RASK_MONDO
ID RASK_MONDO Reviewed; 188 AA.
AC Q07983;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 134.
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 AltName: Full=c-K-ras;
DE AltName: Full=c-Ki-ras;
DE Contains:
DE RecName: Full=GTPase KRas, N-terminally processed;
DE Flags: Precursor;
GN Name=KRAS;
OS Monodelphis domestica (Gray short-tailed opossum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX NCBI_TaxID=13616;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Eye;
RX PubMed=8312604; DOI=10.3109/10425179309015620;
RA Kusewitt D.F., Kelly G., Sabourin C.L.K., Ley R.D.;
RT "Characterization of the K-ras gene of the marsupial Monodelphis
RT domestica.";
RL DNA Seq. 4:37-42(1993).
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 (PubMed:8312604). Plays a role in promoting
CC oncogenic events by inducing transcriptional silencing of tumor
CC suppressor genes (TSGs) in colorectal cancer (CRC) cells in a ZNF304-
CC dependent manner (By similarity). {ECO:0000250|UniProtKB:P01116,
CC ECO:0000269|PubMed:8312604}.
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). Interaction with SOS1 promotes exchange of bound GDP by GTP.
CC {ECO:0000250|UniProtKB:P01116}.
CC -!- SUBUNIT: Interacts with PHLPP. Interacts (active GTP-bound form
CC preferentially) with RGS14 (By similarity). Interacts (when
CC farnesylated) with PDE6D; this promotes dissociation from the cell
CC membrane (By similarity). Interacts with SOS1 (By similarity).
CC Interacts (when farnesylated) with GPR31 (By similarity). Interacts
CC with RAP1GDS1 (By similarity). {ECO:0000250|UniProtKB:P01116,
CC ECO:0000250|UniProtKB:P08644}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01116};
CC Lipid-anchor {ECO:0000250|UniProtKB:P01116}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P01116}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P01116}.
CC -!- PTM: Acetylation at Lys-104 prevents interaction with guanine
CC nucleotide exchange factors (GEFs). {ECO:0000250|UniProtKB:P01116}.
CC -!- DISEASE: Note=Mutation which changes position 61 is implicated in
CC ultraviolet radiation-induced (UVR-induced) eye tumor.
CC {ECO:0000269|PubMed:8312604}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; Z12125; CAA78108.1; -; mRNA.
DR PIR; S31720; S31720.
DR RefSeq; NP_001028153.1; NM_001032981.2.
DR AlphaFoldDB; Q07983; -.
DR BMRB; Q07983; -.
DR SMR; Q07983; -.
DR STRING; 13616.ENSMODP00000021787; -.
DR GeneID; 554186; -.
DR KEGG; mdo:554186; -.
DR CTD; 3845; -.
DR eggNOG; KOG0395; Eukaryota.
DR InParanoid; Q07983; -.
DR OrthoDB; 1259506at2759; -.
DR Proteomes; UP000002280; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:0031647; P:regulation of protein stability; 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 Acetylation; Cell membrane; Cytoplasm; Disease variant; GTP-binding;
KW Hydrolase; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Prenylation; Proto-oncogene; Reference proteome.
FT CHAIN 1..185
FT /note="GTPase KRas"
FT /id="PRO_0000326481"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT CHAIN 2..185
FT /note="GTPase KRas, N-terminally processed"
FT /id="PRO_0000082642"
FT PROPEP 186..188
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT /id="PRO_0000281292"
FT REGION 166..185
FT /note="Hypervariable region"
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 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT MOD_RES 2
FT /note="N-acetylthreonine; in GTPase KRas, N-terminally
FT processed"
FT /evidence="ECO:0000250|UniProtKB:P01116"
FT MOD_RES 104
FT /note="N6-acetyllysine"
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 VARIANT 61
FT /note="Q -> L (in UVR-induced corneal tumor)"
SQ SEQUENCE 188 AA; 21396 MW; B1B6C319A03F29D1 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHHYREQI KRVKDSEDVP MVLVGNKCDL
PSRTVDTKQA QDLARSYGIP FIETSAKTRQ GGDDAFYTLV REIRKHKEKM SKDGKKKKKK
SKTKCIIM
