RASN_RAT
ID RASN_RAT Reviewed; 189 AA.
AC Q04970; Q4KMB1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 179.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8344525; DOI=10.1016/0378-1119(93)90362-7;
RA Carter A.T., Pearson B.M., Dickinson J.R., Lancashire W.E.;
RT "Sequence of the Escherichia coli K-12 edd and eda genes of the Entner-
RT Doudoroff pathway.";
RL Gene 130:155-156(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=8313523; DOI=10.1093/carcin/15.2.307;
RA van Kranen H.J., van Steeg H., Schoren L., Faessen P., de Vries A.,
RA van Iersel P.W., van Kreijl C.F.;
RT "The rat N-ras gene; interference of pseudogenes with the detection of
RT activating point mutations.";
RL Carcinogenesis 15:307-311(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 1-96.
RX PubMed=1714740; DOI=10.1002/mc.2940040405;
RA Fujimoto Y., Ishizaka Y., Tahira T., Sone H., Takahashi H., Enomoto K.,
RA Mori M., Sugimura T., Nagao M.;
RT "Possible involvement of c-myc but not ras genes in hepatocellular
RT carcinomas developing after spontaneous hepatitis in LEC rats.";
RL Mol. Carcinog. 4:269-274(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 8-22.
RX PubMed=2105496; DOI=10.1073/pnas.87.3.1104;
RA McMahon G., Davis E.F., Huber L.J., Kim Y., Wogan G.N.;
RT "Characterization of c-Ki-ras and N-ras oncogenes in aflatoxin B1-induced
RT rat liver tumors.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:1104-1108(1990).
RN [6]
RP INTERACTION WITH RGS14.
RX PubMed=19319189; DOI=10.1371/journal.pone.0004884;
RA Willard F.S., Willard M.D., Kimple A.J., Soundararajan M., Oestreich E.A.,
RA Li X., Sowa N.A., Kimple R.J., Doyle D.A., Der C.J., Zylka M.J.,
RA Snider W.D., Siderovski D.P.;
RT "Regulator of G-protein signaling 14 (RGS14) is a selective H-Ras
RT effector.";
RL PLoS ONE 4:E4884-E4884(2009).
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 -!- SUBUNIT: Interacts (active GTP-bound form) with RASSF7 (By similarity).
CC Interacts (active GTP-bound form preferentially) with RGS14.
CC {ECO:0000250, ECO:0000269|PubMed:19319189}.
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 -!- PTM: Acetylation at Lys-104 prevents interaction with guanine
CC nucleotide exchange factors (GEFs). {ECO:0000250|UniProtKB:P01116}.
CC -!- PTM: Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex at
CC Lys-170 in a non-degradative manner, leading to inhibit Ras signaling
CC by decreasing Ras association with membranes.
CC {ECO:0000250|UniProtKB:P01112}.
CC -!- PTM: Phosphorylation at Ser-89 by STK19 enhances NRAS-association with
CC its downstream effectors. {ECO:0000250|UniProtKB:P01111}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; X68394; CAA48460.1; -; Genomic_DNA.
DR EMBL; BC098659; AAH98659.1; -; mRNA.
DR PIR; I83212; S26621.
DR RefSeq; NP_542944.1; NM_080766.2.
DR RefSeq; XP_006233121.1; XM_006233059.2.
DR AlphaFoldDB; Q04970; -.
DR SMR; Q04970; -.
DR BioGRID; 246744; 1.
DR IntAct; Q04970; 6.
DR MINT; Q04970; -.
DR STRING; 10116.ENSRNOP00000036381; -.
DR PhosphoSitePlus; Q04970; -.
DR SwissPalm; Q04970; -.
DR jPOST; Q04970; -.
DR PaxDb; Q04970; -.
DR PRIDE; Q04970; -.
DR Ensembl; ENSRNOT00000098182; ENSRNOP00000078755; ENSRNOG00000023079.
DR GeneID; 24605; -.
DR KEGG; rno:24605; -.
DR UCSC; RGD:3205; rat.
DR CTD; 4893; -.
DR RGD; 3205; Nras.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000158947; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; Q04970; -.
DR OMA; QGCMGVS; -.
DR OrthoDB; 1259506at2759; -.
DR PhylomeDB; Q04970; -.
DR TreeFam; TF312796; -.
DR Reactome; R-RNO-1169092; Activation of RAS in B cells.
DR Reactome; R-RNO-1250347; SHC1 events in ERBB4 signaling.
DR Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR Reactome; R-RNO-171007; p38MAPK events.
DR Reactome; R-RNO-179812; GRB2 events in EGFR signaling.
DR Reactome; R-RNO-180336; SHC1 events in EGFR signaling.
DR Reactome; R-RNO-186763; Downstream signal transduction.
DR Reactome; R-RNO-1963640; GRB2 events in ERBB2 signaling.
DR Reactome; R-RNO-210993; Tie2 Signaling.
DR Reactome; R-RNO-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-RNO-2424491; DAP12 signaling.
DR Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
DR Reactome; R-RNO-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-RNO-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-RNO-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-RNO-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-RNO-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-RNO-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-RNO-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-RNO-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-RNO-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-RNO-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-RNO-5654719; SHC-mediated cascade:FGFR4.
DR Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR Reactome; R-RNO-5673000; RAF activation.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-5674135; MAP2K and MAPK activation.
DR Reactome; R-RNO-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-RNO-8851805; MET activates RAS signaling.
DR Reactome; R-RNO-9607240; FLT3 Signaling.
DR Reactome; R-RNO-9634635; Estrogen-stimulated signaling through PRKCZ.
DR Reactome; R-RNO-9648002; RAS processing.
DR PRO; PR:Q04970; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000023079; Expressed in lung and 19 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0042832; P:defense response to protozoan; ISO:RGD.
DR GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:RGD.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISO:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0042088; P:T-helper 1 type immune response; ISO:RGD.
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 Isopeptide bond; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Palmitate; Phosphoprotein; Prenylation; Proto-oncogene; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..186
FT /note="GTPase NRas"
FT /id="PRO_0000043014"
FT PROPEP 187..189
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000043015"
FT REGION 166..185
FT /note="Hypervariable region"
FT /evidence="ECO:0000250"
FT MOTIF 32..40
FT /note="Effector region"
FT BINDING 10..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01111"
FT BINDING 29..30
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 MOD_RES 89
FT /note="Phosphoserine"
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"
FT CROSSLNK 170
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P01111"
SQ SEQUENCE 189 AA; 21243 MW; 6898D3F6815B1F82 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNSKSF ADINLYREQI KRVKDSDDVP MVLVGNKCDL
PTRTVDTKQA HELAKSYGIP FIETSAKTRQ GVEDAFYTLV REIRQYRMKK LNSSEDGTQG
CMGLPCVVM
