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Yeast-form wall Protein 1 (GPI-anchored protein 24) (Thiol-extractable peptide 1) (flocculation protein 1)

 YWP1_CANAL              Reviewed;         533 AA.
Q59Y31; A0A1D8PI92;
11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 1.
07-JUN-2017, entry version 59.
RecName: Full=Yeast-form wall Protein 1;
AltName: Full=GPI-anchored protein 24;
AltName: Full=Thiol-extractable peptide 1;
AltName: Full=flocculation protein 1;
Flags: Precursor;
Name=YWP1; Synonyms=FLO1, PGA24, TEP1;
OrderedLocusNames=CAALFM_C208590WA; ORFNames=CaO19.11101, CaO19.3618;
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=237561;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15123810; DOI=10.1073/pnas.0401648101;
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
Davis R.W., Scherer S.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
[2]
GENOME REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
Chibana H., Nantel A., Magee P.T.;
"Assembly of the Candida albicans genome into sixteen supercontigs
aligned on the eight chromosomes.";
Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
"Assembly of a phased diploid Candida albicans genome facilitates
allele-specific measurements and provides a simple model for repeat
and indel structure.";
Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
[4]
PROTEIN SEQUENCE OF 22-33, GLYCOSYLATION, DISRUPTION PHENOTYPE,
FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=15870471; DOI=10.1099/mic.0.27663-0;
Granger B.L., Flenniken M.L., Davis D.A., Mitchell A.P., Cutler J.E.;
"Yeast wall protein 1 of Candida albicans.";
Microbiology 151:1631-1644(2005).
[5]
INDUCTION.
PubMed=14555484; DOI=10.1128/EC.2.5.1018-1024.2003;
Chauhan N., Inglis D., Roman E., Pla J., Li D., Calera J.A.,
Calderone R.;
"Candida albicans response regulator gene SSK1 regulates a subset of
genes whose functions are associated with cell wall biosynthesis and
adaptation to oxidative stress.";
Eukaryot. Cell 2:1018-1024(2003).
[6]
PREDICTION OF GPI-ANCHOR.
PubMed=12845604; DOI=10.1002/yea.1007;
De Groot P.W., Hellingwerf K.J., Klis F.M.;
"Genome-wide identification of fungal GPI proteins.";
Yeast 20:781-796(2003).
[7]
INDUCTION.
PubMed=15218092; DOI=10.1091/mbc.E03-11-0782;
Doedt T., Krishnamurthy S., Bockmuhl D.P., Tebarth B., Stempel C.,
Russell C.L., Brown A.J., Ernst J.F.;
"APSES proteins regulate morphogenesis and metabolism in Candida
albicans.";
Mol. Biol. Cell 15:3167-3180(2004).
[8]
INDUCTION.
PubMed=16151249; DOI=10.1128/EC.4.9.1562-1573.2005;
Murillo L.A., Newport G., Lan C.Y., Habelitz S., Dungan J.,
Agabian N.M.;
"Genome-wide transcription profiling of the early phase of biofilm
formation by Candida albicans.";
Eukaryot. Cell 4:1562-1573(2005).
[9]
INDUCTION.
PubMed=15814841; DOI=10.1091/mbc.E05-01-0071;
Garcia-Sanchez S., Mavor A.L., Russell C.L., Argimon S., Dennison P.,
Enjalbert B., Brown A.J.;
"Global roles of Ssn6 in Tup1- and Nrg1-dependent gene regulation in
the fungal pathogen, Candida albicans.";
Mol. Biol. Cell 16:2913-2925(2005).
[10]
INDUCTION.
PubMed=16455273; DOI=10.1016/j.fgb.2005.12.002;
Castillo L., Martinez A.I., Garcera A., Garcia-Martinez J.,
Ruiz-Herrera J., Valentin E., Sentandreu R.;
"Genomic response programs of Candida albicans following protoplasting
and regeneration.";
Fungal Genet. Biol. 43:124-134(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=17905924; DOI=10.1128/EC.00285-07;
Hiller E., Heine S., Brunner H., Rupp S.;
"Candida albicans Sun41p, a putative glycosidase, is involved in
morphogenesis, cell wall biogenesis, and biofilm formation.";
Eukaryot. Cell 6:2056-2065(2007).
[12]
INDUCTION.
PubMed=18558384; DOI=10.1016/S1672-0229(08)60019-4;
Altenburg S.D., Nielsen-Preiss S.M., Hyman L.E.;
"Increased filamentous growth of Candida albicans in simulated
microgravity.";
Genomics Proteomics Bioinformatics 6:42-50(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=18712765; DOI=10.1002/pmic.200800110;
Castillo L., Calvo E., Martinez A.I., Ruiz-Herrera J., Valentin E.,
Lopez J.A., Sentandreu R.;
"A study of the Candida albicans cell wall proteome.";
Proteomics 8:3871-3881(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
INDUCTION.
