ID RHG27_HUMAN Reviewed; 889 AA.
AC Q6ZUM4; A4FU35; A8K3N5; C9JTF3; Q494U0; Q6NWZ8; Q8WY58;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 3.
DT 01-MAY-2013, entry version 90.
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;
DE AltName: Full=SH3 domain-containing protein 20;
GN Name=ARHGAP27; Synonyms=CAMGAP1, SH3D20; ORFNames=PP905;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo, and Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 270-889 (ISOFORMS 1 AND 3), AND VARIANT
RP GLN-889.
RC TISSUE=Pancreas;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=15492870;
RA Katoh Y., Katoh M.;
RT "Identification and characterization of ARHGAP27 gene in silico.";
RL Int. J. Mol. Med. 14:943-947(2004).
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).
CC -!- SUBUNIT: Interacts with SH3KBP1/CIN85 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC Peripheral membrane protein (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6ZUM4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZUM4-2; Sequence=VSP_031053;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q6ZUM4-3; Sequence=VSP_031056;
CC Note=No experimental confirmation available;
CC Name=4; Synonyms=SH3D20;
CC IsoId=Q6ZUM4-4; Sequence=VSP_031054, VSP_031055;
CC -!- TISSUE SPECIFICITY: Expressed in germinal center B-cell, spleen,
CC chronic lymphocytic leukemia, pancreatic cancer and lung cancer.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- SIMILARITY: Contains 3 WW domains.
CC -!- CAUTION: According to HGNC, ARHGAP27 and SH3D20 are 2 separate
CC genes, corresponding to isoform 2 and isoform 4, respectively.
CC However, a rat transcript and paralog proteins with a similar
CC domain structure suggest the existence of a single gene encoding
CC for a protein of 889 residues as displayed here.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI01389.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAI01390.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAI01391.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF258593; AAG23796.1; -; mRNA.
DR EMBL; AK125535; BAC86196.1; -; mRNA.
DR EMBL; AK290650; BAF83339.1; -; mRNA.
DR EMBL; AC003070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067345; AAH67345.1; -; mRNA.
DR EMBL; BC101388; AAI01389.1; ALT_INIT; mRNA.
DR EMBL; BC101389; AAI01390.1; ALT_INIT; mRNA.
DR EMBL; BC101390; AAI01391.1; ALT_INIT; mRNA.
DR EMBL; BC101391; AAI01392.3; -; mRNA.
DR IPI; IPI00398170; -.
DR IPI; IPI00884998; -.
DR IPI; IPI00885078; -.
DR IPI; IPI00885118; -.
DR RefSeq; NP_777579.2; NM_174919.3.
DR RefSeq; NP_954976.1; NM_199282.2.
DR UniGene; Hs.205326; -.
DR PDB; 3PP2; X-ray; 1.42 A; A/B=491-613.
DR PDBsum; 3PP2; -.
DR ProteinModelPortal; Q6ZUM4; -.
DR SMR; Q6ZUM4; 10-67, 498-612, 678-886.
DR IntAct; Q6ZUM4; 1.
DR STRING; 9606.ENSP00000366121; -.
DR PhosphoSite; Q6ZUM4; -.
DR DMDM; 300669680; -.
DR PaxDb; Q6ZUM4; -.
DR PRIDE; Q6ZUM4; -.
DR Ensembl; ENST00000290470; ENSP00000290470; ENSG00000159314.
DR Ensembl; ENST00000376922; ENSP00000366121; ENSG00000159314.
DR Ensembl; ENST00000428638; ENSP00000403323; ENSG00000159314.
DR Ensembl; ENST00000442348; ENSP00000409330; ENSG00000159314.
DR Ensembl; ENST00000455881; ENSP00000408235; ENSG00000159314.
DR Ensembl; ENST00000528273; ENSP00000436137; ENSG00000159314.
DR Ensembl; ENST00000528384; ENSP00000431591; ENSG00000159314.
DR GeneID; 201176; -.
DR KEGG; hsa:201176; -.
DR UCSC; uc002iix.3; human.
DR UCSC; uc010dal.3; human.
DR CTD; 201176; -.
DR GeneCards; GC17M043476; -.
DR HGNC; HGNC:31813; ARHGAP27.
DR HPA; HPA023919; -.
DR MIM; 610591; gene.
DR neXtProt; NX_Q6ZUM4; -.
DR PharmGKB; PA134873327; -.
DR eggNOG; NOG279563; -.
DR HOVERGEN; HBG005328; -.
DR OMA; KGYIRDQ; -.
DR OrthoDB; EOG4X3H0P; -.
DR GenomeRNAi; 201176; -.
DR NextBio; 90073; -.
DR ArrayExpress; Q6ZUM4; -.
DR Bgee; Q6ZUM4; -.
DR CleanEx; HS_ARHGAP27; -.
DR Genevestigator; Q6ZUM4; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005622; C:intracellular; ISS:HGNC.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0030675; F:Rac GTPase activator activity; ISS:HGNC.
