ID   Q9R0B8_MOUSE            Unreviewed;       152 AA.
AC   Q9R0B8;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 2.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=GTPase HRas {ECO:0000256|ARBA:ARBA00039824};
DE            EC=3.6.5.2 {ECO:0000256|ARBA:ARBA00011984};
DE   AltName: Full=H-Ras-1 {ECO:0000256|ARBA:ARBA00042823};
DE   AltName: Full=Transforming protein p21 {ECO:0000256|ARBA:ARBA00042598};
DE   AltName: Full=c-H-ras {ECO:0000256|ARBA:ARBA00042857};
DE   AltName: Full=p21ras {ECO:0000256|ARBA:ARBA00041966};
DE   Flags: Fragment;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAD56718.2};
RN   [1] {ECO:0000313|EMBL:AAD56718.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129/SvJ {ECO:0000313|EMBL:AAD56718.2};
RX   PubMed=3074812; DOI=10.1002/mc.2940010304;
RA   Brown K., Bailleul B., Ramsden M., Fee F., Krumlauf R., Balmain A.;
RT   "Isolation and characterization of the 5' flanking region of the mouse c-
RT   Harvey-ras gene.";
RL   Mol. Carcinog. 1:161-170(1988).
RN   [2] {ECO:0000313|EMBL:AAD56718.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129/SvJ {ECO:0000313|EMBL:AAD56718.2};
RA   Esteban L.M., Santos E.;
RT   "Genomic sequence of murine H-ras.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00023421};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004342};
CC       Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004342}. Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00037794}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00037794}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004423}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004423}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004423}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC       {ECO:0000256|ARBA:ARBA00008344}.
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DR   EMBL; AF081118; AAD56718.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q9R0B8; -.
DR   IntAct; Q9R0B8; 1.
DR   PeptideAtlas; Q9R0B8; -.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; PS51419; RAB; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAD56718.2"
SQ   SEQUENCE   152 AA;  17279 MW;  2AF00B34F58A8F35 CRC64;
     DSYRKQVVID GETCLLDILD TAGQEEYSAM RDQYMRTGEG FLCVFAINNT KSFEDIHQYR
     EQIKRVKDSD DVPMVLVGNK CDLAARTVES RQAQDLARSY GIPYIKTSAK TRQGVEDAFY
     TLVREIRQHK LRKLNPPDES GPGCMSCKCV LS
//