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Hyphal wall protein 1 (Cell elongation protein 2)

 HWP1_CANAL              Reviewed;         634 AA.
P46593; A0A1D8PLV3; O13424; P87019; Q59TL7;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
15-MAR-2017, sequence version 5.
07-JUN-2017, entry version 72.
RecName: Full=Hyphal wall protein 1;
AltName: Full=Cell elongation protein 2;
Flags: Precursor;
Name=HWP1; Synonyms=ECE2; OrderedLocusNames=CAALFM_C403570WA;
ORFNames=CaO19.1321, CaO19.8901;
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 [GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=9639315;
DOI=10.1002/(SICI)1097-0061(199805)14:7<681::AID-YEA256>3.0.CO;2-8;
Staab J.F., Sundstrom P.;
"Genetic organization and sequence analysis of the hypha-specific cell
wall protein gene HWP1 of Candida albicans.";
Yeast 14:681-686(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=10464197;
Sharkey L.L., McNemar M.D., Saporito-Irwin S.M., Sypherd P.S.,
Fonzi W.A.;
"HWP1 functions in the morphological development of Candida albicans
downstream of EFG1, TUP1, and RBF1.";
J. Bacteriol. 181:5273-5279(1999).
[3]
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).
[4]
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).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-225, INDUCTION, AND SUBCELLULAR
LOCATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=8626424; DOI=10.1074/jbc.271.11.6298;
Staab J.F., Ferrer C.A., Sundstrom P.;
"Developmental expression of a tandemly repeated, proline- and
glutamine-rich amino acid motif on hyphal surfaces on Candida
albicans.";
J. Biol. Chem. 271:6298-6305(1996).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10066176; DOI=10.1126/science.283.5407.1535;
Staab J.F., Bradway S.D., Fidel P.L., Sundstrom P.;
"Adhesive and mammalian transglutaminase substrate properties of
Candida albicans Hwp1.";
Science 283:1535-1538(1999).
[8]
INDUCTION.
PubMed=10790384;
Braun B.R., Johnson A.D.;
"TUP1, CPH1 and EFG1 make independent contributions to filamentation
in Candida albicans.";
Genetics 155:57-67(2000).
[9]
INDUCTION.
PubMed=10978273;
Braun B.R., Head W.S., Wang M.X., Johnson A.D.;
"Identification and characterization of TUP1-regulated genes in
Candida albicans.";
Genetics 156:31-44(2000).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10722594; DOI=10.1128/IAI.68.4.1997-2002.2000;
Tsuchimori N., Sharkey L.L., Fonzi W.A., French S.W.,
Edwards J.E. Jr., Filler S.G.;
"Reduced virulence of HWP1-deficient mutants of Candida albicans and
their interactions with host cells.";
Infect. Immun. 68:1997-2002(2000).
[11]
INDUCTION.
PubMed=11395474; DOI=10.1128/JB.183.13.4090-4093.2001;
Leng P., Lee P.R., Wu H., Brown A.J.;
"Efg1, a morphogenetic regulator in Candida albicans, is a sequence-
specific DNA binding protein.";
J. Bacteriol. 183:4090-4093(2001).
[12]
INDUCTION.
PubMed=11259598; DOI=10.1128/MCB.21.7.2496-2505.2001;
Kadosh D., Johnson A.D.;
"Rfg1, a protein related to the Saccharomyces cerevisiae hypoxic
regulator Rox1, controls filamentous growth and virulence in Candida
albicans.";
Mol. Cell. Biol. 21:2496-2505(2001).
[13]
INDUCTION.
PubMed=11737641; DOI=10.1046/j.1365-2958.2001.02713.x;
Murad A.M., d'Enfert C., Gaillardin C., Tournu H., Tekaia F.,
Talibi D., Marechal D., Marchais V., Cottin J., Brown A.J.;
"Transcript profiling in Candida albicans reveals new cellular
functions for the transcriptional repressors CaTup1, CaMig1 and
CaNrg1.";
Mol. Microbiol. 42:981-993(2001).
[14]
INDUCTION.
PubMed=12406738; DOI=10.1128/AEM.68.11.5459-5463.2002;
Ramage G., Saville S.P., Wickes B.L., Lopez-Ribot J.L.;
"Inhibition of Candida albicans biofilm formation by farnesol, a
quorum-sensing molecule.";
Appl. Environ. Microbiol. 68:5459-5463(2002).