PubMed=19555771; DOI=10.1016/j.fgb.2009.06.005;
Maddi A., Bowman S.M., Free S.J.;
"Trifluoromethanesulfonic acid-based proteomic analysis of cell wall
and secreted proteins of the ascomycetous fungi Neurospora crassa and
Candida albicans.";
Fungal Genet. Biol. 46:768-781(2009).
[15]
INDUCTION.
PubMed=20870877; DOI=10.1128/EC.00159-10;
Synnott J.M., Guida A., Mulhern-Haughey S., Higgins D.G., Butler G.;
"Regulation of the hypoxic response in Candida albicans.";
Eukaryot. Cell 9:1734-1746(2010).
[16]
SUBCELLULAR LOCATION, AND CLEAVAGE BY SAP9 AND SAP10.
PubMed=21097664; DOI=10.1128/EC.00210-10;
Schild L., Heyken A., de Groot P.W., Hiller E., Mock M., de Koster C.,
Horn U., Rupp S., Hube B.;
"Proteolytic cleavage of covalently linked cell wall proteins by
Candida albicans Sap9 and Sap10.";
Eukaryot. Cell 10:98-109(2011).
[17]
INDUCTION.
PubMed=21890817; DOI=10.1128/EC.05196-11;
Ganguly S., Bishop A.C., Xu W., Ghosh S., Nickerson K.W., Lanni F.,
Patton-Vogt J., Mitchell A.P.;
"Zap1 control of cell-cell signaling in Candida albicans biofilms.";
Eukaryot. Cell 10:1448-1454(2011).
[18]
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
INDUCTION.
PubMed=20864472; DOI=10.1099/mic.0.044206-0;
Sosinska G.J., de Koning L.J., de Groot P.W., Manders E.M.,
Dekker H.L., Hellingwerf K.J., de Koster C.G., Klis F.M.;
"Mass spectrometric quantification of the adaptations in the wall
proteome of Candida albicans in response to ambient pH.";
Microbiology 157:136-146(2011).
[19]
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
INDUCTION.
PubMed=21602216; DOI=10.1099/mic.0.049395-0;
Heilmann C.J., Sorgo A.G., Siliakus A.R., Dekker H.L., Brul S.,
de Koster C.G., de Koning L.J., Klis F.M.;
"Hyphal induction in the human fungal pathogen Candida albicans
reveals a characteristic wall protein profile.";
Microbiology 157:2297-2307(2011).
[20]
FUNCTION, INDUCTION, GPI-ANCHOR AT GLY-511, AND SUBCELLULAR LOCATION.
PubMed=22505336; DOI=10.1128/EC.00026-12;
Granger B.L.;
"Insight into the antiadhesive effect of yeast wall protein 1 of
Candida albicans.";
Eukaryot. Cell 11:795-805(2012).
[21]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=23243062; DOI=10.1128/EC.00278-12;
Heilmann C.J., Sorgo A.G., Mohammadi S., Sosinska G.J.,
de Koster C.G., Brul S., de Koning L.J., Klis F.M.;
"Surface stress induces a conserved cell wall stress response in the
pathogenic fungus Candida albicans.";
Eukaryot. Cell 12:254-264(2013).
[22]
INDUCTION, AND FUNCTION.
PubMed=23948468; DOI=10.1016/j.micpath.2013.07.003;
Tian J., Weng L.X., Zhang Y.Q., Wang L.H.;
"BDSF inhibits Candida albicans adherence to urinary catheters.";
Microb. Pathog. 64:33-38(2013).
[23]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=23136884; DOI=10.1111/mmi.12087;
Rohm M., Lindemann E., Hiller E., Ermert D., Lemuth K., Trkulja D.,
Sogukpinar O., Brunner H., Rupp S., Urban C.F., Sohn K.;
"A family of secreted pathogenesis-related proteins in Candida
albicans.";
Mol. Microbiol. 87:132-151(2013).
-!- FUNCTION: Cell wall protein which plays an anti-adhesive role and
promotes dispersal of yeast forms, which allows the organism to
seek new sites for colonization. {ECO:0000269|PubMed:15870471,
ECO:0000269|PubMed:22505336, ECO:0000269|PubMed:23948468}.
-!- SUBCELLULAR LOCATION: Secreted. Secreted, cell wall. Membrane
{ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. Note=In
yeast cultures, is linked covalently to glucans of the wall
matrix, but, as cultures approach stationary phase, accumulates in
the medium and is extractable from cells with disulfide-reducing
agents. Removed from the cell wall by proteolytic cleavage by SAP9
and SAP10.
