RHOU_MOUSE
ID RHOU_MOUSE Reviewed; 261 AA.
AC Q9EQT3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Rho-related GTP-binding protein RhoU;
DE AltName: Full=Rho GTPase-like protein ARHU;
DE AltName: Full=Wnt-1 responsive Cdc42 homolog 1;
DE Short=WRCH-1;
GN Name=Rhou {ECO:0000312|MGI:MGI:1916831};
GN Synonyms=Arhu {ECO:0000312|MGI:MGI:1916831}, G28k,
GN Wrch1 {ECO:0000312|EMBL:AAK83341.1};
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:AAK83341.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11459829; DOI=10.1101/gad.894301;
RA Tao W., Pennica D., Xu L., Kalejta R.F., Levine A.J.;
RT "Wrch-1, a novel member of the Rho gene family that is regulated by Wnt-
RT 1.";
RL Genes Dev. 15:1796-1807(2001).
RN [2] {ECO:0000312|EMBL:BAB18639.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14731133; DOI=10.1111/j.1440-1746.2004.03298.x;
RA Daigo Y., Takayama I., Ponder B.A.J., Caldas C., Ward S.M., Sanders K.M.,
RA Fujino M.A.;
RT "Novel human, mouse and Xenopus genes encoding a member of the RAS
RT superfamily of low-molecular-weight GTP-binding proteins and its
RT downregulation in W/WV mouse jejunum.";
RL J. Gastroenterol. Hepatol. 19:211-217(2004).
CC -!- FUNCTION: Acts upstream of PAK1 to regulate the actin cytoskeleton,
CC adhesion turnover and increase cell migration. Stimulates quiescent
CC cells to reenter the cell cycle. Has no detectable GTPase activity but
CC its high intrinsic guanine nucleotide exchange activity suggests it is
CC constitutively GTP-bound. Plays a role in the regulation of cell
CC morphology and cytoskeletal organization. Required in the control of
CC cell shape (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q7L0Q8};
CC -!- SUBUNIT: Interacts with PAK3 (By similarity). Interacts with ARHGAP30
CC in a GTP-independent manner. In its GTP-loaded conformation, interacts
CC with ARHGAP31. Interacts with PTK2B/PYK2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7L0Q8};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q7L0Q8}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q7L0Q8}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q7L0Q8}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q7L0Q8}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:Q7L0Q8}. Cell projection, podosome
CC {ECO:0000250|UniProtKB:Q7L0Q8}. Note=Localizes to podosomes in SRC-
CC transformed cells. {ECO:0000250|UniProtKB:Q7L0Q8}.
CC -!- PTM: Tyrosine phosphorylated by SRC in response to PTK2B/PYK2
CC activation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000250|UniProtKB:Q7L0Q8}.
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DR EMBL; AF378088; AAK83341.1; -; mRNA.
DR EMBL; AB051827; BAB18639.1; -; mRNA.
DR CCDS; CCDS22762.1; -.
DR RefSeq; NP_598716.1; NM_133955.4.
DR AlphaFoldDB; Q9EQT3; -.
DR SMR; Q9EQT3; -.
DR STRING; 10090.ENSMUSP00000038915; -.
DR iPTMnet; Q9EQT3; -.
DR PhosphoSitePlus; Q9EQT3; -.
DR SwissPalm; Q9EQT3; -.
DR MaxQB; Q9EQT3; -.
DR PaxDb; Q9EQT3; -.
DR PRIDE; Q9EQT3; -.
DR ProteomicsDB; 253236; -.
DR Antibodypedia; 34671; 162 antibodies from 25 providers.
DR DNASU; 69581; -.
DR Ensembl; ENSMUST00000045487; ENSMUSP00000038915; ENSMUSG00000039960.
DR GeneID; 69581; -.
DR KEGG; mmu:69581; -.
DR UCSC; uc009nwm.1; mouse.
DR CTD; 58480; -.
DR MGI; MGI:1916831; Rhou.
DR VEuPathDB; HostDB:ENSMUSG00000039960; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000156644; -.
DR HOGENOM; CLU_041217_21_7_1; -.
DR InParanoid; Q9EQT3; -.
DR OMA; CEKWVPE; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q9EQT3; -.
DR TreeFam; TF321839; -.
DR Reactome; R-MMU-9013420; RHOU GTPase cycle.
DR BioGRID-ORCS; 69581; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Rhou; mouse.
DR PRO; PR:Q9EQT3; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9EQT3; protein.
DR Bgee; ENSMUSG00000039960; Expressed in vestibular membrane of cochlear duct and 261 other tissues.
DR Genevisible; Q9EQT3; MM.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IMP:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:MGI.
DR GO; GO:0032488; P:Cdc42 protein signal transduction; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
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:0000082; P:G1/S transition of mitotic cell cycle; IDA:MGI.
DR GO; GO:0016601; P:Rac protein signal transduction; IDA:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IDA: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 junction; Cell membrane; Cell projection; Golgi apparatus;
KW GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Palmitate; Phosphoprotein; Reference proteome.
FT CHAIN 1..261
FT /note="Rho-related GTP-binding protein RhoU"
FT /id="PRO_0000326436"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q7L0Q8"
FT BINDING 106..110
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q7L0Q8"
FT BINDING 164..167
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT LIPID 259
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q7L0Q8"
SQ SEQUENCE 261 AA; 28354 MW; 8EC4250071E75B14 CRC64;
MAPQQGRPAL PARCEPPAAP PVPPRRERGG RGARGPGVSG GRGRAGGAEG RGVKCVLVGD
GAVGKTSLVV SYTTNGYPTE YIPTAFDNFS AVVSVDGRPV RLQLCDTAGQ DEFDKLRPLC
YTNTDIFLLC FSVVSPTSFQ NVGEKWVPEI RRHCPKAPII LVGTQSDLRE DVKVLIELDK
CKEKPVPEEA AKLCAEEVKA VSYIECSALT QKNLKEVFDA AIVAGIQHSD SQLQPKKSKS
RTPDKVRDLS KSWWRKYCCL A
