RHOV_RAT
ID RHOV_RAT Reviewed; 236 AA.
AC Q9Z1Y0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Rho-related GTP-binding protein RhoV;
DE AltName: Full=Rho family GTPase Chp;
GN Name=Rhov {ECO:0000312|RGD:628824};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC69198.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, GTP-BINDING, TISSUE SPECIFICITY, AND
RP INTERACTION WITH PAK2.
RC TISSUE=Pituitary {ECO:0000312|EMBL:AAC69198.1};
RX PubMed=9778532; DOI=10.1016/s0960-9822(98)70468-3;
RA Aronheim A., Broder Y.C., Cohen A., Fritsch A., Belisle B., Abo A.;
RT "Chp, a homologue of the GTPase Cdc42Hs, activates the JNK pathway and is
RT implicated in reorganizing the actin cytoskeleton.";
RL Curr. Biol. 8:1125-1128(1998).
RN [2] {ECO:0000312|EMBL:AAH86990.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway {ECO:0000312|EMBL:AAH86990.1};
RC TISSUE=Testis {ECO:0000312|EMBL:AAH86990.1};
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).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-40; CYS-227 AND CYS-234, AND
RP PALMITOYLATION AT CYS-234.
RX PubMed=15664990; DOI=10.1074/jbc.m411300200;
RA Chenette E.J., Abo A., Der C.J.;
RT "Critical and distinct roles of amino- and carboxyl-terminal sequences in
RT regulation of the biological activity of the Chp atypical Rho GTPase.";
RL J. Biol. Chem. 280:13784-13792(2005).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-226; ARG-228; TRP-229; LYS-230
RP AND LYS-231.
RX PubMed=16641371; DOI=10.1091/mbc.e05-09-0896;
RA Chenette E.J., Mitin N.Y., Der C.J.;
RT "Multiple sequence elements facilitate Chp Rho GTPase subcellular location,
RT membrane association, and transforming activity.";
RL Mol. Biol. Cell 17:3108-3121(2006).
CC -!- FUNCTION: Plays a role in the control of the actin cytoskeleton via
CC activation of the JNK pathway. {ECO:0000269|PubMed:9778532}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q7L0Q8};
CC -!- SUBUNIT: Interacts with PAK2. {ECO:0000269|PubMed:9778532}.
CC -!- INTERACTION:
CC Q9Z1Y0; Q91XS8: Stk17b; NbExp=2; IntAct=EBI-77480, EBI-77460;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15664990,
CC ECO:0000269|PubMed:16641371}; Lipid-anchor
CC {ECO:0000269|PubMed:15664990, ECO:0000269|PubMed:16641371}; Cytoplasmic
CC side {ECO:0000269|PubMed:15664990, ECO:0000269|PubMed:16641371}.
CC Endosome membrane {ECO:0000269|PubMed:15664990,
CC ECO:0000269|PubMed:16641371}; Lipid-anchor
CC {ECO:0000269|PubMed:15664990, ECO:0000269|PubMed:16641371}; Cytoplasmic
CC side {ECO:0000269|PubMed:15664990, ECO:0000269|PubMed:16641371}.
CC Note=Treatment with TNF activates endosomal but not plasma membrane
CC RHOV. {ECO:0000269|PubMed:15664990, ECO:0000269|PubMed:16641371}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and testis and at lower
CC levels in spleen and lung. {ECO:0000269|PubMed:9778532}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000269|PubMed:9778532}.
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DR EMBL; AF097887; AAC69198.1; -; mRNA.
DR EMBL; BC086990; AAH86990.1; -; mRNA.
DR RefSeq; NP_612551.2; NM_138542.2.
DR AlphaFoldDB; Q9Z1Y0; -.
DR SMR; Q9Z1Y0; -.
DR IntAct; Q9Z1Y0; 2.
DR STRING; 10116.ENSRNOP00000018277; -.
DR PhosphoSitePlus; Q9Z1Y0; -.
DR SwissPalm; Q9Z1Y0; -.
DR PaxDb; Q9Z1Y0; -.
DR PRIDE; Q9Z1Y0; -.
DR GeneID; 171581; -.
DR KEGG; rno:171581; -.
DR UCSC; RGD:628824; rat.
DR CTD; 171177; -.
DR RGD; 628824; Rhov.
DR eggNOG; KOG0393; Eukaryota.
DR InParanoid; Q9Z1Y0; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q9Z1Y0; -.
DR TreeFam; TF321839; -.
DR Reactome; R-RNO-9013424; RHOV GTPase cycle.
DR PRO; PR:Q9Z1Y0; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q9Z1Y0; RN.
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; IDA:RGD.
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_0000326440"
FT REGION 1..28
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:0000269|PubMed:15664990"
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:0000269|PubMed:15664990"
FT MUTAGEN 40
FT /note="G->V: Constitutively GTP-bound and constitutively
FT active."
FT /evidence="ECO:0000269|PubMed:15664990"
FT MUTAGEN 56
FT /note="Y->L: Increase in GDP/GTP cycling."
FT /evidence="ECO:0000269|PubMed:15664990"
FT MUTAGEN 226..228
FT /note="RCR->QCQ: Loss of subcellular location to plasma
FT membrane, decreased association with endomembranes."
FT /evidence="ECO:0000269|PubMed:16641371"
FT MUTAGEN 226
FT /note="R->Q: Loss of subcellular location to plasma
FT membrane."
FT /evidence="ECO:0000269|PubMed:16641371"
FT MUTAGEN 227
FT /note="C->S: No effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:15664990"
FT MUTAGEN 228
FT /note="R->Q: Loss of subcellular location to plasma
FT membrane."
FT /evidence="ECO:0000269|PubMed:16641371"
FT MUTAGEN 229
FT /note="W->Y: Loss of subcellular location to plasma and
FT endosomal membrane."
FT /evidence="ECO:0000269|PubMed:16641371"
FT MUTAGEN 230..231
FT /note="KK->QQ: Loss of subcellular location to plasma
FT membrane, decreased association with endomembranes."
FT /evidence="ECO:0000269|PubMed:16641371"
FT MUTAGEN 230
FT /note="K->Q: Loss of subcellular location to plasma
FT membrane, decreased association with endomembranes."
FT /evidence="ECO:0000269|PubMed:16641371"
FT MUTAGEN 231
FT /note="K->Q: Loss of subcellular location to plasma
FT membrane, decreased association with endomembranes."
FT /evidence="ECO:0000269|PubMed:16641371"
FT MUTAGEN 234
FT /note="C->S: Loss of subcellular location to plasma and
FT endosomal membranes."
FT /evidence="ECO:0000269|PubMed:15664990"
SQ SEQUENCE 236 AA; 26165 MW; 034416FA8CEA2425 CRC64;
MPPRELSEAE PPPLPASTPP PRRRSAPPEL GIKCVLVGDG AVGKSSLIVS YTCNGYPSRY
RPTALDTFSV QVLVDGAPVR IELWDTAGQE DFDRLRSLCY PDTDVFLACF SVVQPSSFQN
ITEKWLPEIR THNPQAPVLL VGTQADLRDD VNVLIQLDQG GREGPVPEPQ AQGLAEKIRA
CCYLECSALT QKNLKEVFDS AILSAIEHKA RLEKKLNAKG VRTLSRCRWK KFFCFV
