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-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE)
DE   TRANSFORMING PROTEIN P21/H-RAS-1 (C-H-RAS).
GN   HRAS1 OR HRAS.
OS   RATTUS NORVEGICUS (RAT).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; MAMMALIA; EUTHERIA;
OC   RODENTIA; SCIUROGNATHI; MURIDAE; MURINAE; RATTUS.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 87064453.
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).
CC   -!- FUNCTION: RAS PROTEINS BIND GDP/GTP AND POSSESS INTRINSIC GTPASE
CC       ACTIVITY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
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; G206559; -.
DR   PIR; A25229; A25229.
DR   PFAM; PF00071; ras; 1.
DR   HSSP; P01112; 1AA9.
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;  1D563F20 CRC32;
     MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
     QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI KRVKDSDDVP MVLVGNKCDL
     AARTVESRQA QDLARSYGIP YIETSAKTRQ GVEDAFYTLV REIRQHKLRK LNPPDESGLG
     CMSCKCVLS
//