryota.
DR eggNOG; KOG4269; Eukaryota.
DR GeneTree; ENSGT00950000182860; -.
DR HOGENOM; CLU_015883_6_1_1; -.
DR InParanoid; A2AB59; -.
DR OMA; WSCHVGP; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; A2AB59; -.
DR TreeFam; TF329345; -.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 544817; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Arhgap27; mouse.
DR PRO; PR:A2AB59; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; A2AB59; protein.
DR Bgee; ENSMUSG00000034255; Expressed in granulocyte and 183 other tissues.
DR ExpressionAtlas; A2AB59; baseline and differential.
DR Genevisible; A2AB59; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00201; WW; 2.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR015767; ARHGAP27.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR23176:SF104; PTHR23176:SF104; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00456; WW; 3.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endocytosis; GTPase activation; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..869
FT /note="Rho GTPase-activating protein 27"
FT /id="PRO_0000317579"
FT DOMAIN 6..69
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 246..280
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 299..333
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 414..447
FT /note="WW 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 477..593
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 677..866
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 104..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6TLK4"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZUM4"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 464
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..217
FT /note="MAADVEGDVYVLVEHPFEYTGKDGRRIAIQPNERYRLLRRSTEHWWHVRREP
FT GGRPFYLPAQYVRELPALGDPAPAPQPSVPQQRPAVPEPLAYDYRFVSTPVGADGSSAE
FT PRGRASSLCGPARQRTGGQRNSLAPGGPACLYVRPAAPVRPAQSLDDLARGGTAPPAGL
FT LGSAGHFKASSVAGSWVCPRPLAPSDSENVYEAIPDLRCPPRAESPK -> MVDMISKL
FT VRRQSRALRA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031057"
FT MOD_RES A2AB59-2:28
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 869 AA; 97049 MW; F53EDBAFE1B2A6E7 CRC64;
MAADVEGDVY VLVEHPFEYT GKDGRRIAIQ PNERYRLLRR STEHWWHVRR EPGGRPFYLP
AQYVRELPAL GDPAPAPQPS VPQQRPAVPE PLAYDYRFVS TPVGADGSSA EPRGRASSLC
GPARQRTGGQ RNSLAPGGPA CLYVRPAAPV RPAQSLDDLA RGGTAPPAGL LGSAGHFKAS
SVAGSWVCPR PLAPSDSENV YEAIPDLRCP PRAESPKQVD DPPEPVYANV ERQPRATSPR
SAAAPPRLSP VWETHTDTGT GRPYYYNPDT GVTTWESPFE TPEGTTSPAT SRASVGSGES
LETEWGQYWD EESRRVFFYN PLTGETAWED ETEELEEDHQ EQLEMQPSLS PRSPGQQRPP
TPETDYPELL ASYPEEDYSP VGSFSDPGPA SPLVAPPGWS CQITPDKQML YTNQFTQEQW
VRLEDQHGKP YFYNPEDSSV QWELPQVPIP APRSVRKSSQ DSDTPAQASP PEEKIKTLDK
AGVLHRTKTV DKGKRLRKKH WSTSWTVLEG GVLTFFKDSK TSAAGGLRQP SKLSTPEYTV
ELKGASLSWA PKDKSSKKNV LELRSRDGSE YLIQHDSEAI ISTWHKAIAE GISELSADLL
QGEEGEPSSA DFGSSERLGS WREEDVRQNA ASPSLSPGGL ESDLSRVRHK LRKFLQRRPT
LQSLRDKGYI KDQVFGCALA QLCERERSPV PRFVQQCIRT VEARGLDIDG LYRISGNLAT
IQKLRYKVDH DERLDLDDGR WEDVHVITGA LKLFFRELPE PLFPFSHFHQ FIAAIKLQDP
AQRSRCVRDL VRTLPAPNQD TLRLLIQHLC RVIEHGEQNR MTVQNVAIVF GPTLLRPEME
EASMPMTMVF QNQVVELILH QCADIFPPH
