ID   RASH_RAT       STANDARD;      PRT;   189 AA.
AC   P20171;
DT   01-FEB-1991 (REL. 17, CREATED)
DT   01-FEB-1991 (REL. 17, LAST SEQUENCE UPDATE)
DT   01-FEB-1994 (REL. 28, LAST ANNOTATION UPDATE)
DE   TRANSFORMING PROTEIN P21/H-RAS-1.
OS   RATTUS NORVEGICUS (RAT).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; RODENTIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RM   87064453
RA   RUTA M., WOLFORD R., DHAR R., DEFEO-JONES D., ELLIS R.W.,
RA   SCOLNICK E.M.;
RL   MOL. CELL. BIOL. 6:1706-1710(1986).
CC   -!- FUNCTION: RAS PROTEINS BIND GDP/GTP AND POSSESS INTRINSIC GTPASE
CC       ACTIVITY.
CC   -!- THE MAMMALIAN RAS GENE FAMILY CONSISTS OF THE HARVEY AND KIRSTEN
CC       RAS GENES (C-HRAS1 AND C-KRAS2), AN INACTIVE PSEUDOGENE OF
CC       EACH (C-HRAS2 AND C-KRAS1) AND THE N-RAS GENE.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M13011; RNRASH1C.
DR   PIR; A25229; A25229.
DR   HSSP; P01112; 1Q21.
KW   PROTO-ONCOGENE; GTP-BINDING; PRENYLATION; LIPOPROTEIN.
FT   NP_BIND      10     17       GTP.
FT   NP_BIND      57     61       GTP.
FT   NP_BIND     116    119       GTP.
FT   DOMAIN       32     40       EFFECTOR REGION.
FT   DOMAIN      166    185       HYPERVARIABLE REGION.
FT   LIPID       184    184       PALMITATE.
FT   LIPID       186    186       FARNESYL.
SQ   SEQUENCE   189 AA;  21314 MW;  176948 CN;
     MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
     QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI KRVKDSDDVP MVLVGNKCDL
     AARTVESRQA QDLARSYGIP YIETSAKTRQ GVEDAFYTLV REIRQHKLRK LNPPDESGLG
     CMSCKCVLS
//