RAS_LENED
ID RAS_LENED Reviewed; 217 AA.
AC P28775;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Ras-like protein;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE Flags: Precursor;
OS Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Omphalotaceae; Lentinula.
OX NCBI_TaxID=5353;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1937010; DOI=10.1016/0378-1119(91)90517-f;
RA Hori K., Kajiwara S., Saito T., Miyazawa H., Katayose Y., Shishido K.;
RT "Cloning, sequence analysis and transcriptional expression of a ras gene of
RT the edible basidiomycete Lentinus edodes.";
RL Gene 105:91-96(1991).
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:P01112};
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).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; D00742; BAA00642.1; -; Genomic_DNA.
DR PIR; JS0619; TVWYRS.
DR AlphaFoldDB; P28775; -.
DR SMR; P28775; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Cell membrane; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Palmitate; Prenylation.
FT CHAIN 1..214
FT /note="Ras-like protein"
FT /id="PRO_0000082677"
FT PROPEP 215..217
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281332"
FT REGION 181..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 39..47
FT /note="Effector region"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 123..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 214
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 210
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 211
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 214
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 217 AA; 24007 MW; 1DB83327DC445AD6 CRC64;
MAGRTTFLRE YKLVVVGGGG VGKSALTIQF IQSHFVDEYD PTIEDSYRKQ CVIDDEVALL
DVLDTAGQEE YGAMREQYMR TGEGFLLVYS ITSRNSFEEI STFHQQILRV KDQDTFPVVV
VANKCDLEYE RQVGMNEGRD LARHFGCKFV ETSAKVRINV DQAFQDLVRE IRKYNKEQQT
TGRMMTGGGG GGPPGTYAGK DPNDEGAGGC CGGCVVL