DR GO; GO:0017124; F:SH3 domain binding; ISS:HGNC.
DR GO; GO:0043089; P:positive regulation of Cdc42 GTPase activity; ISS:HGNC.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:HGNC.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR InterPro; IPR015767; Rho_GTPase_activating.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR001202; WW_dom.
DR PANTHER; PTHR23181; PTHR23181; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00456; WW; 3.
DR SUPFAM; SSF48350; Rho_GAP; 1.
DR SUPFAM; SSF50044; SH3; 1.
DR SUPFAM; SSF51045; WW_Rsp5_WWP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; FALSE_NEG.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Endocytosis; GTPase activation; Membrane; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1 889 Rho GTPase-activating protein 27.
FT /FTId=PRO_0000317578.
FT DOMAIN 8 69 SH3.
FT DOMAIN 246 280 WW 1.
FT DOMAIN 299 333 WW 2.
FT DOMAIN 411 444 WW 3.
FT DOMAIN 496 612 PH.
FT DOMAIN 697 886 Rho-GAP.
FT MOD_RES 156 156 Phosphoserine (By similarity).
FT MOD_RES 216 216 Phosphoserine (By similarity).
FT MOD_RES 228 228 Phosphotyrosine (By similarity).
FT MOD_RES 638 638 Phosphoserine (By similarity).
FT VAR_SEQ 1 341 Missing (in isoform 2).
FT /FTId=VSP_031053.
FT VAR_SEQ 221 263 DDPPEPVYANIERQPRATSPGAAAAPLPSPVWETHTDAGTG
FT RP -> PPRALGRGGGWRARDRARTEPGRKETRSAQRRARR
FT PPLSEDFG (in isoform 4).
FT /FTId=VSP_031054.
FT VAR_SEQ 264 889 Missing (in isoform 4).
FT /FTId=VSP_031055.
FT VAR_SEQ 416 442 Missing (in isoform 3).
FT /FTId=VSP_031056.
FT VARIANT 889 889 H -> Q (in dbSNP:rs34793644).
FT /FTId=VAR_038551.
FT CONFLICT 41 41 S -> N (in Ref. 1; AAG23796).
FT CONFLICT 162 162 C -> R (in Ref. 2; BAF83339).
FT CONFLICT 213 213 P -> R (in Ref. 4; AAH67345).
FT STRAND 499 510
FT STRAND 521 528
FT STRAND 531 536
FT HELIX 549 552
FT STRAND 554 560
FT STRAND 565 568
FT HELIX 571 573
FT STRAND 575 583
FT STRAND 589 593
FT HELIX 597 611
SQ SEQUENCE 889 AA; 98396 MW; E341CCC4D012DA4C CRC64;
MAADVVGDVY VLVEHPFEYT GKDGRRVAIR PNERYRLLRR STEHWWHVRR EPGGRPFYLP
AQYVRELPAL GNPAAAAPPG PHPSPAAPEP LAYDYRFVSA AATAGPDGAP EESGGRASSL
CGPAQRGAAT QRSSLAPGLP ACLYLRPAAP VRPAQSLNDL ACAAVSPPAG LLGSSGSFKA
CSVAGSWVCP RPLARSDSEN VYEVIQDLHV PPPEESAEQV DDPPEPVYAN IERQPRATSP
GAAAAPLPSP VWETHTDAGT GRPYYYNPDT GVTTWESPFE AAEGAASPAT SPASVDSHVS
LETEWGQYWD EESRRVFFYN PLTGETAWED EAENEPEEEL EMQPGLSPGS PGDPRPPTPE
TDYPESLTSY PEEDYSPVGS FGEPGPTSPL TTPPGWSCHV SQDKQMLYTN HFTQEQWVRL
EDPHGKPYFY NPEDSSVRWE LPQVPVPAPR SIHKSSQDGD TPAQASPPEE KVPAELDEVG
SWEEVSPATA AVRTKTLDKA GVLHRTKTAD KGKRLRKKHW SASWTVLEGG VLTFFKDSKT
SAAGGLRQPS KFSTPEYTVE LRGATLSWAP KDKSSRKNVL ELRSRDGSEY LIQHDSEAII
STWHKAIAQG IQELSAELPP EESESSRVDF GSSERLGSWQ EKEEDARPNA AAPALGPVGL
ESDLSKVRHK LRKFLQRRPT LQSLREKGYI KDQVFGCALA ALCERERSRV PRFVQQCIRA
VEARGLDIDG LYRISGNLAT IQKLRYKVDH DERLDLDDGR WEDVHVITGA LKLFFRELPE
PLFPFSHFRQ FIAAIKLQDQ ARRSRCVRDL VRSLPAPNHD TLRMLFQHLC RVIEHGEQNR
MSVQSVAIVF GPTLLRPEVE ETSMPMTMVF QNQVVELILQ QCADIFPPH
//
