RHOV_HUMAN
ID RHOV_HUMAN Reviewed; 236 AA.
AC Q96L33; Q2KHQ5; Q8TDW6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Rho-related GTP-binding protein RhoV;
DE AltName: Full=CDC42-like GTPase 2;
DE AltName: Full=GTP-binding protein-like 2;
DE AltName: Full=Rho GTPase-like protein ARHV;
DE AltName: Full=Wnt-1 responsive Cdc42 homolog 2;
DE Short=WRCH-2;
GN Name=RHOV {ECO:0000312|HGNC:HGNC:18313};
GN Synonyms=ARHV {ECO:0000312|EMBL:BAB86363.1},
GN WRCH2 {ECO:0000312|EMBL:BAB86363.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB86363.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11956592;
RA Katoh M.;
RT "Molecular cloning and characterization of WRCH2 on human chromosome
RT 15q15.";
RL Int. J. Oncol. 20:977-982(2002).
RN [2] {ECO:0000312|EMBL:AAL17966.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11839775; DOI=10.1242/jcs.115.2.239;
RA Wherlock M., Mellor H.;
RT "The Rho GTPase family: a Racs to Wrchs story.";
RL J. Cell Sci. 115:239-240(2002).
RN [3] {ECO:0000312|EMBL:EAW92459.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAI05021.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex {ECO:0000312|EMBL:AAI05021.1}, and
RC Cervix {ECO:0000312|EMBL:AAI12946.2};
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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 -!- INTERACTION:
CC Q96L33; O43639: NCK2; NbExp=4; IntAct=EBI-8538631, EBI-713635;
CC Q96L33; Q9NQU5: PAK6; NbExp=3; IntAct=EBI-8538631, EBI-1053685;
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 TNF activates
CC endosomal but not plasma membrane RHOV. {ECO:0000250|UniProtKB:Q9Z1Y0}.
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas, placenta, and fetal
CC brain. {ECO:0000269|PubMed:11956592}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000250|UniProtKB:Q9Z1Y0}.
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DR EMBL; AB079131; BAB86363.1; -; mRNA.
DR EMBL; AY059636; AAL17966.1; -; mRNA.
DR EMBL; CH471125; EAW92459.1; -; Genomic_DNA.
DR EMBL; BC105020; AAI05021.1; -; mRNA.
DR EMBL; BC105022; AAI05023.1; -; mRNA.
DR EMBL; BC112945; AAI12946.2; -; mRNA.
DR CCDS; CCDS10068.1; -.
DR RefSeq; NP_598378.3; NM_133639.3.
DR AlphaFoldDB; Q96L33; -.
DR SMR; Q96L33; -.
DR BioGRID; 128110; 242.
DR IntAct; Q96L33; 2.
DR MINT; Q96L33; -.
DR STRING; 9606.ENSP00000220507; -.
DR iPTMnet; Q96L33; -.
DR PhosphoSitePlus; Q96L33; -.
DR BioMuta; RHOV; -.
DR DMDM; 74724228; -.
DR EPD; Q96L33; -.
DR MassIVE; Q96L33; -.
DR MaxQB; Q96L33; -.
DR PaxDb; Q96L33; -.
DR PeptideAtlas; Q96L33; -.
DR PRIDE; Q96L33; -.
DR ProteomicsDB; 77144; -.
DR Antibodypedia; 23194; 20 antibodies from 10 providers.
DR DNASU; 171177; -.
DR Ensembl; ENST00000220507.5; ENSP00000220507.4; ENSG00000104140.7.
DR GeneID; 171177; -.
DR KEGG; hsa:171177; -.
DR MANE-Select; ENST00000220507.5; ENSP00000220507.4; NM_133639.4; NP_598378.3.
DR UCSC; uc001znd.3; human.
DR CTD; 171177; -.
DR DisGeNET; 171177; -.
DR GeneCards; RHOV; -.
DR HGNC; HGNC:18313; RHOV.
DR HPA; ENSG00000104140; Tissue enhanced (esophagus, skin, vagina).
DR neXtProt; NX_Q96L33; -.
DR OpenTargets; ENSG00000104140; -.
DR PharmGKB; PA38313; -.
DR VEuPathDB; HostDB:ENSG00000104140; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000157624; -.
DR HOGENOM; CLU_041217_21_7_1; -.
DR InParanoid; Q96L33; -.
DR OMA; TPELGIK; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q96L33; -.
DR TreeFam; TF321839; -.
DR PathwayCommons; Q96L33; -.
DR Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR SignaLink; Q96L33; -.
DR BioGRID-ORCS; 171177; 13 hits in 1077 CRISPR screens.
DR ChiTaRS; RHOV; human.
DR GenomeRNAi; 171177; -.
DR Pharos; Q96L33; Tbio.
DR PRO; PR:Q96L33; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q96L33; protein.
DR Bgee; ENSG00000104140; Expressed in lower esophagus mucosa and 150 other tissues.
DR ExpressionAtlas; Q96L33; baseline and differential.
DR Genevisible; Q96L33; HS.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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 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 1: Evidence at protein 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_0000326438"
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:0007744|PubMed:23186163"
FT LIPID 234
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q7L0Q8"
FT CONFLICT 177
FT /note="K -> R (in Ref. 1; BAB86363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 236 AA; 26217 MW; 334CEEF501107B91 CRC64;
MPPRELSEAE PPPLRAPTPP PRRRSAPPEL GIKCVLVGDG AVGKSSLIVS YTCNGYPARY
RPTALDTFSV QVLVDGAPVR IELWDTAGQE DFDRLRSLCY PDTDVFLACF SVVQPSSFQN
ITEKWLPEIR THNPQAPVLL VGTQADLRDD VNVLIQLDQG GREGPVPQPQ AQGLAEKIRA
CCYLECSALT QKNLKEVFDS AILSAIEHKA RLEKKLNAKG VRTLSRCRWK KFFCFV
