RASM_RAT
ID RASM_RAT Reviewed; 208 AA.
AC P97538; O09021;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Ras-related protein M-Ras;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01116};
DE AltName: Full=Ras-related protein R-Ras3;
DE Flags: Precursor;
GN Name=Mras; Synonyms=Rras3;
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 [MRNA].
RC TISSUE=Brain;
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 SEQUENCE REVISION TO 136.
RA Endo T.;
RL Submitted (JUN-1997) 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: Serve 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 with RGL3
CC (By similarity). Interacts (active GTP-bound form preferentially) with
CC RGS14. {ECO:0000250|UniProtKB:O14807, ECO:0000269|PubMed:19319189}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle cells.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; D89863; BAA20531.1; -; mRNA.
DR PIR; T10774; T10774.
DR AlphaFoldDB; P97538; -.
DR SMR; P97538; -.
DR IntAct; P97538; 2.
DR MINT; P97538; -.
DR STRING; 10116.ENSRNOP00000045851; -.
DR PaxDb; P97538; -.
DR PRIDE; P97538; -.
DR UCSC; RGD:3111; rat.
DR RGD; 3111; Mras.
DR eggNOG; KOG0395; Eukaryota.
DR InParanoid; P97538; -.
DR PhylomeDB; P97538; -.
DR Reactome; R-RNO-5673000; RAF activation.
DR PRO; PR:P97538; -.
DR Proteomes; UP000002494; Unplaced.
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:RGD.
DR GO; GO:0003924; F:GTPase activity; ISO:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; ISO:RGD.
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; Prenylation; Reference proteome.
FT CHAIN 1..205
FT /note="Ras-related protein M-Ras"
FT /id="PRO_0000082656"
FT PROPEP 206..208
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281306"
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"
SQ SEQUENCE 208 AA; 23887 MW; 0869627A12C67E8A CRC64;
MATSAVPSDN LPTYKLVVVG DGGVGKSALT IQFFQKIFVP DYDPTIEDSY LKHTEIDNQW
AILDVLDTAG QEEFSAMREQ YMRTGDGFLI VYSVTDKASF EHVDRFHQLI LRVKDRESFP
MILVANKVDL MHLRKVTRDQ GKEMATKYNI PYIETSAKDP PLNVDKTFHD LVRVIRQQVP
EKNQKKKKKT KWRGDRATGT HKLQCVIL
