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 27-MAR-2024, entry version 188. 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}. 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; 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; 10116-ENSRNOP00000036381; -. DR Ensembl; ENSRNOT00000098182.1; ENSRNOP00000078755.1; ENSRNOG00000023079.4. DR Ensembl; ENSRNOT00055034226; ENSRNOP00055027750; ENSRNOG00055020029. DR Ensembl; ENSRNOT00060053066; ENSRNOP00060044116; ENSRNOG00060030547. DR Ensembl; ENSRNOT00065053199; ENSRNOP00065043696; ENSRNOG00065030867. DR GeneID; 24605; -. DR KEGG; rno:24605; -. DR UCSC; RGD:3205; rat. DR AGR; RGD:3205; -. 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; 8685at2759; -. 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 cell types or 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:0045445; P:myoblast differentiation; IEP: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 type II interferon 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 CDD; cd04138; H_N_K_Ras_like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR24070:SF189; GTPASE NRAS; 1. DR PANTHER; PTHR24070; RAS, DI-RAS, AND RHEB FAMILY MEMBERS OF SMALL GTPASE SUPERFAMILY; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 //