位置:首页 > 蛋白库 > RHOV_MOUSE
RHOV_MOUSE
ID   RHOV_MOUSE              Reviewed;         236 AA.
AC   Q8VDU1;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Rho-related GTP-binding protein RhoV;
GN   Name=Rhov {ECO:0000312|MGI:MGI:2444227};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1] {ECO:0000312|EMBL:BAC29732.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC29732.1};
RC   TISSUE=Skin {ECO:0000312|EMBL:BAC29732.1}, and
RC   Vagina {ECO:0000312|EMBL:BAC29571.1};
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0000312|EMBL:AAH21307.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3 {ECO:0000312|EMBL:AAH21307.1};
RC   TISSUE=Mammary gland {ECO:0000312|EMBL:AAH21307.1};
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Plays a role in the control of the actin cytoskeleton via
CC       activation of the JNK pathway. {ECO:0000250|UniProtKB:Q9Z1Y0}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q7L0Q8};
CC   -!- SUBUNIT: Interacts with PAK2. {ECO:0000250|UniProtKB:Q9Z1Y0}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Z1Y0};
CC       Lipid-anchor {ECO:0000250|UniProtKB:Q9Z1Y0}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q9Z1Y0}. Endosome membrane
CC       {ECO:0000250|UniProtKB:Q9Z1Y0}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q9Z1Y0}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q9Z1Y0}. Note=Treatment with TNFA activates
CC       endosomal but not plasma membrane RHOV. {ECO:0000250|UniProtKB:Q9Z1Y0}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       {ECO:0000250|UniProtKB:Q9Z1Y0}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK036775; BAC29571.1; -; mRNA.
DR   EMBL; AK037170; BAC29732.1; -; mRNA.
DR   EMBL; AL929318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC021307; AAH21307.1; -; mRNA.
DR   CCDS; CCDS16598.1; -.
DR   RefSeq; NP_663505.1; NM_145530.2.
DR   AlphaFoldDB; Q8VDU1; -.
DR   SMR; Q8VDU1; -.
DR   STRING; 10090.ENSMUSP00000041411; -.
DR   PhosphoSitePlus; Q8VDU1; -.
DR   PaxDb; Q8VDU1; -.
DR   PRIDE; Q8VDU1; -.
DR   Antibodypedia; 23194; 20 antibodies from 10 providers.
DR   DNASU; 228543; -.
DR   Ensembl; ENSMUST00000037360; ENSMUSP00000041411; ENSMUSG00000034226.
DR   GeneID; 228543; -.
DR   KEGG; mmu:228543; -.
DR   UCSC; uc008ltm.2; mouse.
DR   CTD; 171177; -.
DR   MGI; MGI:2444227; Rhov.
DR   VEuPathDB; HostDB:ENSMUSG00000034226; -.
DR   eggNOG; KOG0393; Eukaryota.
DR   GeneTree; ENSGT00940000157624; -.
DR   HOGENOM; CLU_041217_21_7_1; -.
DR   InParanoid; Q8VDU1; -.
DR   OMA; TPELGIK; -.
DR   OrthoDB; 1091615at2759; -.
DR   PhylomeDB; Q8VDU1; -.
DR   TreeFam; TF321839; -.
DR   Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR   BioGRID-ORCS; 228543; 1 hit in 74 CRISPR screens.
DR   PRO; PR:Q8VDU1; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8VDU1; protein.
DR   Bgee; ENSMUSG00000034226; Expressed in lip and 114 other tissues.
DR   Genevisible; Q8VDU1; MM.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0032488; P:Cdc42 protein signal transduction; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; ISO:MGI.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR003578; Small_GTPase_Rho.
DR   PANTHER; PTHR24072; PTHR24072; 1.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Endosome; GTP-binding; Lipoprotein; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Palmitate; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..236
FT                   /note="Rho-related GTP-binding protein RhoV"
FT                   /id="PRO_0000326439"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38..45
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1Y0"
FT   BINDING         85..89
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L0Q8"
FT   BINDING         143..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61586"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96L33"
FT   LIPID           234
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1Y0"
SQ   SEQUENCE   236 AA;  26148 MW;  36121B1A9CDA1627 CRC64;
     MPPRELSEAE PPPLPASTPP PRRRSAPPEL GIKCVLVGDG AVGKSSLIVS YTCNGYPARY
     RPTALDTFSV QVLVDGAPVR IELWDTAGQE DFDRLRSLCY PDTDVFLACF SVVQPSSFQN
     ITEKWLPEIR THNPQAPVLL VGTQADLRDD VNVLIQLDQG GREGPVPQPQ AQGLAEKIRA
     CCYLECSALT QKNLKEVFDS AILSAIEHKA RLEKKLNAKG VRTLSRCRWK KFFCFV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024