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Rho GTPase-activating protein 27 (CIN85-associated multi-domain-containing Rho GTPase-activating protein 1) (Rho-type GTPase-activating protein 27)

 RHG27_RAT               Reviewed;         869 AA.
Q6TLK4;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
22-NOV-2017, entry version 95.
RecName: Full=Rho GTPase-activating protein 27;
AltName: Full=CIN85-associated multi-domain-containing Rho GTPase-activating protein 1;
AltName: Full=Rho-type GTPase-activating protein 27;
Name=Arhgap27; Synonyms=Camgap1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
INTERACTION WITH SH3KBP1.
STRAIN=Sprague-Dawley;
PubMed=15147912; DOI=10.1016/j.febslet.2004.03.101;
Sakakibara T., Nemoto Y., Nukiwa T., Takeshima H.;
"Identification and characterization of a novel Rho GTPase activating
protein implicated in receptor-mediated endocytosis.";
FEBS Lett. 566:294-300(2004).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-632, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Rho GTPase-activating protein which may be involved in
clathrin-mediated endocytosis. GTPase activators for the Rho-type
GTPases act by converting them to an inactive GDP-bound state. Has
activity toward CDC42 and RAC1. {ECO:0000269|PubMed:15147912}.
-!- SUBUNIT: Interacts with SH3KBP1/CIN85.
{ECO:0000269|PubMed:15147912}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15147912}.
Membrane {ECO:0000269|PubMed:15147912}; Peripheral membrane
protein {ECO:0000269|PubMed:15147912}.
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EMBL; AY394725; AAQ94494.1; -; mRNA.
RefSeq; NP_942054.1; NM_198759.1.
UniGene; Rn.17895; -.
ProteinModelPortal; Q6TLK4; -.
SMR; Q6TLK4; -.
STRING; 10116.ENSRNOP00000034607; -.
iPTMnet; Q6TLK4; -.
PhosphoSitePlus; Q6TLK4; -.
PaxDb; Q6TLK4; -.
PRIDE; Q6TLK4; -.
GeneID; 303583; -.
KEGG; rno:303583; -.
CTD; 201176; -.
RGD; 735202; Arhgap27.
eggNOG; KOG1450; Eukaryota.
eggNOG; KOG4269; Eukaryota.
eggNOG; ENOG410ZP6T; LUCA.
HOGENOM; HOG000294167; -.
HOVERGEN; HBG005328; -.
InParanoid; Q6TLK4; -.
KO; K20636; -.
PhylomeDB; Q6TLK4; -.
PRO; PR:Q6TLK4; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005622; C:intracellular; IMP:HGNC.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005096; F:GTPase activator activity; IDA:HGNC.
GO; GO:0017124; F:SH3 domain binding; IDA:HGNC.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:HGNC.
GO; GO:0006898; P:receptor-mediated endocytosis; IMP:HGNC.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
CDD; cd00201; WW; 3.
Gene3D; 1.10.555.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR001202; WW_dom.
InterPro; IPR036020; WW_dom_sf.
Pfam; PF00169; PH; 1.
Pfam; PF00620; RhoGAP; 1.
Pfam; PF00397; WW; 2.
SMART; SM00233; PH; 1.
SMART; SM00324; RhoGAP; 1.
SMART; SM00456; WW; 3.
SUPFAM; SSF48350; SSF48350; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF51045; SSF51045; 3.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50238; RHOGAP; 1.
PROSITE; PS50002; SH3; 1.
PROSITE; PS50020; WW_DOMAIN_2; 3.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Endocytosis; GTPase activation;
Membrane; Phosphoprotein; Reference proteome; Repeat; SH3 domain.
CHAIN 1 869 Rho GTPase-activating protein 27.
/FTId=PRO_0000317580.
DOMAIN 6 69 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 246 280 WW 1. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 299 333 WW 2. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 414 447 WW 3. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 477 593 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 677 866 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
MOD_RES 155 155 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000250|UniProtKB:A2AB59}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000250|UniProtKB:Q6ZUM4}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000250|UniProtKB:A2AB59}.
MOD_RES 459 459 Phosphoserine.
{ECO:0000250|UniProtKB:A2AB59}.
MOD_RES 462 462 Phosphoserine.
{ECO:0000250|UniProtKB:A2AB59}.
MOD_RES 464 464 Phosphothreonine.
{ECO:0000250|UniProtKB:A2AB59}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000250|UniProtKB:Q6ZUM4}.
MOD_RES 632 632 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
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


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