RASN_DANRE
ID RASN_DANRE Reviewed; 188 AA.
AC P79737;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=GTPase NRas;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01116};
DE AltName: Full=Transforming protein N-Ras;
DE AltName: Full=ZRas-B1;
DE Flags: Precursor;
GN Name=nras;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9116869;
RA Cheng R., Bradford S., Barnes D., Williams D., Hendricks J., Bailey G.;
RT "Cloning, sequencing, and embryonic expression of an N-ras proto-oncogene
RT isolated from an enriched zebrafish (Danio rerio) cDNA library.";
RL Mol. Mar. Biol. Biotechnol. 6:40-47(1997).
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; U62619; AAB40625.1; -; mRNA.
DR AlphaFoldDB; P79737; -.
DR SMR; P79737; -.
DR STRING; 7955.ENSDARP00000055741; -.
DR PaxDb; P79737; -.
DR ZFIN; ZDB-GENE-990415-166; nras.
DR eggNOG; KOG0395; Eukaryota.
DR InParanoid; P79737; -.
DR Reactome; R-DRE-1169092; Activation of RAS in B cells.
DR Reactome; R-DRE-1250347; SHC1 events in ERBB4 signaling.
DR Reactome; R-DRE-1433557; Signaling by SCF-KIT.
DR Reactome; R-DRE-171007; p38MAPK events.
DR Reactome; R-DRE-179812; GRB2 events in EGFR signaling.
DR Reactome; R-DRE-180336; SHC1 events in EGFR signaling.
DR Reactome; R-DRE-186763; Downstream signal transduction.
DR Reactome; R-DRE-1963640; GRB2 events in ERBB2 signaling.
DR Reactome; R-DRE-210993; Tie2 Signaling.
DR Reactome; R-DRE-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-DRE-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-DRE-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-DRE-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-DRE-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-DRE-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-DRE-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-DRE-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-DRE-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-DRE-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-DRE-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-DRE-5654719; SHC-mediated cascade:FGFR4.
DR Reactome; R-DRE-5658442; Regulation of RAS by GAPs.
DR Reactome; R-DRE-5673000; RAF activation.
DR Reactome; R-DRE-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DRE-5674135; MAP2K and MAPK activation.
DR Reactome; R-DRE-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR Reactome; R-DRE-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-DRE-8851805; MET activates RAS signaling.
DR Reactome; R-DRE-9634635; Estrogen-stimulated signaling through PRKCZ.
DR Reactome; R-DRE-9648002; RAS processing.
DR PRO; PR:P79737; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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: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..185
FT /note="GTPase NRas"
FT /id="PRO_0000043018"
FT PROPEP 186..188
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000043019"
FT REGION 165..184
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 180
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P01111"
FT LIPID 185
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P01111"
SQ SEQUENCE 188 AA; 21339 MW; E9FDD913CF5BCFDE CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNSKSF ADVHLYREQI KRVKDSDDVP MVLVGNICDL
ARTVDTKQAQ ELARSYGIEF VETSAKTRQG VEDAFYTLVR EIRHYRMKKL NSREDRKQGC
LGVSCEVM