[15]
FUNCTION.
PubMed=12011025; DOI=10.1128/IAI.70.6.3281-3283.2002;
Sundstrom P., Cutler J.E., Staab J.F.;
"Reevaluation of the role of HWP1 in systemic candidiasis by use of
Candida albicans strains with selectable marker URA3 targeted to the
ENO1 locus.";
Infect. Immun. 70:3281-3283(2002).
[16]
PREDICTION AS A SUBSTRATE FOR KEX2 CLEAVAGE.
PubMed=12419804; DOI=10.1074/jbc.M209713200;
Newport G., Kuo A., Flattery A., Gill C., Blake J.J., Kurtz M.B.,
Abruzzo G.K., Agabian N.;
"Inactivation of Kex2p diminishes the virulence of Candida albicans.";
J. Biol. Chem. 278:1713-1720(2003).
[17]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11865405; DOI=10.1086/338836;
Sundstrom P., Balish E., Allen C.M.;
"Essential role of the Candida albicans transglutaminase substrate,
hyphal wall protein 1, in lethal oroesophageal candidiasis in
immunodeficient mice.";
J. Infect. Dis. 185:521-530(2002).
[18]
SUBCELLULAR LOCATION.
PubMed=14565982; DOI=10.1091/mbc.E03-04-0264;
Daniels K.J., Lockhart S.R., Staab J.F., Sundstrom P., Soll D.R.;
"The adhesin Hwp1 and the first daughter cell localize to the a/a
portion of the conjugation bridge during Candida albicans mating.";
Mol. Biol. Cell 14:4920-4930(2003).
[19]
GPI-ANCHOR AT GLY-613, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
GLY-613.
PubMed=14651643; DOI=10.1046/j.1365-2958.2003.03794.x;
Mao Y., Zhang Z., Wong B.;
"Use of green fluorescent protein fusions to analyse the N- and C-
terminal signal peptides of GPI-anchored cell wall proteins in Candida
albicans.";
Mol. Microbiol. 50:1617-1628(2003).
[20]
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).
[21]
INDUCTION.
PubMed=15302825; DOI=10.1128/EC.3.4.919-931.2004;
Miwa T., Takagi Y., Shinozaki M., Yun C.W., Schell W.A., Perfect J.R.,
Kumagai H., Tamaki H.;
"Gpr1, a putative G-protein-coupled receptor, regulates morphogenesis
and hypha formation in the pathogenic fungus Candida albicans.";
Eukaryot. Cell 3:919-931(2004).
[22]
FUNCTION, GLYCOSYLATION, GPI-ANCHOR, AND CELL WALL ANCHORAGE.
PubMed=15262971; DOI=10.1074/jbc.M406005200;
Staab J.F., Bahn Y.S., Tai C.H., Cook P.F., Sundstrom P.;
"Expression of transglutaminase substrate activity on Candida albicans
germ tubes through a coiled, disulfide-bonded N-terminal domain of
Hwp1 requires C-terminal glycosylphosphatidylinositol modification.";
J. Biol. Chem. 279:40737-40747(2004).
[23]
INDUCTION.
PubMed=15964282; DOI=10.1016/j.cub.2005.05.047;
Nobile C.J., Mitchell A.P.;
"Regulation of cell-surface genes and biofilm formation by the C.
albicans transcription factor Bcr1p.";
Curr. Biol. 15:1150-1155(2005).
[24]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17030992; DOI=10.1128/EC.00194-06;
Nobile C.J., Nett J.E., Andes D.R., Mitchell A.P.;
"Function of Candida albicans adhesin Hwp1 in biofilm formation.";
Eukaryot. Cell 5:1604-1610(2006).
[25]
INDUCTION.
PubMed=17042758; DOI=10.1111/j.1567-1364.2006.00130.x;
Sohn K., Senyurek I., Fertey J., Konigsdorfer A., Joffroy C.,
Hauser N., Zelt G., Brunner H., Rupp S.;
"An in vitro assay to study the transcriptional response during
adherence of Candida albicans to different human epithelia.";
FEMS Yeast Res. 6:1085-1093(2006).
[26]
FUNCTION, AND INDUCTION.
PubMed=17005778; DOI=10.1099/jmm.0.46737-0;
Naglik J.R., Fostira F., Ruprai J., Staab J.F., Challacombe S.J.,
Sundstrom P.;
"Candida albicans HWP1 gene expression and host antibody responses in
colonization and disease.";
J. Med. Microbiol. 55:1323-1327(2006).
[27]
INDUCTION.
