RASN_XENLA
ID RASN_XENLA Reviewed; 189 AA.
AC Q91806; A4FVD4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=8393141; DOI=10.1128/mcb.13.8.4953-4966.1993;
RA Spevak W., Keiper B.D., Stratowa C., Castanon M.J.;
RT "Saccharomyces cerevisiae cdc15 mutants arrested at a late stage in
RT anaphase are rescued by Xenopus cDNAs encoding N-ras or a protein with
RT beta-transducin repeats.";
RL Mol. Cell. Biol. 13:4953-4966(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) 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).
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 -!- DEVELOPMENTAL STAGE: Present in fully grown and progesterone-matured
CC oocytes. The level change vera little even after zygotic gene
CC transcription begins following the mid-blastula transition. Do not
CC increase in abundance in the gastrula, neurula, tailbud, or tadpole
CC embryo. {ECO:0000269|PubMed:8393141}.
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; M97960; AAA02809.1; -; mRNA.
DR EMBL; BC133746; AAI33747.1; -; mRNA.
DR PIR; A48088; A48088.
DR RefSeq; NP_001084337.1; NM_001090868.1.
DR RefSeq; XP_018100433.1; XM_018244944.1.
DR AlphaFoldDB; Q91806; -.
DR SMR; Q91806; -.
DR MaxQB; Q91806; -.
DR DNASU; 399446; -.
DR GeneID; 399446; -.
DR KEGG; xla:399446; -.
DR CTD; 399446; -.
DR Xenbase; XB-GENE-6085929; nras.L.
DR OMA; QGCMGVS; -.
DR OrthoDB; 1259506at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 399446; Expressed in gastrula and 19 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: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..186
FT /note="GTPase NRas"
FT /id="PRO_0000043020"
FT PROPEP 187..189
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000043021"
FT REGION 166..185
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 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"
SQ SEQUENCE 189 AA; 21382 MW; 3DDD4B2739C870A0 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNSKSF ADINAYREQI KRVKDSDDVP MVLVGNKCDL
PSRTVDTKQA QELARSYGIP FIETSAKTRQ GVEDAFYTLV REIHQYRMKK LDSSEDNNQG
CIRIPCKLM
