ID   RASH_MSVHA              Reviewed;         241 AA.
AC   P01115; O40604;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   23-FEB-2022, entry version 128.
DE   RecName: Full=Transforming protein p29;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE   Contains:
DE     RecName: Full=Transforming protein p21;
DE   Flags: Precursor;
GN   Name=H-RAS;
OS   Harvey murine sarcoma virus.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX   NCBI_TaxID=11807;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=6287572; DOI=10.1126/science.6287572;
RA   Dhar R., Ellis R.W., Shih T.Y., Oroszlan S., Shapiro B., Maizel J.,
RA   Lowy D., Scolnick E.;
RT   "Nucleotide sequence of the p21 transforming protein of Harvey murine
RT   sarcoma virus.";
RL   Science 217:934-937(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6087292; DOI=10.1093/nar/12.14.5583;
RA   Yasuda S., Furuichi M., Soeda E.;
RT   "An altered DNA sequence encompassing the ras gene of Harvey murine sarcoma
RT   virus.";
RL   Nucleic Acids Res. 12:5583-5588(1984).
RN   [3]
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   [4]
RP   CHARACTERIZATION.
RX   PubMed=6247068; DOI=10.1016/0092-8674(80)90091-4;
RA   Willingham M.C., Pastan I., Shih T.Y., Scolnick E.M.;
RT   "Localization of the src gene product of the Harvey strain of MSV to plasma
RT   membrane of transformed cells by electron microscopic
RT   immunocytochemistry.";
RL   Cell 19:1005-1014(1980).
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; Lipid-anchor; Cytoplasmic
CC       side. Note=Inner surface of plasma membrane.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA46570.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA25322.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X00740; CAA25322.1; ALT_INIT; Genomic_DNA.
DR   EMBL; J02207; AAA46569.1; -; Genomic_RNA.
DR   EMBL; J02207; AAA46570.1; ALT_INIT; Genomic_RNA.
DR   EMBL; M24154; AAA46568.1; -; Genomic_RNA.
DR   PIR; A01363; TVMV3H.
DR   BMRB; P01115; -.
DR   SMR; P01115; -.
DR   SwissPalm; P01115; -.
DR   Proteomes; UP000232675; Genome.
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   GTP-binding; Host cell membrane; Host membrane; Hydrolase; Lipoprotein;
KW   Membrane; Methylation; Nucleotide-binding; Oncogene; Palmitate;
KW   Prenylation.
FT   CHAIN           1..238
FT                   /note="Transforming protein p29"
FT                   /id="PRO_0000030183"
FT   CHAIN           53..238
FT                   /note="Transforming protein p21"
FT                   /id="PRO_0000030184"
FT   PROPEP          239..241
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000030185"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         238
FT                   /note="Cysteine methyl ester; by host"
FT                   /evidence="ECO:0000305"
FT   LIPID           233
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000255"
FT   LIPID           236
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000255"
FT   LIPID           238
FT                   /note="S-farnesyl cysteine; by host"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        174
FT                   /note="G -> A (in Ref. 2; CAA25322)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   241 AA;  26328 MW;  5A8983BFCD826C04 CRC64;
     MPAARAAPAA DEPMRDPVAP VRAPALPRPA PGAVAPASGG ARAPGLAAPV EAMTEYKLVV
     VGARGVGKSA LTIQLIQNHF VDEYDPTIED SYRKQVVIDG ETCLLDILDT TGQEEYSAMR
     DQYMRTGEGF LCVFAINNTK SFEDIHQYRE QIKRVKDSDD VPMVLVGNKC DLAGRTVESR
     QAQDLARSYG IPYIETSAKT RQGVEDAFYT LVREIRQHKL RKLNPPDESG PGCMSCKCVL
     S