PubMed=16427765; DOI=10.1016/j.micpath.2005.11.002;
Doyle T.C., Nawotka K.A., Purchio A.F., Akin A.R., Francis K.P.,
Contag P.R.;
"Expression of firefly luciferase in Candida albicans and its use in
the selection of stable transformants.";
Microb. Pathog. 40:69-81(2006).
[28]
INDUCTION.
PubMed=16267276; DOI=10.1091/mbc.E05-06-0502;
Cao F., Lane S., Raniga P.P., Lu Y., Zhou Z., Ramon K., Chen J.,
Liu H.;
"The Flo8 transcription factor is essential for hyphal development and
virulence in Candida albicans.";
Mol. Biol. Cell 17:295-307(2006).
[29]
FUNCTION.
PubMed=16839200; DOI=10.1371/journal.ppat.0020063;
Nobile C.J., Andes D.R., Nett J.E., Smith F.J., Yue F., Phan Q.T.,
Edwards J.E., Filler S.G., Mitchell A.P.;
"Critical role of Bcr1-dependent adhesins in C. albicans biofilm
formation in vitro and in vivo.";
PLoS Pathog. 2:E63-E63(2006).
[30]
DIAGNOSTIC TOOL.
PubMed=17448251; DOI=10.1186/1471-2180-7-35;
Lain A., Elguezabal N., Brena S., Garcia-Ruiz J.C., Del Palacio A.,
Moragues M.D., Ponton J.;
"Diagnosis of invasive candidiasis by enzyme-linked immunosorbent
assay using the N-terminal fragment of Candida albicans hyphal wall
protein 1.";
BMC Microbiol. 7:35-35(2007).
[31]
INDUCTION.
PubMed=17220463; DOI=10.1128/EC.00341-06;
Kim S., Wolyniak M.J., Staab J.F., Sundstrom P.;
"A 368-base-pair cis-acting HWP1 promoter region, HCR, of Candida
albicans confers hypha-specific gene regulation and binds
architectural transcription factors Nhp6 and Gcf1p.";
Eukaryot. Cell 6:693-709(2007).
[32]
FUNCTION, AND SUBSTRATE FOR HOST TRANSGLUTAMINASES.
PubMed=17686003; DOI=10.1111/j.1600-0714.2007.00565.x;
Ponniah G., Rollenhagen C., Bahn Y.S., Staab J.F., Sundstrom P.;
"State of differentiation defines buccal epithelial cell affinity for
cross-linking to Candida albicans Hwp1.";
J. Oral Pathol. Med. 36:456-467(2007).
[33]
INDUCTION.
PubMed=17325946; DOI=10.1080/13693780601028691;
Pendrak M.L., Roberts D.D.;
"Hemoglobin is an effective inducer of hyphal differentiation in
Candida albicans.";
Med. Mycol. 45:61-71(2007).
[34]
INDUCTION.
PubMed=17909983; DOI=10.1007/s11046-007-9068-x;
Ramage G., Wickes B.L., Lopez-Ribot J.L.;
"Inhibition on Candida albicans biofilm formation using divalent
cation chelators (EDTA).";
Mycopathologia 164:301-306(2007).
[35]
INDUCTION.
PubMed=18424510; DOI=10.1128/EC.00357-07;
Kebaara B.W., Langford M.L., Navarathna D.H., Dumitru R.,
Nickerson K.W., Atkin A.L.;
"Candida albicans Tup1 is involved in farnesol-mediated inhibition of
filamentous-growth induction.";
Eukaryot. Cell 7:980-987(2008).
[36]
SUBCELLULAR LOCATION, AND GPI-ANCHOR.
PubMed=18723603; DOI=10.1128/EC.00148-08;
Mao Y., Zhang Z., Gast C., Wong B.;
"C-terminal signals regulate targeting of
glycosylphosphatidylinositol-anchored proteins to the cell wall or
plasma membrane in Candida albicans.";
Eukaryot. Cell 7:1906-1915(2008).
[37]
FUNCTION, AND INDUCTION.
PubMed=18837169;
Nas T., Kalkanci A., Fidan I., Hizel K., Bolat S., Yolbakan S.,
Yilmaz E., Ozkan S., Kustimur S.;
"Expression of ALS1, HWP1 and SAP4 genes in Candida albicans strains
isolated from women with vaginitis.";
Folia Microbiol. (Praha) 53:179-183(2008).
