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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_MOUSE             Reviewed;         869 AA.
A2AB59; Q3V366; Q4V9V5;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 1.
25-OCT-2017, entry version 94.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 749-869.
STRAIN=Czech II; TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
TISSUE SPECIFICITY.
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-28 (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-350; SER-459;
SER-462; THR-464; SER-469; SER-632 AND SER-636, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT TYR-28 (ISOFORM 2), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with SH3KBP1/CIN85. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=A2AB59-1; Sequence=Displayed;
Name=2;
IsoId=A2AB59-2; Sequence=VSP_031057;
Note=No experimental confirmation available. Contains a
phosphotyrosine at position 28. {ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:21183079};
-!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney,
lung, small intestine and thymus. {ECO:0000269|PubMed:15147912}.
-!- SEQUENCE CAUTION:
Sequence=AAH96671.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK046763; BAE20660.1; -; mRNA.
EMBL; AL772325; CAM16599.1; -; Genomic_DNA.
EMBL; AL662804; CAM16599.1; JOINED; Genomic_DNA.
EMBL; AL662804; CAM21566.1; -; Genomic_DNA.
EMBL; AL772325; CAM21566.1; JOINED; Genomic_DNA.
EMBL; BC096671; AAH96671.1; ALT_INIT; mRNA.
CCDS; CCDS25517.1; -. [A2AB59-2]
CCDS; CCDS56815.1; -. [A2AB59-1]
RefSeq; NP_001192165.1; NM_001205236.1. [A2AB59-1]
RefSeq; NP_598476.2; NM_133715.5. [A2AB59-2]
UniGene; Mm.259113; -.
UniGene; Mm.397197; -.
ProteinModelPortal; A2AB59; -.
SMR; A2AB59; -.
STRING; 10090.ENSMUSP00000102639; -.
iPTMnet; A2AB59; -.
PhosphoSitePlus; A2AB59; -.
EPD; A2AB59; -.
MaxQB; A2AB59; -.
PaxDb; A2AB59; -.
PeptideAtlas; A2AB59; -.
PRIDE; A2AB59; -.
Ensembl; ENSMUST00000041385; ENSMUSP00000039427; ENSMUSG00000034255. [A2AB59-2]
Ensembl; ENSMUST00000107024; ENSMUSP00000102639; ENSMUSG00000034255. [A2AB59-1]
GeneID; 544817; -.
KEGG; mmu:544817; -.
UCSC; uc007luc.2; mouse. [A2AB59-1]
UCSC; uc007lud.2; mouse. [A2AB59-2]
CTD; 201176; -.
MGI; MGI:1916903; Arhgap27.
eggNOG; KOG1450; Eukaryota.
eggNOG; KOG4269; Eukaryota.
eggNOG; ENOG410ZP6T; LUCA.
GeneTree; ENSGT00890000139322; -.
HOGENOM; HOG000294167; -.
HOVERGEN; HBG005328; -.
InParanoid; A2AB59; -.
KO; K20636; -.
OMA; ETVWEDE; -.
OrthoDB; EOG091G164H; -.
PhylomeDB; A2AB59; -.
TreeFam; TF329345; -.
ChiTaRS; Arhgap27; mouse.
PRO; PR:A2AB59; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000034255; -.
CleanEx; MM_ARHGAP27; -.
ExpressionAtlas; A2AB59; baseline and differential.
Genevisible; A2AB59; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0005622; C:intracellular; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
CDD; cd00201; WW; 2.
Gene3D; 1.10.555.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
InterPro; IPR036028; SH3-like_dom.
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; SSF50998; SSF50998; 2.
SUPFAM; SSF51045; SSF51045; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50238; RHOGAP; 1.
PROSITE; PS50002; SH3; 1.
PROSITE; PS50020; WW_DOMAIN_2; 3.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Endocytosis;
GTPase activation; Membrane; Phosphoprotein; Reference proteome;
Repeat; SH3 domain.
CHAIN 1 869 Rho GTPase-activating protein 27.
/FTId=PRO_0000317579.
DOMAIN 8 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:0000250|UniProtKB:Q6TLK4}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000250|UniProtKB:Q6ZUM4}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 459 459 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 462 462 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 464 464 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 632 632 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 636 636 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 217 MAADVEGDVYVLVEHPFEYTGKDGRRIAIQPNERYRLLRRS
TEHWWHVRREPGGRPFYLPAQYVRELPALGDPAPAPQPSVP
QQRPAVPEPLAYDYRFVSTPVGADGSSAEPRGRASSLCGPA
RQRTGGQRNSLAPGGPACLYVRPAAPVRPAQSLDDLARGGT
APPAGLLGSAGHFKASSVAGSWVCPRPLAPSDSENVYEAIP
DLRCPPRAESPK -> MVDMISKLVRRQSRALRA (in
isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_031057.
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


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