ID   RASK_CYPCA              Reviewed;         188 AA.
AC   Q9YH38;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 100.
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   Cyprinus carpio (Common carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=7962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chang M.S., Chang Y., Chang G.D., Huang F.L., Huang C.-J.;
RT   "Molecular cloning and sequencing of two carp cDNAs encoding ras-related
RT   proteins.";
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC       activity. Plays an important role in the regulation of cell
CC       proliferation. May play a role in promoting oncogenic events by
CC       inducing transcriptional silencing of tumor suppressor genes (TSGs).
CC       {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; U53782; AAD10839.1; -; mRNA.
DR   RefSeq; XP_018931987.1; XM_019076442.1.
DR   AlphaFoldDB; Q9YH38; -.
DR   SMR; Q9YH38; -.
DR   Ensembl; ENSCCRT00000048906; ENSCCRP00000045106; ENSCCRG00000024099.
DR   Ensembl; ENSCCRT00015066163; ENSCCRP00015064053; ENSCCRG00015026141.
DR   Ensembl; ENSCCRT00020063392; ENSCCRP00020057501; ENSCCRG00020027247.
DR   GeneID; 109059246; -.
DR   KEGG; ccar:109059246; -.
DR   GeneTree; ENSGT00940000155871; -.
DR   OrthoDB; 1259506at2759; -.
DR   Proteomes; UP000694384; Unplaced.
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..185
FT                   /note="GTPase KRas"
FT                   /id="PRO_0000082646"
FT   PROPEP          186..188
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P01116"
FT                   /id="PRO_0000281296"
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;  21425 MW;  DED5B18DAF359860 CRC64;
     MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
     QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHHYREQI KRVKDSEDVP MVLVGNKCDL
     PSRSVDTKQA QDLARSYGIP FIETSAKTRQ GVDDAFYTLV REIRKHKEKM SKEGKKKKKK
     SKTKCVLM