RASK_ORYLA
ID RASK_ORYLA Reviewed; 188 AA.
AC O42277;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=GTPase KRas;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01116};
DE AltName: Full=Ki-Ras;
DE Short=K-ras;
DE Flags: Precursor;
GN Name=kras1;
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Clepper L.L., Van Beneden R.J.;
RT "Cloning of two c-Ki-ras cDNA gene sequences and a putative pseudogene from
RT the medaka fish (Oryzias latipes).";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC activity (By similarity). Plays an important role in the regulation of
CC cell proliferation. {ECO:0000250|UniProtKB:P01116}.
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). {ECO:0000250|UniProtKB:P01116}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01116};
CC Lipid-anchor {ECO:0000250|UniProtKB:P01116}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P01116}. Cytoplasm
CC {ECO:0000250|UniProtKB:P01116}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; AF030545; AAB86487.1; -; mRNA.
DR RefSeq; XP_011474153.1; XM_011475851.1.
DR AlphaFoldDB; O42277; -.
DR BMRB; O42277; -.
DR SMR; O42277; -.
DR STRING; 8090.ENSORLP00000023599; -.
DR Ensembl; ENSORLT00000044860; ENSORLP00000041975; ENSORLG00000024102.
DR Ensembl; ENSORLT00015017248; ENSORLP00015010623; ENSORLG00015011467.
DR Ensembl; ENSORLT00020029220; ENSORLP00020034465; ENSORLG00020020961.
DR GeneID; 100049322; -.
DR CTD; 3845; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000155871; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; O42277; -.
DR OMA; CCSGCVV; -.
DR Proteomes; UP000001038; Chromosome 6.
DR Proteomes; UP000265180; Chromosome 6.
DR Proteomes; UP000265200; Chromosome 6.
DR Bgee; ENSORLG00000024102; Expressed in animal zygote and 14 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
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; Cytoplasm; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..185
FT /note="GTPase KRas"
FT /id="PRO_0000082647"
FT PROPEP 186..188
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT /id="PRO_0000281297"
FT REGION 167..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 32..40
FT /note="Effector region"
FT COMPBIAS 170..188
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT BINDING 29..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT BINDING 59..60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT MOD_RES 185
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT LIPID 185
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P01116"
SQ SEQUENCE 188 AA; 21451 MW; DAC1B71AA04C2DA0 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHHYREQI KRVKDSEDVP MVLVGNKCDL
PTRTVDTKQA QDLARSFGIP FIETSAKTRQ GVDDAFYTLV REIRKHKEKM SKEGKKKKKK
SKTKCILM
