RASL_COPCI
ID RASL_COPCI Reviewed; 215 AA.
AC Q05058;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=24 kDa Ras-like protein;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01116};
DE Flags: Precursor;
GN Name=CC-RAS;
OS Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=5346;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 30114;
RX PubMed=8462879; DOI=10.1016/0378-1119(93)90335-z;
RA Ishibashi O., Shishido K.;
RT "Nucleotide sequence of a ras gene from the basidiomycete Coprinus
RT cinereus.";
RL Gene 125:233-234(1993).
CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC activity.
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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D13295; BAA02552.1; -; Genomic_DNA.
DR PIR; JN0562; JN0562.
DR AlphaFoldDB; Q05058; -.
DR SMR; Q05058; -.
DR VEuPathDB; FungiDB:CC1G_06445; -.
DR VEuPathDB; FungiDB:CC2G_007301; -.
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; Prenylation.
FT CHAIN 1..212
FT /note="24 kDa Ras-like protein"
FT /id="PRO_0000082703"
FT PROPEP 213..215
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281357"
FT REGION 179..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 39..47
FT /note="Effector region"
FT /evidence="ECO:0000305"
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 212
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 212
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 215 AA; 24012 MW; 37B42DA51EFFF897 CRC64;
MAARAQFLRE YKLVVVGGGG VGKSALTIQF IQSHFVDEYD PTIEDSYRKQ CIIDDEVALL
DVLDTAGQEE YGAMREQYMR TGEGFLLVYS ITSRNSFEEI SIFHQQILRV KDQDSFPVIV
VANKCDLEYE RQVGMNEGRD LAKHFGCKFI ETSAKQRINV DEAFSNLVRE IRKYNREQQT
GRPAIAAGGG GPAGSYTQDR HHDEAPGCCA GCVIA
