RASN_PIG
ID RASN_PIG Reviewed; 189 AA.
AC Q2MJK3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 126.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RA Xie H.T., Xiong Y.Z., Lei M.G., Xu D.Q.;
RT "Isolation, sequence analysis and expression profile of a novel swine
RT gene.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (active GTP-bound form preferentially) with RGS14.
CC Interacts (active GTP-bound form) with RASSF7 (By similarity).
CC {ECO:0000250}.
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; DQ325522; ABC55723.1; -; mRNA.
DR RefSeq; NP_001038002.1; NM_001044537.1.
DR AlphaFoldDB; Q2MJK3; -.
DR SMR; Q2MJK3; -.
DR STRING; 9823.ENSSSCP00000007203; -.
DR PaxDb; Q2MJK3; -.
DR PeptideAtlas; Q2MJK3; -.
DR PRIDE; Q2MJK3; -.
DR Ensembl; ENSSSCT00000038488; ENSSSCP00000046185; ENSSSCG00000032477.
DR Ensembl; ENSSSCT00005016701; ENSSSCP00005009969; ENSSSCG00005010802.
DR Ensembl; ENSSSCT00015088424; ENSSSCP00015036059; ENSSSCG00015065826.
DR Ensembl; ENSSSCT00025020871; ENSSSCP00025008582; ENSSSCG00025015558.
DR Ensembl; ENSSSCT00030071584; ENSSSCP00030032626; ENSSSCG00030051390.
DR Ensembl; ENSSSCT00035052241; ENSSSCP00035021001; ENSSSCG00035039325.
DR Ensembl; ENSSSCT00040026984; ENSSSCP00040011402; ENSSSCG00040019987.
DR Ensembl; ENSSSCT00045016798; ENSSSCP00045011590; ENSSSCG00045009917.
DR Ensembl; ENSSSCT00050054942; ENSSSCP00050023236; ENSSSCG00050040592.
DR Ensembl; ENSSSCT00055024396; ENSSSCP00055019361; ENSSSCG00055012395.
DR Ensembl; ENSSSCT00060096238; ENSSSCP00060041641; ENSSSCG00060070493.
DR Ensembl; ENSSSCT00065040494; ENSSSCP00065017119; ENSSSCG00065029998.
DR Ensembl; ENSSSCT00070009201; ENSSSCP00070007551; ENSSSCG00070004868.
DR GeneID; 100739349; -.
DR KEGG; ssc:100739349; -.
DR CTD; 4893; -.
DR VGNC; VGNC:98827; NRAS.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000158947; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; Q2MJK3; -.
DR OMA; QGCMGVS; -.
DR OrthoDB; 1259506at2759; -.
DR TreeFam; TF312796; -.
DR Reactome; R-SSC-1169092; Activation of RAS in B cells.
DR Reactome; R-SSC-1250347; SHC1 events in ERBB4 signaling.
DR Reactome; R-SSC-1433557; Signaling by SCF-KIT.
DR Reactome; R-SSC-171007; p38MAPK events.
DR Reactome; R-SSC-179812; GRB2 events in EGFR signaling.
DR Reactome; R-SSC-180336; SHC1 events in EGFR signaling.
DR Reactome; R-SSC-186763; Downstream signal transduction.
DR Reactome; R-SSC-1963640; GRB2 events in ERBB2 signaling.
DR Reactome; R-SSC-210993; Tie2 Signaling.
DR Reactome; R-SSC-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-SSC-2424491; DAP12 signaling.
DR Reactome; R-SSC-2871796; FCERI mediated MAPK activation.
DR Reactome; R-SSC-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-SSC-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-SSC-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-SSC-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-SSC-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-SSC-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-SSC-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-SSC-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-SSC-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-SSC-5654719; SHC-mediated cascade:FGFR4.
DR Reactome; R-SSC-5658442; Regulation of RAS by GAPs.
DR Reactome; R-SSC-5673000; RAF activation.
DR Reactome; R-SSC-5673001; RAF/MAP kinase cascade.
DR Reactome; R-SSC-5674135; MAP2K and MAPK activation.
DR Reactome; R-SSC-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR Reactome; R-SSC-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-SSC-8851805; MET activates RAS signaling.
DR Reactome; R-SSC-9607240; FLT3 Signaling.
DR Reactome; R-SSC-9634635; Estrogen-stimulated signaling through PRKCZ.
DR Reactome; R-SSC-9648002; RAS processing.
DR Proteomes; UP000008227; Chromosome 4.
DR Proteomes; UP000314985; Chromosome 4.
DR Bgee; ENSSSCG00000032477; Expressed in penis and 45 other tissues.
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 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_0000261123"
FT PROPEP 187..189
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000261124"
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; 21229 MW; 6898D3F6815B1EC7 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNSKSF ADINLYREQI KRVKDSDDVP MVLVGNKCDL
PTRTVDTKQA HELAKSYGIP FIETSAKTRQ GVEDAFYTLV REIRQYRMKK LNSSDDGTQG
CMGLPCVVM
