ID RASM_MOUSE Reviewed; 208 AA.
AC O08989;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 27-MAR-2024, entry version 182.
DE RecName: Full=Ras-related protein M-Ras;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01116};
DE AltName: Full=Muscle and microspikes Ras;
DE AltName: Full=Ras-related protein R-Ras3;
DE AltName: Full=X-Ras;
DE Flags: Precursor;
GN Name=Mras; Synonyms=Xras;
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=9395237; DOI=10.1038/sj.onc.1201416;
RA Matsumoto K., Asano T., Endo T.;
RT "Novel small GTPase M-Ras participates in reorganization of actin
RT cytoskeleton.";
RL Oncogene 15:2409-2417(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=10477695;
RA Louahed J., Grasso L., De Smet C., van Roost E., Wildmann C.,
RA Nicolaides N.C., Levitt R.C., Renauld J.-C.;
RT "Interleukin-9-induced expression of M-Ras/R-Ras3 oncogene in T-helper
RT clones.";
RL Blood 94:1701-1710(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Leslie K.B., Schrader J.W.;
RT "Characterization of a transforming, novel ras-related molecule.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [5]
RP INTERACTION WITH RGL3.
RX PubMed=11313946; DOI=10.1038/sj.onc.1204053;
RA Ehrhardt G.R., Korherr C., Wieler J.S., Knaus M., Schrader J.W.;
RT "A novel potential effector of M-Ras and p21 Ras negatively regulates p21
RT Ras-mediated gene induction and cell growth.";
RL Oncogene 20:188-197(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, 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: Serves as an important signal transducer for a novel upstream
CC stimuli in controlling cell proliferation. Activates the MAP kinase
CC pathway (By similarity). {ECO:0000250|UniProtKB:O14807}.
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; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P01116};
CC -!- SUBUNIT: Forms a multiprotein complex with SHOC2, Raf (RAF1) and
CC protein phosphatase 1 (PPP1CA, PPP1CB and PPP1CC). Interacts (active
CC GTP-bound form preferentially) with RGS14 (By similarity). Interacts
CC with RGL3. {ECO:0000250|UniProtKB:P97538, ECO:0000269|PubMed:11313946}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB004879; BAA20538.1; -; mRNA.
DR EMBL; AF043581; AAD02277.1; -; mRNA.
DR EMBL; AF031159; AAD01926.1; -; mRNA.
DR EMBL; BC024389; AAH24389.1; -; mRNA.
DR CCDS; CCDS23433.1; -.
DR RefSeq; NP_032650.1; NM_008624.3.
DR RefSeq; XP_006510888.1; XM_006510825.2.
DR PDB; 1X1R; X-ray; 1.30 A; A=1-178.
DR PDB; 1X1S; X-ray; 2.20 A; A=1-178.
DR PDB; 3KKO; X-ray; 1.90 A; A/B/P=1-178.
DR PDB; 3KKP; X-ray; 1.35 A; A=1-178.
DR PDB; 3KKQ; X-ray; 1.20 A; A=1-178.
DR PDB; 3PIR; X-ray; 2.75 A; A=1-178.
DR PDB; 3PIT; X-ray; 1.55 A; A=1-178.
DR PDBsum; 1X1R; -.
DR PDBsum; 1X1S; -.
DR PDBsum; 3KKO; -.
DR PDBsum; 3KKP; -.
DR PDBsum; 3KKQ; -.
DR PDBsum; 3PIR; -.
DR PDBsum; 3PIT; -.
DR AlphaFoldDB; O08989; -.
DR SMR; O08989; -.
DR BioGRID; 201483; 2.
DR STRING; 10090.ENSMUSP00000035045; -.
DR iPTMnet; O08989; -.
DR PhosphoSitePlus; O08989; -.
DR PaxDb; 10090-ENSMUSP00000035045; -.
DR PeptideAtlas; O08989; -.
DR ProteomicsDB; 255111; -.
DR Pumba; O08989; -.
DR Antibodypedia; 33434; 200 antibodies from 26 providers.
DR DNASU; 17532; -.
DR Ensembl; ENSMUST00000035045.15; ENSMUSP00000035045.9; ENSMUSG00000032470.18.
DR Ensembl; ENSMUST00000119472.8; ENSMUSP00000112407.2; ENSMUSG00000032470.18.
DR Ensembl; ENSMUST00000122384.9; ENSMUSP00000113275.2; ENSMUSG00000032470.18.
DR GeneID; 17532; -.
DR KEGG; mmu:17532; -.
DR UCSC; uc009rec.1; mouse.
DR AGR; MGI:1100856; -.
DR CTD; 22808; -.
DR MGI; MGI:1100856; Mras.
DR VEuPathDB; HostDB:ENSMUSG00000032470; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000156353; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; O08989; -.
DR OMA; DRDVYPM; -.
DR OrthoDB; 8685at2759; -.
DR PhylomeDB; O08989; -.
DR TreeFam; TF312796; -.
DR Reactome; R-MMU-5673000; RAF activation.
DR BioGRID-ORCS; 17532; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Mras; mouse.
DR EvolutionaryTrace; O08989; -.
DR PRO; PR:O08989; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; O08989; Protein.
DR Bgee; ENSMUSG00000032470; Expressed in dentate gyrus of hippocampal formation granule cell and 212 other cell types or tissues.
DR ExpressionAtlas; O08989; baseline and differential.
DR Genevisible; O08989; MM.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0030742; F:GTP-dependent protein binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; ISO:MGI.
DR CDD; cd04145; M_R_Ras_like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR24070; RAS, DI-RAS, AND RHEB FAMILY MEMBERS OF SMALL GTPASE SUPERFAMILY; 1.
DR PANTHER; PTHR24070:SF268; RAS-RELATED PROTEIN M-RAS; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00176; RAN; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..205
FT /note="Ras-related protein M-Ras"
FT /id="PRO_0000082655"
FT PROPEP 206..208
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281305"
FT MOTIF 42..50
FT /note="Effector region"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 67..71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 205
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 205
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:3KKQ"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:3KKQ"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:3KKP"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:3KKP"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:3KKQ"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:3KKQ"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3KKQ"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:3KKQ"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:3KKQ"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:3KKQ"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:3KKQ"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:3KKQ"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:3KKP"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:3KKQ"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:3KKQ"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:3KKQ"
FT HELIX 164..177
FT /evidence="ECO:0007829|PDB:3KKQ"
SQ SEQUENCE 208 AA; 23901 MW; 975CFDD1FDF37FCF CRC64;
MATSAVPSEN LPTYKLVVVG DGGVGKSALT IQFFQKIFVP DYDPTIEDSY LKHTEIDNQW
AILDVLDTAG QEEFSAMREQ YMRTGDGFLI VYSVTDKASF EHVDRFHQLI LRVKDRESFP
MILVANKVDL MHLRKVTRDQ GKEMATKYNI PYIETSAKDP PLNVDKTFHD LVRVIRQQVP
EKNQKKKKKT KWRGDRATGT HKLQCVIL
//
