RASK_MSVKI
ID RASK_MSVKI Reviewed; 189 AA.
AC P01117;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=GTPase KRas;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01116};
DE AltName: Full=Ki-Ras;
DE AltName: Full=Transforming protein p21/K-Ras;
DE Flags: Precursor;
GN Name=K-RAS; Synonyms=KIS;
OS Kirsten murine sarcoma virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11808;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6287573; DOI=10.1126/science.6287573;
RA Tsuchida N., Ryder T., Ohtsubo E.;
RT "Nucleotide sequence of the oncogene encoding the p21 transforming protein
RT of Kirsten murine sarcoma virus.";
RL Science 217:937-939(1982).
RN [2]
RP REVIEW.
RX PubMed=3304147; DOI=10.1146/annurev.bi.56.070187.004023;
RA Barbacid M.;
RT "Ras genes.";
RL Annu. Rev. Biochem. 56:779-827(1987).
RN [3]
RP PROTEIN SEQUENCE OF 50-64, AND PHOSPHORYLATION AT THR-59.
RX PubMed=6288698; DOI=10.1016/s0021-9258(18)33830-4;
RA Shih T.Y., Stokes P.E., Smythers G.W., Dhar R., Oroszlan S.;
RT "Characterization of the phosphorylation sites and the surrounding amino
RT acid sequences of the p21 transforming proteins coded for by the Harvey and
RT Kirsten strains of murine sarcoma viruses.";
RL J. Biol. Chem. 257:11767-11773(1982).
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 -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. Activated by a guanine nucleotide-
CC exchange factor (GEF) and inactivated by a GTPase-activating protein
CC (GAP).
CC -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- MISCELLANEOUS: This p21 transforming protein was generated by a
CC transduction of rodent cellular K-Ras-2 gene.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; J02228; AAA46572.1; -; Genomic_RNA.
DR PIR; A01366; TVMV2K.
DR SMR; P01117; -.
DR iPTMnet; P01117; -.
DR SwissPalm; P01117; -.
DR PRIDE; P01117; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P: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; 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 Direct protein sequencing; GTP-binding; Host cell membrane; Host membrane;
KW Hydrolase; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Oncogene; Palmitate; Phosphoprotein; Prenylation.
FT CHAIN 1..186
FT /note="GTPase KRas"
FT /id="PRO_0000030189"
FT PROPEP 187..189
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000030190"
FT MOTIF 32..40
FT /note="Effector region"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 59
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:6288698"
FT MOD_RES 186
FT /note="Cysteine methyl ester; by host"
FT /evidence="ECO:0000305"
FT LIPID 180
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255"
FT LIPID 186
FT /note="S-farnesyl cysteine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 189 AA; 21715 MW; BBA3FB03EC374A4E CRC64;
MTEYKLVVVG ASGVGKSALT IQLIQNHFVD EYDPTIQDSY RKQVVIDGET CLLDILDTTG
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHHYREQL KRVKDSEDVP MVLVGNKCDL
PSRTVDTKQA QELARSYGIP FIETSAKTRQ RVEDAFYTLV REIRQYRLKK ISKEEKTPGC
VKIKKCVIM
