RASK_KRYMA
ID RASK_KRYMA Reviewed; 188 AA.
AC Q5EFX7; Q5EFX6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
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 Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Lee Y.-M., Park E.-H., Lee J.-S.;
RT "Tissue-specific alternative splicing of Ki-ras gene from the self-
RT fertilizing fish Rivulus marmoratus (Cyprinodontiformes, Rivulidae).";
RL Submitted (JAN-2005) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5EFX7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5EFX7-2; Sequence=VSP_015305, VSP_015306;
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; AY886900; AAW78851.1; -; mRNA.
DR EMBL; AY886901; AAW78852.1; -; mRNA.
DR AlphaFoldDB; Q5EFX7; -.
DR BMRB; Q5EFX7; -.
DR SMR; Q5EFX7; -.
DR STRING; 37003.ENSKMAP00000002614; -.
DR Proteomes; UP000264800; Whole Genome Shotgun 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 Alternative splicing; 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_0000082648"
FT PROPEP 186..188
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT /id="PRO_0000281298"
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"
FT VAR_SEQ 151..153
FT /note="GVD -> RVE (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_015305"
FT VAR_SEQ 165..188
FT /note="KHKEKMSKEGKKKKKKSKTKCILM -> QYRLSKISKEEKTPGCVQLKKCVV
FT M (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_015306"
SQ SEQUENCE 188 AA; 21527 MW; 58DD59FFAB219985 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHHYREQI KRVKDSEDVP MVLVGNKYDL
PTRTVDTKQA QDLARSYGIP FIETSAKTRQ GVDDAFYTLV REIRKHKEKM SKEGKKKKKK
SKTKCILM
