ID   RASK_XENLA              Reviewed;         187 AA.
AC   Q05147;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=kras;
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].
RX   PubMed=2189109;
RA   Baum E.Z., Bebernitz G.A.;
RT   "K-ras oncogene expression in Xenopus laevis.";
RL   Oncogene 5:763-767(1990).
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}.
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; X53246; CAA37336.1; -; mRNA.
DR   PIR; A60192; A60192.
DR   RefSeq; NP_001095209.1; NM_001101739.1.
DR   AlphaFoldDB; Q05147; -.
DR   BMRB; Q05147; -.
DR   SMR; Q05147; -.
DR   GeneID; 373672; -.
DR   CTD; 373672; -.
DR   Proteomes; UP000186698; Genome assembly.
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:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
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..184
FT                   /note="GTPase KRas"
FT                   /id="PRO_0000082649"
FT   PROPEP          185..187
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P01116"
FT                   /id="PRO_0000281299"
FT   REGION          168..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           32..40
FT                   /note="Effector region"
FT   COMPBIAS        170..187
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         184
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:P01116"
FT   LIPID           184
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P01116"
SQ   SEQUENCE   187 AA;  21276 MW;  EF2182030BFEDC90 CRC64;
     MTEYKLVVVG AVGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
     QEEYSAMRDQ YMRTGEGFLC VFAINNIKSF EDIHHYREQI KRVKDSEDVP MVLVGNKCAL
     PSRTVDTKQA QDLARSYGIP FIETSAKTRQ GVDDAFYTLV REIRKHKEKM SKDGKKKKKS
     KTKCSIL