RND1_BOVIN
ID RND1_BOVIN Reviewed; 232 AA.
AC Q2HJ68;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Rho-related GTP-binding protein Rho6;
DE AltName: Full=Rho family GTPase 1;
DE AltName: Full=Rnd1;
DE Flags: Precursor;
GN Name=RND1; Synonyms=RHO6;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lacks intrinsic GTPase activity. Has a low affinity for GDP,
CC and constitutively binds GTP. Controls rearrangements of the actin
CC cytoskeleton. Induces the Rac-dependent neuritic process formation in
CC part by disruption of the cortical actin filaments. Causes the
CC formation of many neuritic processes from the cell body with disruption
CC of the cortical actin filaments (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds GRB7 and PLXNB1. Interacts with PLXNA2. Interacts with
CC UBXD5 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; BC113283; AAI13284.1; -; mRNA.
DR RefSeq; NP_001039481.1; NM_001046016.1.
DR AlphaFoldDB; Q2HJ68; -.
DR SMR; Q2HJ68; -.
DR STRING; 9913.ENSBTAP00000024996; -.
DR PaxDb; Q2HJ68; -.
DR Ensembl; ENSBTAT00000024996; ENSBTAP00000024996; ENSBTAG00000018773.
DR GeneID; 508869; -.
DR KEGG; bta:508869; -.
DR CTD; 27289; -.
DR VEuPathDB; HostDB:ENSBTAG00000018773; -.
DR VGNC; VGNC:34004; RND1.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000158666; -.
DR HOGENOM; CLU_041217_21_1_1; -.
DR InParanoid; Q2HJ68; -.
DR OMA; ISRPDTF; -.
DR OrthoDB; 1395905at2759; -.
DR TreeFam; TF330887; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000018773; Expressed in intramuscular adipose tissue and 100 other tissues.
DR ExpressionAtlas; Q2HJ68; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0016322; P:neuron remodeling; IEA:Ensembl.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
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; Cytoplasm; Cytoskeleton; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..229
FT /note="Rho-related GTP-binding protein Rho6"
FT /id="PRO_0000236246"
FT PROPEP 230..232
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281225"
FT MOTIF 42..50
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 23..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 38..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 125..128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 169..170
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT MOD_RES 229
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 229
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 232 AA; 26029 MW; 11BC0ACB8624BAED CRC64;
MKERRAPQPV VARCKLVLVG DVQCGKTAML QVLAKDCYPE TYVPTVFENY TACLETEEQR
VELSLWDTSG SPYYDNVRPL CYSDSDAVLL CFDISRPETV DSALKKWRTE ILDYCPSTRV
LLIGCKTDLR TDLSTLMELS HQKQAPISYE QGCAIAKQLG AEIYLEGSAF TSEKSIHSIF
RTASMVCLNK PSPMPPKSPV RSLSKRLLHL PSRSELISST FKKEKAKSCS IM
