RAC1_BETVU
ID RAC1_BETVU Reviewed; 197 AA.
AC Q39435;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Rac-like GTP-binding protein RHO1;
DE AltName: Full=RHO1Bv;
DE Flags: Precursor;
GN Name=RHO1;
OS Beta vulgaris (Sugar beet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX NCBI_TaxID=161934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. D100 KS 38080;
RX PubMed=8680960;
RA Dallery E., Quief S., Ben-Jilany K.E., Kerckaert J.-P., Hagege D.;
RT "Molecular cloning and structural analysis of cDNAs that encode 3 small
RT GTP-binding proteins from sugar beet.";
RL C. R. Acad. Sci. III, Sci. Vie 319:91-97(1996).
CC -!- FUNCTION: Inactive GDP-bound Rho GTPases reside in the cytosol, are
CC found in a complex with Rho GDP-dissociation inhibitors (Rho GDIs), and
CC are released from the GDI protein in order to translocate to membranes
CC upon activation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=Associated with the
CC membrane when activated.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; Z49191; CAA89050.1; -; mRNA.
DR RefSeq; NP_001290012.1; NM_001303083.1.
DR RefSeq; XP_010679891.1; XM_010681589.2.
DR AlphaFoldDB; Q39435; -.
DR SMR; Q39435; -.
DR EnsemblPlants; KMT09564; KMT09564; BVRB_6g130240.
DR GeneID; 104895157; -.
DR Gramene; KMT09564; KMT09564; BVRB_6g130240.
DR KEGG; bvg:104895157; -.
DR PhylomeDB; Q39435; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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 Cytoplasm; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation.
FT CHAIN 1..194
FT /note="Rac-like GTP-binding protein RHO1"
FT /id="PRO_0000198926"
FT PROPEP 195..197
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000227588"
FT MOTIF 35..43
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 13..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 60..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 118..121
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 194
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 194
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 197 AA; 21516 MW; 5C7AC19CB2F780B2 CRC64;
MSASRFIKCV TVGDGAVGKT CLLISYTSNT FPTDYVPTVF DNFSANVVVN GATVNLGLWD
TAGQEDYNRL RPLSYRGADV FILAFSLISK ASYENVSKKW IPELKHYAPG VPIVLVGTKL
DLRDDKQFFI DHPGAVPITT AQGEELRKLI GAPAYIECSS KTQQNVKAVF DAAIKVVLQP
PKTKKKKSKA QKACSIL
