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 27-MAR-2024, entry version 134. 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}. 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; U62619; AAB40625.1; -; mRNA. DR AlphaFoldDB; P79737; -. DR SMR; P79737; -. DR STRING; 7955.ENSDARP00000055741; -. DR PaxDb; 7955-ENSDARP00000055741; -. DR AGR; ZFIN:ZDB-GENE-990415-166; -. 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 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 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 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 //