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 05-OCT-2010, entry version 88. DE RecName: Full=GTPase HRas; DE AltName: Full=H-Ras-1; DE AltName: Full=Transforming protein p21; DE AltName: Full=c-H-ras; DE AltName: Full=p21ras; DE Contains: DE RecName: Full=GTPase HRas, N-terminally processed; DE Flags: Precursor; 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; DOI=10.1073/pnas.84.3.774; 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 ISOPRENYLATION AT CYS-186, CLEAVAGE, AND METHYLATION AT CYS-186. RX MEDLINE=88263004; PubMed=3290900; DOI=10.1073/pnas.85.13.4643; RA Clarke S., Vogel J.P., Deschenes R.J., Stock J.; RT "Posttranslational modification of the Ha-ras oncogene protein: RT evidence for a third class of protein carboxyl methyltransferases."; RL Proc. Natl. Acad. Sci. U.S.A. 85:4643-4647(1988). RN [4] 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: Forms a signaling complex with RASGRP1 and DGKZ. In its CC GTP-bound form interacts with PLCE1. Interacts with TBC1D10C. CC Interacts with RGL3 and RASSF5. Interacts with HSPD1 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic CC side (By similarity). Golgi apparatus membrane; Lipid-anchor (By CC similarity). Note=Shuttles between the plasma membrane and the CC 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 -!- PTM: S-nitrosylated; critical for redox regulation. Important for CC stimulating guanine nucleotide exchange. No structural CC perturbation on nitrosylation. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family. 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; AAA42009.1; -; Genomic_DNA. DR EMBL; M15188; AAA42008.1; -; Genomic_DNA. DR IPI; IPI00196529; -. DR PIR; A25229; A25229. DR UniGene; Rn.102180; -. DR UniGene; Rn.129785; -. DR ProteinModelPortal; P20171; -. DR SMR; P20171; 1-171. DR MINT; MINT-4996514; -. DR STRING; P20171; -. DR Ensembl; ENSRNOT00000022363; ENSRNOP00000022363; ENSRNOG00000016611. DR UCSC; BC086608; rat. DR RGD; 2827; Hras. DR eggNOG; maNOG09147; -. DR HOVERGEN; HBG009351; -. DR InParanoid; P20171; -. DR PhylomeDB; P20171; -. DR Genevestigator; P20171; -. DR GermOnline; ENSRNOG00000016611; Rattus norvegicus. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005792; C:microsome; IDA:RGD. DR GO; GO:0005886; C:plasma membrane; IMP:RGD. DR GO; GO:0005625; C:soluble fraction; IDA:RGD. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0006915; P:apoptosis; IMP:RGD. DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:RGD. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:RGD. DR GO; GO:0051291; P:protein heterooligomerization; IPI:RGD. DR GO; GO:0007265; P:Ras protein signal transduction; IMP:RGD. DR GO; GO:0035176; P:social behavior; IEP:RGD. DR InterPro; IPR003577; GTPase_Ras. DR InterPro; IPR013753; Ras. DR InterPro; IPR001806; Ras_GTPase. DR InterPro; IPR015592; Ras_Ras_related. DR InterPro; IPR020849; Ras_small_GTPase. DR InterPro; IPR005225; Small_GTP-bd. DR PANTHER; PTHR11708:SF125; Ras_Ras_related; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00173; RAS; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51421; RAS; 1. PE 1: Evidence at protein level; KW Acetylation; Cell membrane; Golgi apparatus; GTP-binding; Lipoprotein; KW Membrane; Methylation; Nucleotide-binding; Palmitate; Prenylation; KW Proto-oncogene; S-nitrosylation. FT CHAIN 1 186 GTPase HRas. FT /FTId=PRO_0000043000. FT INIT_MET 1 1 Removed; alternate (By similarity). FT CHAIN 2 186 GTPase HRas, N-terminally processed. FT /FTId=PRO_0000326479. 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 1 1 N-acetylmethionine; in GTPase HRas; FT alternate (By similarity). FT MOD_RES 2 2 N-acetylthreonine; in GTPase HRas, N- FT terminally processed (By similarity). FT MOD_RES 118 118 S-nitrosocysteine (By similarity). FT MOD_RES 186 186 Cysteine methyl ester. 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: Constitutively active. FT Constitutively interacts and stimulates FT PLCE1 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 //