ID   RASH_MSVNS              Reviewed;         189 AA.
AC   P23175;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   08-NOV-2023, entry version 123.
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   Murine sarcoma virus NS.C58.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC   Moloney murine sarcoma virus.
OX   NCBI_TaxID=11815;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3035212; DOI=10.1128/jvi.61.7.2109-2119.1987;
RA   Fredrickson T.N., O'Neill R.R., Rutledge R.A., Theodore T.S., Martin M.A.,
RA   Ruscetti S.K., Austin J.B., Hartley J.W.;
RT   "Biologic and molecular characterization of two newly isolated ras-
RT   containing murine leukemia viruses.";
RL   J. Virol. 61:2109-2119(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   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000305}.
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DR   EMBL; M30733; AAA46574.1; -; Genomic_RNA.
DR   SMR; P23175; -.
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_0000030181"
FT   PROPEP          187..189
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000030182"
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;  21397 MW;  1B6272D68C479FC0 CRC64;
     MTEYKLVVVG ARGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
     QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI KRVKDSDDVP MVLVGNKCDL
     AARTVESRQA QDLARSYGIP YIETSAKTRQ GVEDAFYTLV REIRQHKLRK LNPPDESGPG
     CMSCKCVLS
//