[38]
FUNCTION.
PubMed=18765290; DOI=10.1016/j.fgb.2008.08.003;
Plaine A., Walker L., Da Costa G., Mora-Montes H.M., McKinnon A.,
Gow N.A., Gaillardin C., Munro C.A., Richard M.L.;
"Functional analysis of Candida albicans GPI-anchored proteins: roles
in cell wall integrity and caspofungin sensitivity.";
Fungal Genet. Biol. 45:1404-1414(2008).
[39]
GLYCOSYLATION.
PubMed=18644880; DOI=10.1128/IAI.00368-08;
Fradin C., Slomianny M.C., Mille C., Masset A., Robert R., Sendid B.,
Ernst J.F., Michalski J.C., Poulain D.;
"Beta-1,2 oligomannose adhesin epitopes are widely distributed over
the different families of Candida albicans cell wall mannoproteins and
are associated through both N- and O-glycosylation processes.";
Infect. Immun. 76:4509-4517(2008).
[40]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=18227255; DOI=10.1099/mic.0.2007/012617-0;
Sosinska G.J., de Groot P.W., Teixeira de Mattos M.J., Dekker H.L.,
de Koster C.G., Hellingwerf K.J., Klis F.M.;
"Hypoxic conditions and iron restriction affect the cell-wall proteome
of Candida albicans grown under vagina-simulative conditions.";
Microbiology 154:510-520(2008).
[41]
PRODUCTION OF VACCINES.
PubMed=18725625; DOI=10.1073/pnas.0803195105;
Xin H., Dziadek S., Bundle D.R., Cutler J.E.;
"Synthetic glycopeptide vaccines combining beta-mannan and peptide
epitopes induce protection against candidiasis.";
Proc. Natl. Acad. Sci. U.S.A. 105:13526-13531(2008).
[42]
INDUCTION.
PubMed=19652383; DOI=10.1248/bpb.32.1417;
Cheng A., Sun L., Wu X., Lou H.;
"The inhibitory effect of a macrocyclic bisbibenzyl riccardin D on the
biofilms of Candida albicans.";
Biol. Pharm. Bull. 32:1417-1421(2009).
[43]
INDUCTION.
PubMed=19734367; DOI=10.1128/EC.00190-09;
Su C., Li Y., Lu Y., Chen J.;
"Mss11, a transcriptional activator, is required for hyphal
development in Candida albicans.";
Eukaryot. Cell 8:1780-1791(2009).
[44]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19837954; DOI=10.1128/EC.00245-09;
Ene I.V., Bennett R.J.;
"Hwp1 and related adhesins contribute to both mating and biofilm
formation in Candida albicans.";
Eukaryot. Cell 8:1909-1913(2009).
[45]
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).
[46]
INDUCTION.
PubMed=20194705; DOI=10.1128/AAC.01638-09;
Vediyappan G., Rossignol T., d'Enfert C.;
"Interaction of Candida albicans biofilms with antifungals:
transcriptional response and binding of antifungals to beta-glucans.";
Antimicrob. Agents Chemother. 54:2096-2111(2010).
[47]
FUNCTION.
PubMed=20709785; DOI=10.1128/EC.00103-10;
Nobbs A.H., Vickerman M.M., Jenkinson H.F.;
"Heterologous expression of Candida albicans cell wall-associated
adhesins in Saccharomyces cerevisiae Reveals differential
specificities in adherence and biofilm formation and in binding oral
Streptococcus gordonii.";
Eukaryot. Cell 9:1622-1634(2010).
[48]
INDUCTION.
PubMed=20572249; DOI=10.1002/cbic.201000086;
Vilchez R., Lemme A., Ballhausen B., Thiel V., Schulz S., Jansen R.,
Sztajer H., Wagner-Dobler I.;
"Streptococcus mutans inhibits Candida albicans hyphal formation by
the fatty acid signaling molecule trans-2-decenoic acid (SDSF).";
ChemBioChem 11:1552-1562(2010).
[49]
INDUCTION.
PubMed=20706577; DOI=10.1371/journal.pone.0012050;
Murzyn A., Krasowska A., Stefanowicz P., Dziadkowiec D.,
Lukaszewicz M.;
"Capric acid secreted by S. boulardii inhibits C. albicans filamentous
growth, adhesion and biofilm formation.";
PLoS ONE 5:E12050-E12050(2010).
