RASN_CHICK
ID RASN_CHICK Reviewed; 189 AA.
AC Q5F352;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=GTPase NRas;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01116};
DE AltName: Full=Transforming protein N-Ras;
DE Flags: Precursor;
GN Name=NRAS; ORFNames=RCJMB04_34f10;
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 [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC activity. {ECO:0000250|UniProtKB:P01111}.
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:P01116};
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|UniProtKB:P01111};
CC Lipid-anchor {ECO:0000250|UniProtKB:P01111}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P01111}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P01111}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P01111}. Note=Shuttles between the plasma
CC membrane and the Golgi apparatus. {ECO:0000250|UniProtKB:P01111}.
CC -!- PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. Depalmitoylated by
CC ABHD17A, ABHD17B and ABHD17C. A continuous cycle of de- and re-
CC palmitoylation regulates rapid exchange between plasma membrane and
CC Golgi. {ECO:0000250|UniProtKB:P01111}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; AJ851798; CAH65432.1; -; mRNA.
DR RefSeq; NP_001012567.1; NM_001012549.1.
DR AlphaFoldDB; Q5F352; -.
DR SMR; Q5F352; -.
DR STRING; 9031.ENSGALP00000043468; -.
DR PaxDb; Q5F352; -.
DR Ensembl; ENSGALT00000043422; ENSGALP00000043468; ENSGALG00000026692.
DR GeneID; 419885; -.
DR KEGG; gga:419885; -.
DR CTD; 4893; -.
DR VEuPathDB; HostDB:geneid_419885; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000158947; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; Q5F352; -.
DR OMA; QGCMGVS; -.
DR OrthoDB; 1259506at2759; -.
DR PhylomeDB; Q5F352; -.
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-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-6798695; Neutrophil degranulation.
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:Q5F352; -.
DR Proteomes; UP000000539; Chromosome 26.
DR Bgee; ENSGALG00000026692; Expressed in granulocyte and 14 other tissues.
DR ExpressionAtlas; Q5F352; baseline and differential.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cell membrane; Golgi apparatus; GTP-binding; Hydrolase; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Palmitate; Prenylation;
KW Reference proteome.
FT CHAIN 1..186
FT /note="GTPase NRas"
FT /id="PRO_0000043016"
FT PROPEP 187..189
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000043017"
FT REGION 166..185
FT /note="Hypervariable region"
FT /evidence="ECO:0000250"
FT MOTIF 32..40
FT /note="Effector region"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01111"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01111"
FT LIPID 181
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P01111"
FT LIPID 186
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P01111"
SQ SEQUENCE 189 AA; 21278 MW; 52A8D86371920698 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNSKSF ADINLYREQI KRVKDSDDVP MVLVGNKCDL
PTRTVDTKQA QELAKSYGIP FIETSAKTRQ GVEDAFYTLV REIRQYRMKK LNSNEDGNQG
CMGLSCIVM
