ID   RASH_MSVMO              Reviewed;         189 AA.
AC   P01113;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   13-SEP-2023, entry version 129.
DE   RecName: Full=GTPase HRas;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE   AltName: Full=Transforming protein p21/H-Ras;
DE   Flags: Precursor;
GN   Name=H-RAS;
OS   Moloney murine sarcoma virus (MoMSV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX   NCBI_TaxID=11809;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2983103; DOI=10.1128/jvi.53.3.984-987.1985;
RA   Reddy E.P., Lipman D., Andersen P.R., Tronick S.R., Aaronson S.A.;
RT   "Nucleotide sequence analysis of the BALB/c murine sarcoma virus
RT   transforming gene.";
RL   J. Virol. 53:984-987(1985).
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).
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:P01112};
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:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- MISCELLANEOUS: This p21 transforming protein was generated by a
CC       transduction of rodent cellular H-ras-1 gene.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; M10035; AAA46575.1; -; Genomic_RNA.
DR   PIR; A01361; TVMVB.
DR   BMRB; P01113; -.
DR   SMR; P01113; -.
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   CDD; cd04138; H_N_K_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:SF385; GTPASE HRAS; 1.
DR   PANTHER; PTHR24070; RAS, DI-RAS, AND RHEB FAMILY MEMBERS OF SMALL GTPASE SUPERFAMILY; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 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   3: Inferred from homology;
KW   GTP-binding; Host cell membrane; Host membrane; Hydrolase; Lipoprotein;
KW   Membrane; Methylation; Nucleotide-binding; Oncogene; Palmitate;
KW   Prenylation.
FT   CHAIN           1..186
FT                   /note="GTPase HRas"
FT                   /id="PRO_0000030179"
FT   PROPEP          187..189
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000030180"
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         186
FT                   /note="Cysteine methyl ester; by host"
FT                   /evidence="ECO:0000305"
FT   LIPID           181
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000255"
FT   LIPID           184
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;  21368 MW;  22624F6AC0185A4E CRC64;
     MTEYKLVVVG AKGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
     QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI KRVKDSDDVP MVLVGNKCDL
     AARTVESRQA QDLARSYGIP YIKTSAKTRQ GVEDAFYTLV REIRQHKLRK LNPPDESGPG
     CMSCKCVLS
//