RASH_CHICK
ID RASH_CHICK Reviewed; 189 AA.
AC P08642;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=GTPase HRas;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
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=HRAS; Synonyms=HRAS1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF ARG-164.
RX PubMed=3011401; DOI=10.1002/j.1460-2075.1986.tb04213.x;
RA Westaway D., Papkoff J., Moskovici C., Varmus H.E.;
RT "Identification of a provirally activated c-Ha-ras oncogene in an avian
RT nephroblastoma via a novel procedure: cDNA cloning of a chimaeric viral-
RT host transcript.";
RL EMBO J. 5:301-309(1986).
CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC activity.
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:0000250|UniProtKB:P01112};
CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. Activated by a guanine nucleotide-
CC exchange factor (GEF) and inactivated by a GTPase-activating protein
CC (GAP).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Shuttles between the
CC plasma membrane and the Golgi apparatus. {ECO:0000250}.
CC -!- PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous cycle of
CC de- and re-palmitoylation regulates rapid exchange between plasma
CC membrane and Golgi. {ECO:0000250|UniProtKB:P01112}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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; X03578; CAA27258.1; -; mRNA.
DR PIR; A24617; TVCHRS.
DR RefSeq; NP_990623.1; NM_205292.1.
DR AlphaFoldDB; P08642; -.
DR BMRB; P08642; -.
DR SMR; P08642; -.
DR STRING; 9031.ENSGALP00000011140; -.
DR PaxDb; P08642; -.
DR Ensembl; ENSGALT00000053439; ENSGALP00000055362; ENSGALG00000029260.
DR Ensembl; ENSGALT00000061350; ENSGALP00000051306; ENSGALG00000029260.
DR Ensembl; ENSGALT00000079859; ENSGALP00000056118; ENSGALG00000029260.
DR Ensembl; ENSGALT00000097197; ENSGALP00000073065; ENSGALG00000029260.
DR GeneID; 396229; -.
DR KEGG; gga:396229; -.
DR CTD; 3265; -.
DR VEuPathDB; HostDB:geneid_396229; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000155653; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P08642; -.
DR OMA; HYREQIR; -.
DR OrthoDB; 1259506at2759; -.
DR PhylomeDB; P08642; -.
DR TreeFam; TF312796; -.
DR Reactome; R-GGA-1169092; Activation of RAS in B cells.
DR Reactome; R-GGA-1250347; SHC1 events in ERBB4 signaling.
DR Reactome; R-GGA-1433557; Signaling by SCF-KIT.
DR Reactome; R-GGA-171007; p38MAPK events.
DR Reactome; R-GGA-179812; GRB2 events in EGFR signaling.
DR Reactome; R-GGA-180336; SHC1 events in EGFR signaling.
DR Reactome; R-GGA-186763; Downstream signal transduction.
DR Reactome; R-GGA-1963640; GRB2 events in ERBB2 signaling.
DR Reactome; R-GGA-210993; Tie2 Signaling.
DR Reactome; R-GGA-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-GGA-2424491; DAP12 signaling.
DR Reactome; R-GGA-2871796; FCERI mediated MAPK activation.
DR Reactome; R-GGA-3928662; EPHB-mediated forward signaling.
DR Reactome; R-GGA-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-GGA-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-GGA-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-GGA-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-GGA-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-GGA-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-GGA-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-GGA-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-GGA-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-GGA-5654719; SHC-mediated cascade:FGFR4.
DR Reactome; R-GGA-5673000; RAF activation.
DR Reactome; R-GGA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-GGA-5674135; MAP2K and MAPK activation.
DR Reactome; R-GGA-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-GGA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-GGA-8851805; MET activates RAS signaling.
DR Reactome; R-GGA-9607240; FLT3 Signaling.
DR Reactome; R-GGA-9634635; Estrogen-stimulated signaling through PRKCZ.
DR Reactome; R-GGA-9648002; RAS processing.
DR PRO; PR:P08642; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000029260; Expressed in brain and 13 other tissues.
DR ExpressionAtlas; P08642; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1905360; C:GTPase complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
DR GO; GO:0090398; P:cellular senescence; IEA:Ensembl.
DR GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
DR GO; GO:2000630; P:positive regulation of miRNA metabolic process; IEA:Ensembl.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; IEA:Ensembl.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IEA:Ensembl.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0090303; P:positive regulation of wound healing; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0042088; P:T-helper 1 type immune response; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 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; Hydrolase;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Palmitate;
KW Prenylation; Proto-oncogene; Reference proteome; S-nitrosylation.
FT CHAIN 1..186
FT /note="GTPase HRas"
FT /id="PRO_0000434307"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT CHAIN 2..186
FT /note="GTPase HRas, N-terminally processed"
FT /id="PRO_0000043002"
FT PROPEP 187..189
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000043003"
FT REGION 166..185
FT /note="Hypervariable region"
FT MOTIF 32..40
FT /note="Effector region"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT MOD_RES 2
FT /note="N-acetylthreonine; in GTPase HRas, N-terminally
FT processed"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT MOD_RES 118
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT MOD_RES 186
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT LIPID 181
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT LIPID 184
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT LIPID 186
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT MUTAGEN 164
FT /note="R->A: Loss of GTP-binding activity."
FT /evidence="ECO:0000269|PubMed:3011401"
SQ SEQUENCE 189 AA; 21365 MW; 0E7BA6C929482387 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI KRVKDSDDVP MVLVGNKCDL
PARTVETRQA QDLARSYGIP YIETSAKTRQ GVEDAFYTLV REIRQHKLRK LNPPDESGPG
CMNCKCVIS
