RAS1_CANAX
ID RAS1_CANAX Reviewed; 290 AA.
AC P0CY32; Q9UQX7;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 41.
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;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1006;
RX PubMed=10515923; DOI=10.1128/jb.181.20.6339-6346.1999;
RA Feng Q., Summers E., Guo B., Fink G.;
RT "Ras signaling is required for serum-induced hyphal differentiation in
RT Candida albicans.";
RL J. Bacteriol. 181:6339-6346(1999).
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 (By similarity). {ECO:0000250}.
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; AF177670; AAD52662.1; -; Genomic_DNA.
DR AlphaFoldDB; P0CY32; -.
DR SMR; P0CY32; -.
DR CGD; CAL0000184093; RAS1.
DR VEuPathDB; FungiDB:C2_10210C_A; -.
DR VEuPathDB; FungiDB:CAWG_06092; -.
DR PhylomeDB; P0CY32; -.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:CGD.
DR GO; GO:0019933; P:cAMP-mediated signaling; IMP:CGD.
DR GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IMP:CGD.
DR GO; GO:0036164; P:cell-abiotic substrate adhesion; IMP:CGD.
DR GO; GO:0097308; P:cellular response to farnesol; IMP:CGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IMP:CGD.
DR GO; GO:0034605; P:cellular response to heat; IMP:CGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036171; P:filamentous growth of a population of unicellular organisms in response to chemical stimulus; IMP:CGD.
DR GO; GO:0036168; P:filamentous growth of a population of unicellular organisms in response to heat; IMP:CGD.
DR GO; GO:0030682; P:mitigation of host defenses by symbiont; IMP:CGD.
DR GO; GO:0036166; P:phenotypic switching; IMP:CGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:CGD.
DR GO; GO:1900430; P:positive regulation of filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:1900445; P:positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:1900439; P:positive regulation of filamentous growth of a population of unicellular organisms in response to chemical stimulus; IMP:CGD.
DR GO; GO:1900433; P:positive regulation of filamentous growth of a population of unicellular organisms in response to heat; IMP:CGD.
DR GO; GO:1900241; P:positive regulation of phenotypic switching; IMP:CGD.
DR GO; GO:0007265; P:Ras protein signal transduction; IGI:CGD.
DR GO; GO:1900231; P:regulation of single-species biofilm formation on inanimate substrate; IMP:CGD.
DR GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
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..287
FT /note="Ras-like protein 1"
FT /id="PRO_0000082673"
FT PROPEP 288..290
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281321"
FT REGION 176..290
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 287
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 286
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 287
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 290 AA; 32452 MW; D3268187BF61A91F 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 SQSQRQQQQQ QQEPQQQSEN QFSGQKQSSS KSKNGCCVIV
