RHG27_RAT
ID RHG27_RAT Reviewed; 869 AA.
AC Q6TLK4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 110.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH SH3KBP1.
RC STRAIN=Sprague-Dawley;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-632, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. {ECO:0000269|PubMed:15147912}.
CC -!- SUBUNIT: Interacts with SH3KBP1/CIN85. {ECO:0000269|PubMed:15147912}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15147912}. Membrane
CC {ECO:0000269|PubMed:15147912}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15147912}.
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DR EMBL; AY394725; AAQ94494.1; -; mRNA.
DR RefSeq; NP_942054.1; NM_198759.1.
DR AlphaFoldDB; Q6TLK4; -.
DR SMR; Q6TLK4; -.
DR STRING; 10116.ENSRNOP00000034607; -.
DR iPTMnet; Q6TLK4; -.
DR PhosphoSitePlus; Q6TLK4; -.
DR PaxDb; Q6TLK4; -.
DR PRIDE; Q6TLK4; -.
DR GeneID; 303583; -.
DR KEGG; rno:303583; -.
DR CTD; 201176; -.
DR RGD; 735202; Arhgap27.
DR eggNOG; KOG1450; Eukaryota.
DR eggNOG; KOG4269; Eukaryota.
DR InParanoid; Q6TLK4; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; Q6TLK4; -.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR PRO; PR:Q6TLK4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IDA:HGNC-UCL.
DR GO; GO:0017124; F:SH3 domain binding; IDA:HGNC-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:HGNC-UCL.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:MGI.
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; 3.
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; 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; SSF51045; SSF51045; 3.
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 Cytoplasm; Endocytosis; GTPase activation; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..869
FT /note="Rho GTPase-activating protein 27"
FT /id="PRO_0000317580"
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..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..299
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:0007744|PubMed:22673903"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AB59"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZUM4"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AB59"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AB59"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AB59"
FT MOD_RES 464
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A2AB59"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZUM4"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 869 AA; 97180 MW; 59E7855A46B2ADE3 CRC64;
MAADVEGDVY VLVEHPFEYT GKDGRLIAIQ PNERCRLLRR STEHWWHVRR EPGGRPFYLP
AQYVRELPAL GDPVPAPQPS VLQQRPTVPE PLAYDYRFVS TPVGADGSSA EPRGRASSLC
GPARQRTSGQ RNSLAPGGPA CLYLRPAAPV RPAQSLDDLA RGGTAPPAGL LGSAGHFKAS
SVAGSWVCPR PLARSDSENV YEAIPDLRCP PRAKSPKQVD EPPEPVYANV ERQPQVTSPR
SAAAPPRLSP VWETHTDAGT GRPYYYNPDT GVTTWESPFE APEGATSPTT SRASVGSGES
LETEWGQYWD EESGRVFFYN PLTGETVWED ETEELEDDPE EQLEMQPSLS PRSPGQQRPP
TPETDYPELL TSYPEEDYSP VGSFSDLGPT SPLVAPPGWS CQITPEKQML YTNQFTQEQW
VRLEDQEGKP YFYNPEDSSV QWELPQVPVP APRSGRKSSQ DSDTPAQASP PEEKIKTLDK
AGVLHRTKTV DKGKRLRKKH WNASWTVLEG GVLTFFKDSK TSAASGLRQP SKLSTPEYTV
ELRGASLSWA PKDKSSKKNV LELRSRDGSE YLIQHDSEAI ISTWHKAIAE GIEELSADLP
QREEGEPSSA DFGSSERLGS WKEEDVRPNA ASPSLNPGSQ ESDLSRVRHK LRKFLQRRPT
LQSLREKGYI KDQVFGCALA QLCERERSPV PRFVQQCIRT VEARGLDIDG LYRISGNLAT
IQKLRYKVDH DERLDLDDGR WEDVHVITGA LKLFFRELPE PLFPFSHFHQ FIAAIKLQDP
AQRSRCVRDL VRTLPAPNHD TLRLLIQHLC RVIEHGEQNR MSVQNVAIVF GPTLLRPEME
EASMPMTMVF QNQVVELILH QCADIFPPH
