RHOU_BOVIN
ID RHOU_BOVIN Reviewed; 255 AA.
AC A5D7J5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Rho-related GTP-binding protein RhoU;
GN Name=RHOU {ECO:0000250|UniProtKB:Q7L0Q8};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAI40581.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI40581.1};
RC TISSUE=Hippocampus {ECO:0000312|EMBL:AAI40581.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; BC140580; AAI40581.1; -; mRNA.
DR RefSeq; NP_001091616.1; NM_001098147.1.
DR AlphaFoldDB; A5D7J5; -.
DR SMR; A5D7J5; -.
DR STRING; 9913.ENSBTAP00000024876; -.
DR PaxDb; A5D7J5; -.
DR Ensembl; ENSBTAT00000024876; ENSBTAP00000024876; ENSBTAG00000018691.
DR GeneID; 781044; -.
DR KEGG; bta:781044; -.
DR CTD; 58480; -.
DR VEuPathDB; HostDB:ENSBTAG00000018691; -.
DR VGNC; VGNC:33955; RHOU.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000156644; -.
DR HOGENOM; CLU_041217_21_7_1; -.
DR InParanoid; A5D7J5; -.
DR OMA; CEKWVPE; -.
DR OrthoDB; 1091615at2759; -.
DR TreeFam; TF321839; -.
DR Reactome; R-BTA-9013420; RHOU GTPase cycle.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000018691; Expressed in prostate gland and 104 other tissues.
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; 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: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:0008360; P:regulation of cell shape; ISS:UniProtKB.
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..255
FT /note="Rho-related GTP-binding protein RhoU"
FT /id="PRO_0000326434"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 53..60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q7L0Q8"
FT BINDING 100..104
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q7L0Q8"
FT BINDING 158..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61586"
FT LIPID 253
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q7L0Q8"
SQ SEQUENCE 255 AA; 27824 MW; 7650FAC590D64E52 CRC64;
MPPQQGDPAF PGRCEAPPVP PRRERGVRGP GAPGGRGRAG GPEGHGVKCV LVGDGAVGKT
SLVVSYTTNG YPTEYIPTAF DNFSAVVSVD GRPVKLQLCD TAGQDEFDKL RPLCYTNADI
FLLCFSVVGP SSFQNVSEKW VPEIRCHCPK APIILVGTQS DLREDVKVLI ELDKCKEKPV
PEEAARLCAE EIKATSYIEC SALTQKNLKE VFDAAIVAGI QYSDSQQQPK KSKSRTPDKM
KTLSKSWWKK YCCFV
