RASN_CAVPO
ID RASN_CAVPO Reviewed; 189 AA.
AC P12825;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 168.
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 Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3029126; DOI=10.1016/s0021-9258(18)61428-0;
RA Doniger J., Notario V., Dipaolo J.A.;
RT "Carcinogens with diverse mutagenic activities initiate neoplastic guinea
RT pig cells that acquire the same N-ras point mutation.";
RL J. Biol. Chem. 262:3813-3819(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RX PubMed=3281097;
RA Doniger J.;
RT "Alternative splicing results in a truncated N-ras protein.";
RL Oncogene 2:293-294(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=2; TISSUE=Fetal fibroblast;
RX PubMed=3133626;
RA Doniger J.;
RT "Differential conservation of non-coding regions within human and guinea
RT pig N-ras genes.";
RL Oncogene 1:331-334(1987).
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 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P12825-1; Sequence=Displayed;
CC Name=2; Synonyms=Truncated;
CC IsoId=P12825-2; Sequence=VSP_005535, VSP_005536;
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; X60128; CAA42716.1; -; mRNA.
DR EMBL; M15808; AAA37050.1; -; Genomic_DNA.
DR EMBL; X60151; CAA42724.1; -; Genomic_DNA.
DR PIR; A23652; TVGPRT.
DR PIR; A26552; TVGPRS.
DR RefSeq; NP_001166369.1; NM_001172898.1. [P12825-1]
DR RefSeq; XP_005007810.1; XM_005007753.2. [P12825-1]
DR AlphaFoldDB; P12825; -.
DR SMR; P12825; -.
DR STRING; 10141.ENSCPOP00000016765; -.
DR Ensembl; ENSCPOT00000010808; ENSCPOP00000009613; ENSCPOG00000021833. [P12825-1]
DR Ensembl; ENSCPOT00000021061; ENSCPOP00000016765; ENSCPOG00000021833. [P12825-1]
DR GeneID; 100135584; -.
DR KEGG; cpoc:100135584; -.
DR CTD; 4893; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000158947; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P12825; -.
DR OMA; QGCMGVS; -.
DR OrthoDB; 1259506at2759; -.
DR TreeFam; TF312796; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000021833; Expressed in testis and 12 other tissues.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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; Alternative splicing; Cell membrane; Golgi apparatus;
KW GTP-binding; Hydrolase; Isopeptide bond; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Palmitate; Phosphoprotein; Prenylation;
KW Proto-oncogene; Reference proteome; Ubl conjugation.
FT CHAIN 1..186
FT /note="GTPase NRas"
FT /id="PRO_0000043004"
FT PROPEP 187..189
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000043005"
FT REGION 166..185
FT /note="Hypervariable region"
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"
FT VAR_SEQ 98..106
FT /note="EQIKRVKDS -> VLKMHFTHS (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005535"
FT VAR_SEQ 107..189
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005536"
SQ SEQUENCE 189 AA; 21256 MW; 52A8D3F6815B1EDD CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNSKSF ADINLYREQI KRVKDSDDVP MVLVGNKCDL
PTRTVDTKQA HELAKSYGIP FIETSAKTRQ GVEDAFYTLV REIRQYRMKK LNSNDDGTQG
CMGLPCVVM
