GenomeNet

Database: UniProt
Entry: Q6TUE6_RAT
LinkDB: Q6TUE6_RAT
Original site: Q6TUE6_RAT 
ID   Q6TUE6_RAT              Unreviewed;      1245 AA.
AC   Q6TUE6; E9PTJ5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   31-JUL-2019, entry version 120.
DE   SubName: Full=LRRGT00098 {ECO:0000313|EMBL:AAQ91054.1};
DE   SubName: Full=Rho GTPase-activating protein 5 {ECO:0000313|Ensembl:ENSRNOP00000047384};
GN   Name=Arhgap5 {ECO:0000313|Ensembl:ENSRNOP00000047384,
GN   ECO:0000313|RGD:1308507};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|EMBL:AAQ91054.1};
RN   [1] {ECO:0000313|EMBL:AAQ91054.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sprague-Dawley {ECO:0000313|EMBL:AAQ91054.1};
RA   Xu C.S., Chang C.F., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y.,
RA   Yang K.J., Zhao L.F., Ma H., Wang L., Wang S.F., Xing X.K., Shen G.M.,
RA   Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
RT   "Liver regeneration after PH.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000047384, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000047384,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000047384}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000047384};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [4] {ECO:0000213|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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DR   EMBL; AABR07064283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY387084; AAQ91054.1; -; mRNA.
DR   RefSeq; NP_001041334.1; NM_001047869.1.
DR   STRING; 10116.ENSRNOP00000047384; -.
DR   Ensembl; ENSRNOT00000041373; ENSRNOP00000047384; ENSRNOG00000004696.
DR   GeneID; 299012; -.
DR   KEGG; rno:299012; -.
DR   UCSC; RGD:1308507; rat.
DR   CTD; 394; -.
DR   RGD; 1308507; Arhgap5.
DR   eggNOG; KOG4271; Eukaryota.
DR   eggNOG; ENOG410XR4E; LUCA.
DR   GeneTree; ENSGT00940000154553; -.
DR   HOGENOM; HOG000001561; -.
DR   KO; K13709; -.
DR   OrthoDB; 110157at2759; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000004696; Expressed in 9 organ(s), highest expression level in brain.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0042169; F:SH2 domain binding; IBA:GO_Central.
DR   GO; GO:0030879; P:mammary gland development; IEP:RGD.
DR   Gene3D; 1.10.10.440; -; 3.
DR   InterPro; IPR002713; FF_domain.
DR   InterPro; IPR036517; FF_domain_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039007; pG1.
DR   InterPro; IPR032835; RhoGAP-FF1.
DR   InterPro; IPR039006; RhoGAP_pG2.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF01846; FF; 1.
DR   Pfam; PF00071; Ras; 1.
DR   Pfam; PF16512; RhoGAP-FF1; 1.
DR   SMART; SM00441; FF; 4.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF81698; SSF81698; 1.
DR   PROSITE; PS51676; FF; 4.
DR   PROSITE; PS51852; PG1; 1.
DR   PROSITE; PS51853; PG2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002494};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:Q6TUE6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT   DOMAIN      266    324       FF. {ECO:0000259|PROSITE:PS51676}.
FT   DOMAIN      365    419       FF. {ECO:0000259|PROSITE:PS51676}.
FT   DOMAIN      426    480       FF. {ECO:0000259|PROSITE:PS51676}.
FT   DOMAIN      481    547       FF. {ECO:0000259|PROSITE:PS51676}.
FT   DOMAIN      589    762       PG1 pseudoGTPase. {ECO:0000259|PROSITE:
FT                                PS51852}.
FT   DOMAIN      778    943       PG2 pseudoGTPase. {ECO:0000259|PROSITE:
FT                                PS51853}.
FT   REGION      974   1003       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1021   1049       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1068   1088       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1128   1156       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1168   1245       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED      308    328       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS   1023   1037       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS   1168   1199       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS   1218   1245       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   1245 AA;  142758 MW;  40728811B86B2E31 CRC64;
     MAKNKEPRPP SYTVSVVGLS GTEKDKGNCG VGKSCLCNRF VRSKADEYYP EHTSVLSTID
     FGGRVVNNDH FLYWGDITQN GEDGVECKIH VIEQTEFIDD QTFLPHRSTN LQPYIKRAAA
     SKLQSAEKLM YICTDQLGLE QDFEQKQMPE GKLNVDGFLL CIDVSQGCNR KFDDQLKFVN
     NLFVQLSKSK KPVIIAATKC DECVDHYLRE VQAFASNKKN LLVVETSARF NVNIETCFTA
     LVQMLDKTRG KPKIIPYLDA YKTQRQLVVT ATDKFEKLVQ TVRDYHATWK TVSNKLKNHP
     DYEEYINLEG TRKARNTFSK HIEQLKQEHI RKRREEYIST LPRAFNTLLP DLEEIEHLNW
     LEALKLMEKR ADFQLCFVVL EKTPWDETDH IDKINDRRIP FDLLSTLEAE KVYQNHVQHL
     ISEKRRIEMK EKFKKTLEKI QFISPGQPWE EVMCFVMEDE AFKYITEADS KEVYGRHQRE
     IVEKAKEEFQ EMLFEHSELF YDLDLNATPS SDKMSEIHTV LSEEPRYKAL QKLAPDRESL
     LLKHIGFVYH PTKETCLSGQ YCTDIKVENL LANSLLHSDH NRSRLYHDST NIDKVNLFIL
     GKDGLAQELA NEIRTQSTDD EYALDGKIYE LDLRPVDAKS PYILSQLWTA AFKPHGCFCV
     FNSIESLSFI GEFIGKIRTE ASQIRKDKYM ANLPFTLILA NQRDSISKNL PILRHQGQQL
     ANKLQCPFVD VPAGTYPRKF NESQIKQALR GVLESVKHNL DVVSPVPINK DVSEADLRIV
     MCAMCGDPFS VDIILSPFLD SHSCSAAQAG QNNSLMLDKI IGEKRRRIQI TILSYHSSIG
     VRKDELVHGY ILVYSAKRKA SMGMLRAFLS EVQDTIPVQL VAVTDSQADF FENEAIKELM
     TEGEHIATEI TAKFTALYSL SQYHRQTEVF TLFFSDVLEK KNMIENSYLS DNTRESTHQS
     EDVFLPSPRD CFPYNNYPDS DDDTEAPPPY SPIGDDVQLL PTPSDRSRYR LDLEGNEYPV
     HSTPNCHDHE RNHKVPPPIK PKPVVPKTNV KKLDPNLLKT IEAGIGKNPR KQTSRVPLAH
     PEDMDSSDNY AEPLDTIFKQ KGYPDEIYVV PDDSQNRIIK IRNSFVNNTQ GDEENGFSDR
     TSKGHGERRP SKYKYKSKTL FSKAKSYYRR THSDASDDEA FPTSKTKRKG RHRGSEEDPL
     LSPVETWKGG IDNPAITSDQ EVDDKKIKKK PHKVKEDKKG FVSKG
//
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