-!- INDUCTION: Expression is greatest during yeast exponential-phase
growth, but down-regulated in stationary phase and upon
filamentation. Expression is also increased during growth in
hypoxic conditions. Expression decreases in biofilm cultures and
becomes undetectable through late stage biofilm formation. Up-
regulated when the extracellular phosphate concentration is low or
in presence of Cis-2-dodecenoic acid (BDSF). Repressed during cell
wall regeneration. Expression is positively regulated by EFG1 and
EFH1, and negatively regulated by SSN6 and SSK1.
{ECO:0000269|PubMed:14555484, ECO:0000269|PubMed:15218092,
ECO:0000269|PubMed:15814841, ECO:0000269|PubMed:15870471,
ECO:0000269|PubMed:16151249, ECO:0000269|PubMed:16455273,
ECO:0000269|PubMed:18558384, ECO:0000269|PubMed:19555771,
ECO:0000269|PubMed:20864472, ECO:0000269|PubMed:20870877,
ECO:0000269|PubMed:21602216, ECO:0000269|PubMed:21890817,
ECO:0000269|PubMed:22505336, ECO:0000269|PubMed:23948468}.
-!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
reticulum and serves to target the protein to the cell surface.
There, the glucosamine-inositol phospholipid moiety is cleaved off
and the GPI-modified mannoprotein is covalently attached via its
lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer
cell wall layer. {ECO:0000269|PubMed:21097664}.
-!- PTM: Cleaved by SAP9 and SAP10, which leads to its release from
the cell wall.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:15870471}.
-!- DISRUPTION PHENOTYPE: Leads to increased adhesion and biofilm
formation. {ECO:0000269|PubMed:15870471}.
-!- SIMILARITY: Belongs to the flocculin family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; CP017624; AOW27847.1; -; Genomic_DNA.
RefSeq; XP_714462.1; XM_709369.2.
ProteinModelPortal; Q59Y31; -.
PRIDE; Q59Y31; -.
GeneID; 3643915; -.
KEGG; cal:CAALFM_C208590WA; -.
CGD; CAL0000183265; YWP1.
InParanoid; Q59Y31; -.
OrthoDB; EOG092C4EDZ; -.
PRO; PR:Q59Y31; -.
Proteomes; UP000000559; Chromosome 2.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:CGD.
GO; GO:0005576; C:extracellular region; IDA:CGD.
GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
GO; GO:0044406; P:adhesion of symbiont to host; IDA:CGD.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0044010; P:single-species biofilm formation; IMP:CGD.
InterPro; IPR025928; Flocculin_t3_rpt.
Pfam; PF13928; Flocculin_t3; 3.
1: Evidence at protein level;
Cell adhesion; Cell wall; Complete proteome;
Direct protein sequencing; Glycoprotein; GPI-anchor; Lipoprotein;
Membrane; Reference proteome; Secreted; Signal.
SIGNAL 1 21 {ECO:0000269|PubMed:15870471}.
CHAIN 22 511 Yeast-form wall Protein 1.
/FTId=PRO_0000424775.
PROPEP 512 533 Removed in mature form.
/FTId=PRO_0000424776.
COMPBIAS 165 207 Ser-rich.
COMPBIAS 210 419 Thr-rich.
COMPBIAS 431 525 Ala-rich.
LIPID 511 511 GPI-anchor amidated glycine.
{ECO:0000269|PubMed:22505336}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 533 AA; 54278 MW; 257F9C08A1D0A206 CRC64;
MKVSTIFAAA SALFAATTTL AQDVACLVDN QQVAVVDLDT GVCPFTIPAS LAAFFTFVSL
EEYNVQFYYT IVNNVRYNTD IRNAGKVINV PARNLYGAGA VPFFQVHLEK QLEANSTAAI
RRRLMGETPI VKRDQIDDFI ASIENTEGTA LEGSTLEVVD YVPGSSSASP SGSASPSGSE
SGSGSDSATI RSTTVVSSSS CESSGDSAAT ATGANGESTV TEQNTVVVTI TSCHNDACHA
TTVPATASIG VTTVHGTETI FTTYCPLSSY ETVESTKVIT ITSCSENKCQ ETTVEATPST
ATTVSEGVVT EYVTYCPVSS VETVASTKVI TVVACDEHKC HETTAVATPT EVTTVVEGST
THYVTYKPTG SGPTQGETYA TNAITSEGTV YVPKTTAVTT HGSTFETVAY ITVTKATPTK
GGEQHQPGSP AGAATSAPGA PAPGASGAHA STANKVTVEA QATPGTLTPE NTVAGGVNGE
QVAVSAKTTI SQTTVAKASG SGKAAISTFE GAAAASAGAS VLALALIPLA YFI


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