ID   RASH_RRASV              Reviewed;         248 AA.
AC   P01114;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   13-SEP-2023, entry version 133.
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=RAS;
OS   Rasheed rat sarcoma virus.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC   Murine leukemia virus.
OX   NCBI_TaxID=11816;
OH   NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6344220; DOI=10.1126/science.6344220;
RA   Rasheed S., Norman G.L., Heidecker G.;
RT   "Nucleotide sequence of the Rasheed rat sarcoma virus oncogene: new
RT   mutations.";
RL   Science 221:155-157(1983).
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; J02294; AAA47420.1; -; Genomic_RNA.
DR   PIR; A01362; TVMVRS.
DR   BMRB; P01114; -.
DR   SMR; P01114; -.
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; 1.10.150.180; Gamma-retroviral matrix domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR000840; G_retro_matrix.
DR   InterPro; IPR036946; G_retro_matrix_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010999; Retrovr_matrix.
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; PF01140; Gag_MA; 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   SUPFAM; SSF47836; Retroviral matrix proteins; 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..245
FT                   /note="Transforming protein p29"
FT                   /id="PRO_0000030186"
FT   CHAIN           59..245
FT                   /note="Transforming protein p21"
FT                   /id="PRO_0000030187"
FT   PROPEP          246..248
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000030188"
FT   REGION          28..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         245
FT                   /note="Cysteine methyl ester; by host"
FT                   /evidence="ECO:0000305"
FT   LIPID           240
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000255"
FT   LIPID           243
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000255"
FT   LIPID           245
FT                   /note="S-farnesyl cysteine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   248 AA;  27424 MW;  9A0CC2CD8EFD7F5C CRC64;
     MGQSLTTPLS LTLDHWKDVR DRARDQSVEI KKGPLRRSGT VAPASGGAGA PGLAAPVEAM
     TEYKLVVVGA RGVGKSALTI QLIQNHFVDE YDPTIEDSYR KQVVIDGETC LLDILDTAGQ
     EEYSAMRDQY MRTGEGFLCV FAINNTKSFE DIHQYREQIK RVKDSDDVPM VLVGNKCDLA
     AHTVESRQAQ DLARSYGIPY IETSAKTRPG VEDAFYTLVR EIRQHKLRKL NPPDESGPGC
     MSCKCVLS
//