RAS1_CANAW
ID RAS1_CANAW Reviewed; 288 AA.
AC C4YKT4; Q9UQX7; Q9UVU4;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Ras-like protein 1;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE AltName: Full=Ras homolog type B;
DE Flags: Precursor;
GN Name=RAS1; ORFNames=CAWG_06092;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-216 INS AND GLN-SER-251
RP INS, AND FUNCTION.
RC STRAIN=WO-1;
RX PubMed=11722734; DOI=10.1046/j.1365-2958.2001.02672.x;
RA Leberer E., Harcus D., Dignard D., Johnson L., Ushinsky S., Thomas D.Y.,
RA Schroeppel K.;
RT "Ras links cellular morphogenesis to virulence by regulation of the MAP
RT kinase and cAMP signalling pathways in the pathogenic fungus Candida
RT albicans.";
RL Mol. Microbiol. 42:673-687(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Required for the regulation of both a MAP kinase signaling
CC pathway and a cAMP signaling pathway. The activation of these pathways
CC contributes to the pathogenicity of the cells through the induction of
CC the morphological transition from the yeast to the polarized
CC filamentous form. {ECO:0000269|PubMed:11722734}.
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; AF134251; AAF03566.1; -; Genomic_DNA.
DR EMBL; AF134252; AAF03567.1; -; Genomic_DNA.
DR EMBL; CH672354; EEQ47513.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YKT4; -.
DR SMR; C4YKT4; -.
DR STRING; 5476.C4YKT4; -.
DR EnsemblFungi; EEQ47513; EEQ47513; CAWG_06092.
DR VEuPathDB; FungiDB:CAWG_06092; -.
DR HOGENOM; CLU_041217_9_0_1; -.
DR OMA; EYSPTIE; -.
DR PHI-base; PHI:507; -.
DR Proteomes; UP000001429; Chromosome 2, Supercontig 1.9.
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..285
FT /note="Ras-like protein 1"
FT /id="PRO_0000413060"
FT PROPEP 286..288
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000413061"
FT REGION 176..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 33..41
FT /note="Effector region"
FT BINDING 11..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 58..62
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 117..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 285
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 284
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 285
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT VARIANT 216
FT /note="N -> NN (in allele A)"
FT /evidence="ECO:0000269|PubMed:11722734"
FT VARIANT 251
FT /note="S -> SQS (in allele B)"
SQ SEQUENCE 288 AA; 32237 MW; 25A85F4B93D2DDBC CRC64;
MLREYKLVVV GGGGVGKSAL TIQLIQSHFV DEYDPTIEDS YRKQCTIDDQ QVLLDVLDTA
GQEEYSAMRE QYMRTGEGFL LVYSINSLNS FQELNSFYDQ ILRVKDSDNV PVLVVGNKCD
LEMERQVSYE DGLALANSFN CPFLETSAKQ RINVEEAFYG LVRNINQYNA KIAEAEKQQQ
QQQQQQNANQ QGQDQYGQQK DNQQSQFNNQ INNNNNTSAV NGGVSSDGII DQNGNGGVSS
GQANLPNQSQ SQRQQQQQQQ EPQQQSENQF SGQKQSSSKS KNGCCVIV