[50]
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).
[51]
INDUCTION.
PubMed=21924600; DOI=10.1016/j.phymed.2011.08.060;
Khodavandi A., Harmal N.S., Alizadeh F., Scully O.J., Sidik S.M.,
Othman F., Sekawi Z., Ng K.P., Chong P.P.;
"Comparison between allicin and fluconazole in Candida albicans
biofilm inhibition and in suppression of HWP1 gene expression.";
Phytomedicine 19:56-63(2011).
[52]
FUNCTION.
PubMed=21283544; DOI=10.1371/journal.pone.0016218;
Dwivedi P., Thompson A., Xie Z., Kashleva H., Ganguly S.,
Mitchell A.P., Dongari-Bagtzoglou A.;
"Role of Bcr1-activated genes Hwp1 and Hyr1 in Candida albicans oral
mucosal biofilms and neutrophil evasion.";
PLoS ONE 6:E16218-E16218(2011).
[53]
INDUCTION.
PubMed=23226409; DOI=10.1371/journal.pone.0050866;
Tsang P.W., Bandara H.M., Fong W.P.;
"Purpurin suppresses Candida albicans biofilm formation and hyphal
development.";
PLoS ONE 7:E50866-E50866(2012).
[54]
INDUCTION.
PubMed=23229567; DOI=10.1007/s00253-012-4549-3;
Lee S.H., Jeon J.E., Ahn C.H., Chung S.C., Shin J., Oh K.B.;
"Inhibition of yeast-to-hypha transition in Candida albicans by
phorbasin H isolated from Phorbas sp.";
Appl. Microbiol. Biotechnol. 97:3141-3148(2013).
[55]
INDUCTION.
PubMed=23262131; DOI=10.1016/j.jbiotec.2012.12.004;
Heintz-Buschart A., Eickhoff H., Hohn E., Bilitewski U.;
"Identification of inhibitors of yeast-to-hyphae transition in Candida
albicans by a reporter screening assay.";
J. Biotechnol. 164:137-142(2013).
[56]
INDUCTION.
PubMed=23210679; DOI=10.3109/13693786.2012.743051;
Hsu C.C., Lai W.L., Chuang K.C., Lee M.H., Tsai Y.C.;
"The inhibitory activity of linalool against the filamentous growth
and biofilm formation in Candida albicans.";
Med. Mycol. 51:473-482(2013).
[57]
INDUCTION.
PubMed=24252340; DOI=10.1016/j.phymed.2013.10.028;
Khan A., Ahmad A., Xess I., Khan L.A., Manzoor N.;
"Ocimum sanctum essential oil inhibits virulence attributes in Candida
albicans.";
Phytomedicine 21:448-452(2014).
[58]
INDUCTION.
PubMed=23704884; DOI=10.1371/journal.pone.0062902;
Samaranayake Y.H., Cheung B.P., Yau J.Y., Yeung S.K.,
Samaranayake L.P.;
"Human serum promotes Candida albicans biofilm growth and virulence
gene expression on silicone biomaterial.";
PLoS ONE 8:E62902-E62902(2013).
[59]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=24260489; DOI=10.1371/journal.pone.0080842;
Staab J.F., Datta K., Rhee P.;
"Niche-specific requirement for hyphal wall protein 1 in virulence of
Candida albicans.";
PLoS ONE 8:E80842-E80842(2013).
[60]
INDUCTION.
PubMed=23904484; DOI=10.1073/pnas.1305982110;
Fazly A., Jain C., Dehner A.C., Issi L., Lilly E.A., Ali A., Cao H.,
Fidel P.L. Jr., Rao R.P., Kaufman P.D.;
"Chemical screening identifies filastatin, a small molecule inhibitor
of Candida albicans adhesion, morphogenesis, and pathogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 110:13594-13599(2013).
