ID   RASH_RAT                Reviewed;         189 AA.
AC   P20171;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   09-JAN-2007, entry version 54.
DE   GTPase HRas precursor (Transforming protein p21) (p21ras) (H-Ras-1)
DE   (c-H-ras).
GN   Name=Hras1; Synonyms=Hras;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=87064453; PubMed=3023901;
RA   Ruta M., Wolford R., Dhar R., Defeo-Jones D., Ellis R.W.,
RA   Scolnick E.M.;
RT   "Nucleotide sequence of the two rat cellular rasH genes.";
RL   Mol. Cell. Biol. 6:1706-1710(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
RX   PubMed=3027702;
RA   Damante G., Filetti S., Rapoport B.;
RT   "Nucleotide sequence and characterization of the 5' flanking region of
RT   the rat Ha-ras protooncogene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:774-778(1987).
RN   [3]
RP   INTERACTION WITH PLCE1, AND MUTAGENESIS OF ASN-26; THR-35; GLU-37;
RP   ASP-38; TYR-40; GLN-61 AND CYS-186.
RX   MEDLINE=21099252; PubMed=11179219; DOI=10.1093/emboj/20.4.743;
RA   Kelley G.G., Reks S.E., Ondrako J.M., Smrcka A.V.;
RT   "Phospholipase C(epsilon): a novel Ras effector.";
RL   EMBO J. 20:743-754(2001).
CC   -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC       activity.
CC   -!- ENZYME REGULATION: Alternate between an inactive form bound to GDP
CC       and an active form bound to GTP. Activated by a guanine
CC       nucleotide-exchange factor (GEF) and inactivated by a GTPase-
CC       activating protein (GAP).
CC   -!- SUBUNIT: In its GTP-bound form interacts with PLCE1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; cytoplasmic
CC       side (By similarity). Golgi apparatus; Golgi apparatus membrane;
CC       lipid-anchor (By similarity). Note=Shuttles between the plasma
CC       membrane and the Golgi apparatus (By similarity).
CC   -!- PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous
CC       cycle of de- and re-palmitoylation regulates rapid exchange
CC       between plasma membrane and Golgi (By similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
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DR   EMBL; M13011; AAA42009.1; -; Genomic_DNA.
DR   EMBL; M15188; AAA42008.1; -; Genomic_DNA.
DR   PIR; A25229; A25229.
DR   HSSP; P01112; 6Q21.
DR   SMR; P20171; 1-166.
DR   GermOnline; ENSRNOG00000016611; Rattus norvegicus.
DR   Ensembl; ENSRNOG00000016611; Rattus norvegicus.
DR   RGD; 2827; Hras.
DR   InterPro; IPR003577; GTPase_Ras.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_trnsfrmng.
DR   InterPro; IPR005225; Small_GTP_bd.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00173; RAS; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
KW   Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Palmitate; Prenylation; Proto-oncogene.
FT   CHAIN         1    186       GTPase HRas.
FT                                /FTId=PRO_0000043000.
FT   PROPEP      187    189       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000043001.
FT   NP_BIND      10     17       GTP.
FT   NP_BIND      57     61       GTP.
FT   NP_BIND     116    119       GTP.
FT   REGION      166    185       Hypervariable region.
FT   MOTIF        32     40       Effector region.
FT   MOD_RES     186    186       Cysteine methyl ester (in mature form)
FT                                (By similarity).
FT   LIPID       181    181       S-palmitoyl cysteine (By similarity).
FT   LIPID       184    184       S-palmitoyl cysteine.
FT   LIPID       186    186       S-farnesyl cysteine.
FT   MUTAGEN      26     26       N->G: Interacts and partially stimulates
FT                                PLCE1; when associated with L-61.
FT   MUTAGEN      35     35       T->S: No interaction and stimulation of
FT                                PLCE1; when associated with L-61.
FT   MUTAGEN      37     37       E->G: Reduced interaction and stimulation
FT                                of PLCE1; when associated with L-61.
FT   MUTAGEN      38     38       D->N: Reduced interaction and stimulation
FT                                of PLCE1; when associated with L-61.
FT   MUTAGEN      40     40       Y->C: No interaction and stimulation of
FT                                PLCE1; when associated with L-61.
FT   MUTAGEN      61     61       Q->L: Constituvely active. Constitutively
FT                                interacts and stimulates PLCE1
FT                                phospholipase activity. Reduced
FT                                interaction and stimulation of PLCE1;
FT                                when associated with G-37 and N-38. No
FT                                interaction and stimulation of PLCE1;
FT                                when associated with S-35 and C-40.
FT                                Interacts and partially stimulates PLCE1;
FT                                when associated with G-26. Interacts but
FT                                does not stimulate PLCE1; when associated
FT                                with S-186.
FT   MUTAGEN     186    186       C->S: Interacts but does not stimulate
FT                                PLCE1; when associated with L-61.
SQ   SEQUENCE   189 AA;  21314 MW;  EE6DD9B533E2856A CRC64;
     MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
     QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI KRVKDSDDVP MVLVGNKCDL
     AARTVESRQA QDLARSYGIP YIETSAKTRQ GVEDAFYTLV REIRQHKLRK LNPPDESGLG
     CMSCKCVLS
//