RRAS_RAT
ID RRAS_RAT Reviewed; 218 AA.
AC D3Z8L7;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Ras-related protein R-Ras;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P62070};
DE AltName: Full=p23;
DE Flags: Precursor;
GN Name=Rras;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG Genoscope - CEA;
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH RGS14.
RX PubMed=19319189; DOI=10.1371/journal.pone.0004884;
RA Willard F.S., Willard M.D., Kimple A.J., Soundararajan M., Oestreich E.A.,
RA Li X., Sowa N.A., Kimple R.J., Doyle D.A., Der C.J., Zylka M.J.,
RA Snider W.D., Siderovski D.P.;
RT "Regulator of G-protein signaling 14 (RGS14) is a selective H-Ras
RT effector.";
RL PLoS ONE 4:E4884-E4884(2009).
CC -!- FUNCTION: Regulates the organization of the actin cytoskeleton. With
CC OSPBL3, modulates integrin beta-1 (ITGB1) activity.
CC {ECO:0000250|UniProtKB:P10301}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:P62070};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P62070};
CC -!- SUBUNIT: Interacts with PLCE1 (By similarity). Interacts (active GTP-
CC bound form preferentially) with RGS14 (PubMed:19319189). Interacts with
CC OSBPL3 (By similarity). Interacts with ZDHHC19 (By similarity).
CC {ECO:0000250|UniProtKB:P10301, ECO:0000269|PubMed:19319189}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Inner surface of
CC plasma membrane possibly with attachment requiring acylation of the C-
CC terminal cysteine. {ECO:0000250}.
CC -!- PTM: S-palmitoylated by ZDHHC19, leading to increased association with
CC membranes and with rafts/caveolae as well as enhanced cell viability.
CC {ECO:0000250|UniProtKB:P10301}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; FQ211166; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH473979; EDM07427.1; -; Genomic_DNA.
DR RefSeq; NP_001101951.1; NM_001108481.1.
DR AlphaFoldDB; D3Z8L7; -.
DR SMR; D3Z8L7; -.
DR CORUM; D3Z8L7; -.
DR STRING; 10116.ENSRNOP00000027809; -.
DR SwissPalm; D3Z8L7; -.
DR jPOST; D3Z8L7; -.
DR PaxDb; D3Z8L7; -.
DR PeptideAtlas; D3Z8L7; -.
DR PRIDE; D3Z8L7; -.
DR Ensembl; ENSRNOT00000027809; ENSRNOP00000027809; ENSRNOG00000037247.
DR GeneID; 361568; -.
DR KEGG; rno:361568; -.
DR UCSC; RGD:1311443; rat.
DR CTD; 6237; -.
DR RGD; 1311443; Rras.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000160972; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; D3Z8L7; -.
DR OMA; GCPCILL; -.
DR OrthoDB; 1259506at2759; -.
DR PhylomeDB; D3Z8L7; -.
DR TreeFam; TF312796; -.
DR Reactome; R-RNO-416550; Sema4D mediated inhibition of cell attachment and migration.
DR PRO; PR:D3Z8L7; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000037247; Expressed in lung and 19 other tissues.
DR Genevisible; D3Z8L7; RN.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0019003; F:GDP binding; ISO:RGD.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0060325; P:face morphogenesis; ISO:RGD.
DR GO; GO:0002521; P:leukocyte differentiation; ISO:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR GO; GO:1900148; P:negative regulation of Schwann cell migration; IEA:Ensembl.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:1904906; P:positive regulation of endothelial cell-matrix adhesion via fibronectin; ISO:RGD.
DR GO; GO:2001214; P:positive regulation of vasculogenesis; ISO:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0036135; P:Schwann cell migration; IEA:Ensembl.
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; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Palmitate; Prenylation; Reference proteome.
FT CHAIN 1..215
FT /note="Ras-related protein R-Ras"
FT /id="PRO_0000408475"
FT PROPEP 216..218
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000408476"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 58..66
FT /note="Effector region"
FT BINDING 36..44
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P10301"
FT BINDING 83..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P10301"
FT BINDING 172..174
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P10301"
FT MOD_RES 215
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 215
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 142
FT /note="N -> S (in Ref. 1; FQ211166)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 218 AA; 23909 MW; 3410B3A4274EEEED CRC64;
MSSGAASGTG RGRPRGGGPG PRDPPPGETH KLVVVGGGGV GKSALTIQFI QSYFVSDYDP
TIEDSYTKIC TVDGIPARLD ILDTAGQEEF GAMREQYMRA GNGFLLVFAI NDRQSFIEVS
KLFTQILRVK DRDDFPIVLV GNKADLETQR QVLRSEASSF SASHHMTYFE ASAKLRLNVD
EAFEQLVRTV RKYQEQELPP SPPSAPRKKD GRCPCVLL
