RASK_MELGA
ID RASK_MELGA Reviewed; 188 AA.
AC P79800;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=GTPase KRas;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01116};
DE AltName: Full=K-Ras 2;
DE AltName: Full=Ki-Ras;
DE Short=K-ras;
DE Flags: Precursor;
GN Name=KRAS;
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RX PubMed=8921837; DOI=10.1016/0378-1119(96)00250-8;
RA Chajut A., Gazit A., Yaniv A.;
RT "The turkey c-rap1A proto-oncogene is expressed via two distinct
RT promoters.";
RL Gene 177:7-10(1996).
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; X85754; CAA59755.1; -; mRNA.
DR PIR; JC5154; JC5154.
DR RefSeq; NP_001290152.1; NM_001303223.1.
DR PDB; 6XI7; X-ray; 1.95 A; A=1-169.
DR PDBsum; 6XI7; -.
DR AlphaFoldDB; P79800; -.
DR BMRB; P79800; -.
DR SMR; P79800; -.
DR PRIDE; P79800; -.
DR Ensembl; ENSMGAT00000020086; ENSMGAP00000017540; ENSMGAG00000013673.
DR GeneID; 100151750; -.
DR KEGG; mgp:100151750; -.
DR CTD; 3845; -.
DR GeneTree; ENSGT00940000155871; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P79800; -.
DR OMA; CCSGCVV; -.
DR OrthoDB; 1259506at2759; -.
DR Proteomes; UP000001645; Chromosome 1.
DR Bgee; ENSMGAG00000013673; Expressed in ileum and 17 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: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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; GTP-binding; Hydrolase;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW Reference proteome.
FT CHAIN 1..185
FT /note="GTPase KRas"
FT /id="PRO_0000082645"
FT PROPEP 186..188
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT /id="PRO_0000281295"
FT REGION 168..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"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:6XI7"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:6XI7"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:6XI7"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:6XI7"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:6XI7"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:6XI7"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:6XI7"
FT HELIX 87..104
FT /evidence="ECO:0007829|PDB:6XI7"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:6XI7"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:6XI7"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6XI7"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:6XI7"
FT HELIX 152..166
FT /evidence="ECO:0007829|PDB:6XI7"
SQ SEQUENCE 188 AA; 21453 MW; AAB6C319BB259865 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHHYREQI KRVKDSEDVP MVLVGNKCDL
PSRTVDTKQA QDLARSYGIP FIETSAKTRQ GVDDAFYTLV REIRKHKEKM SKDGKKKKKK
TKTKCIIM
