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Ras-like protein 1 (Ras homolog type B)

 RAS1_CANAW              Reviewed;         288 AA.
C4YKT4; Q9UQX7; Q9UVU4;
19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
28-JUL-2009, sequence version 1.
12-SEP-2018, entry version 55.
RecName: Full=Ras-like protein 1;
AltName: Full=Ras homolog type B;
Flags: Precursor;
Name=RAS1; ORFNames=CAWG_06092;
Candida albicans (strain WO-1) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=294748;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-216 INS AND
GLN-SER-251 INS, AND FUNCTION.
STRAIN=WO-1;
PubMed=11722734; DOI=10.1046/j.1365-2958.2001.02672.x;
Leberer E., Harcus D., Dignard D., Johnson L., Ushinsky S.,
Thomas D.Y., Schroeppel K.;
"Ras links cellular morphogenesis to virulence by regulation of the
MAP kinase and cAMP signalling pathways in the pathogenic fungus
Candida albicans.";
Mol. Microbiol. 42:673-687(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=WO-1;
PubMed=19465905; DOI=10.1038/nature08064;
Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L.,
Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S.,
Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J., Harris D.,
Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E.,
Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J.,
Santos M.C., Schmitzberger F.F., Sherlock G., Shah P.,
Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I.,
Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W.,
Kellis M., Cuomo C.A.;
"Evolution of pathogenicity and sexual reproduction in eight Candida
genomes.";
Nature 459:657-662(2009).
-!- FUNCTION: Required for the regulation of both a MAP kinase
signaling pathway and a cAMP signaling pathway. The activation of
these pathways contributes to the pathogenicity of the cells
through the induction of the morphological transition from the
yeast to the polarized filamentous form.
{ECO:0000269|PubMed:11722734}.
-!- ACTIVITY REGULATION: Alternates between an inactive form bound to
GDP and an active form bound to GTP. Activated by a guanine
nucleotide-exchange factor (GEF) and inactivated by a GTPase-
activating protein (GAP).
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}; Cytoplasmic side {ECO:0000305}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF134251; AAF03566.1; -; Genomic_DNA.
EMBL; AF134252; AAF03567.1; -; Genomic_DNA.
EMBL; CH672354; EEQ47513.1; -; Genomic_DNA.
ProteinModelPortal; C4YKT4; -.
SMR; C4YKT4; -.
EnsemblFungi; EEQ47513; EEQ47513; CAWG_06092.
HOGENOM; HOG000233973; -.
OMA; CLQHFVE; -.
OrthoDB; EOG092C4VY0; -.
Proteomes; UP000001429; Chromosome 2, Supercontig 1.9.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR020849; Small_GTPase_Ras-type.
PANTHER; PTHR24070; PTHR24070; 1.
Pfam; PF00071; Ras; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51421; RAS; 1.
3: Inferred from homology;
Cell membrane; Complete proteome; GTP-binding; Lipoprotein; Membrane;
Methylation; Nucleotide-binding; Palmitate; Prenylation.
CHAIN 1 285 Ras-like protein 1.
/FTId=PRO_0000413060.
PROPEP 286 288 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000413061.
NP_BIND 11 18 GTP. {ECO:0000250}.
NP_BIND 58 62 GTP. {ECO:0000250}.
NP_BIND 117 120 GTP. {ECO:0000250}.
MOTIF 33 41 Effector region.
COMPBIAS 11 16 Poly-Gly.
COMPBIAS 178 186 Poly-Gln.
COMPBIAS 212 216 Poly-Asn.
COMPBIAS 252 260 Poly-Gln.
MOD_RES 285 285 Cysteine methyl ester. {ECO:0000250}.
LIPID 284 284 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 285 285 S-farnesyl cysteine. {ECO:0000250}.
VARIANT 216 216 N -> NN (in allele A).
{ECO:0000269|PubMed:11722734}.
VARIANT 251 251 S -> SQS (in allele B).
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


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