RRAS_MOUSE
ID RRAS_MOUSE Reviewed; 218 AA.
AC P10833;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 183.
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 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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3098437; DOI=10.1016/0092-8674(87)90364-3;
RA Lowe D.G., Capon D.J., Delwart E., Sakaguchi A.Y., Naylor S.L.,
RA Goeddel D.V.;
RT "Structure of the human and murine R-ras genes, novel genes closely related
RT to ras proto-oncogenes.";
RL Cell 48:137-146(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). Interacts with
CC OSBPL3 (By similarity). Interacts with ZDHHC19 (By similarity).
CC {ECO:0000250|UniProtKB:D3Z8L7, ECO:0000250|UniProtKB:P10301}.
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 (By similarity with RAS).
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; M21019; AAA40038.1; -; mRNA.
DR EMBL; BC009105; AAH09105.1; -; mRNA.
DR CCDS; CCDS21226.1; -.
DR RefSeq; NP_033127.1; NM_009101.2.
DR AlphaFoldDB; P10833; -.
DR SMR; P10833; -.
DR BioGRID; 203020; 1.
DR STRING; 10090.ENSMUSP00000042150; -.
DR iPTMnet; P10833; -.
DR PhosphoSitePlus; P10833; -.
DR SwissPalm; P10833; -.
DR EPD; P10833; -.
DR jPOST; P10833; -.
DR PaxDb; P10833; -.
DR PeptideAtlas; P10833; -.
DR PRIDE; P10833; -.
DR ProteomicsDB; 262708; -.
DR Antibodypedia; 32074; 240 antibodies from 32 providers.
DR DNASU; 20130; -.
DR Ensembl; ENSMUST00000044111; ENSMUSP00000042150; ENSMUSG00000038387.
DR GeneID; 20130; -.
DR KEGG; mmu:20130; -.
DR UCSC; uc009gss.1; mouse.
DR CTD; 6237; -.
DR MGI; MGI:98179; Rras.
DR VEuPathDB; HostDB:ENSMUSG00000038387; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000160972; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P10833; -.
DR OMA; GCPCILL; -.
DR OrthoDB; 1259506at2759; -.
DR PhylomeDB; P10833; -.
DR TreeFam; TF312796; -.
DR Reactome; R-MMU-416550; Sema4D mediated inhibition of cell attachment and migration.
DR BioGRID-ORCS; 20130; 3 hits in 78 CRISPR screens.
DR PRO; PR:P10833; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P10833; protein.
DR Bgee; ENSMUSG00000038387; Expressed in aorta tunica media and 254 other tissues.
DR ExpressionAtlas; P10833; baseline and differential.
DR Genevisible; P10833; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0016477; P:cell migration; IGI:MGI.
DR GO; GO:0060325; P:face morphogenesis; ISO:MGI.
DR GO; GO:0002521; P:leukocyte differentiation; ISO:MGI.
DR GO; GO:1900148; P:negative regulation of Schwann cell migration; IGI:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:1904906; P:positive regulation of endothelial cell-matrix adhesion via fibronectin; ISO:MGI.
DR GO; GO:2001214; P:positive regulation of vasculogenesis; ISO:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0036135; P:Schwann cell migration; IGI: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; 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_0000082651"
FT PROPEP 216..218
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281301"
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"
SQ SEQUENCE 218 AA; 23764 MW; C1D32CE7904322E5 CRC64;
MSSGAASGTG RGRPRGGGPG PRDPPPGETH KLVVVGGGGV GKSALTIQFI QSYFVSDYDP
TIEDSYTKIC TVDGIPARLD ILDTAGQEEF GAMREQYMRA GNGFLLVFAI NDRQSFNEVG
KLFTQILRVK DRDDFPIVLV GNKADLENQR QVLRSEASSF SASHHMTYFE ASAKLRLNVD
EAFEQLVRAV RKYQEQELPP SPPSAPRKKD GGCPCVLL
