RAS1_CANAL
ID RAS1_CANAL Reviewed; 290 AA.
AC Q59XU5; A0A1D8PIN4;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Ras-like protein 1;
DE AltName: Full=Ras homolog type B;
DE Flags: Precursor;
GN Name=RAS1; OrderedLocusNames=CAALFM_C210210CA;
GN ORFNames=CaO19.1760, CaO19.9329;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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 -!- 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; CP017624; AOW27998.1; -; Genomic_DNA.
DR RefSeq; XP_714405.2; XM_709312.2.
DR AlphaFoldDB; Q59XU5; -.
DR SMR; Q59XU5; -.
DR BioGRID; 1227021; 3.
DR STRING; 237561.Q59XU5; -.
DR PRIDE; Q59XU5; -.
DR GeneID; 3643927; -.
DR KEGG; cal:CAALFM_C210210CA; -.
DR VEuPathDB; FungiDB:C2_10210C_A; -.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_0_1; -.
DR InParanoid; Q59XU5; -.
DR OMA; EYSPTIE; -.
DR OrthoDB; 1259506at2759; -.
DR PRO; PR:Q59XU5; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
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; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Palmitate; Prenylation; Reference proteome.
FT CHAIN 1..287
FT /note="Ras-like protein 1"
FT /id="PRO_0000413058"
FT PROPEP 288..290
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000413059"
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