-!- FUNCTION: Major hyphal cell wall protein which plays a role of
adhesin and is required for mating, normal hyphal development,
cell-to-cell adhesive functions necessary for biofilm integrity,
attachment to host, and virulence. Promotes interactions with host
and bacterial molecules, thus leading to effective colonization
within polymicrobial communities. Plays a crucial role in
gastrointestinal colonization, in mucosal symptomatic and
asymptomatic infections, in vaginitis, as well as in lethal
oroesophageal candidiasis, caused by the combined action of fungal
virulence factors and host inflammatory responses when protective
immunity is absent. {ECO:0000269|PubMed:10066176,
ECO:0000269|PubMed:10464197, ECO:0000269|PubMed:10722594,
ECO:0000269|PubMed:11865405, ECO:0000269|PubMed:12011025,
ECO:0000269|PubMed:15262971, ECO:0000269|PubMed:16839200,
ECO:0000269|PubMed:17005778, ECO:0000269|PubMed:17030992,
ECO:0000269|PubMed:17686003, ECO:0000269|PubMed:18765290,
ECO:0000269|PubMed:18837169, ECO:0000269|PubMed:19837954,
ECO:0000269|PubMed:20709785, ECO:0000269|PubMed:21283544,
ECO:0000269|PubMed:24260489}.
-!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor,
GPI-anchor. Note=Hyphal surface. Localizes to the a/a Portion of
the conjugation bridge during mating.
-!- DEVELOPMENTAL STAGE: Found in hyphal but not yeast forms.
-!- INDUCTION: The promoter contains a 368 bp region, the HWP1 control
region (HCR), which is target of transcription factors and is
critical for activation under hypha-inducing conditions.
Expression is positively regulated by BCR1, EFG1, FLO8, GPA2,
GPR1, MSS11, RBF1, and RFG1; and negatively regulated by NRG1 and
TUP1. Transcription is induced in an adhesion-dependent manner and
in presence of human serum or hemoglobin. Expression is down-
regulated by hypoxic conditions, allicine, ethylenediaminetetra-
acetic acid (EDTA), farnesol, linalool, riccardin D, purpurin,
filastatin, phorbasin H, Ocimum sanctum essential oil (OSEO), as
well as many substances belonging to chemical classes such as
methyl aryl-oxazoline carboxylates, dihydrobenzo-d-isoxazolones,
and thiazolo-4,5-e-benzoisoxazoles. Moreover, the competitors
Saccharomyces boulardii or Streptococcus mutans secrete
respectively capric acid and trans-2-decenoic acid (SDSF) which
also suppress HWP1 expression. {ECO:0000269|PubMed:10464197,
ECO:0000269|PubMed:10790384, ECO:0000269|PubMed:10978273,
ECO:0000269|PubMed:11259598, ECO:0000269|PubMed:11395474,
ECO:0000269|PubMed:11737641, ECO:0000269|PubMed:12406738,
ECO:0000269|PubMed:15302825, ECO:0000269|PubMed:15964282,
ECO:0000269|PubMed:16267276, ECO:0000269|PubMed:16427765,
ECO:0000269|PubMed:17005778, ECO:0000269|PubMed:17042758,
ECO:0000269|PubMed:17220463, ECO:0000269|PubMed:17325946,
ECO:0000269|PubMed:17909983, ECO:0000269|PubMed:18227255,
ECO:0000269|PubMed:18424510, ECO:0000269|PubMed:18837169,
ECO:0000269|PubMed:19555771, ECO:0000269|PubMed:19652383,
ECO:0000269|PubMed:19734367, ECO:0000269|PubMed:20194705,
ECO:0000269|PubMed:20572249, ECO:0000269|PubMed:20706577,
ECO:0000269|PubMed:20864472, ECO:0000269|PubMed:21924600,
ECO:0000269|PubMed:23210679, ECO:0000269|PubMed:23226409,
ECO:0000269|PubMed:23229567, ECO:0000269|PubMed:23262131,
ECO:0000269|PubMed:23704884, ECO:0000269|PubMed:23904484,
ECO:0000269|PubMed:24252340, ECO:0000269|PubMed:8626424}.
-!- 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.
-!- PTM: Serves as a substrate for mammalian transglutaminases which
are necessary for cross-linking between HWP1 and host epithelial
cells. Also predicted to be a substrate for cleavage by KEX2.
-!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:15262971,
ECO:0000269|PubMed:18644880}.
-!- DISRUPTION PHENOTYPE: Reduces the overall mating frequency in both
liquid and solid media. Impairs stable attachments to human buccal
epithelial cells and reduces capacity to cause systemic
candidiasis in mice. Produces a thin biofilm that lacks much of
the hyphal mass found in the wild type cell.
{ECO:0000269|PubMed:10066176, ECO:0000269|PubMed:10722594,
ECO:0000269|PubMed:11865405, ECO:0000269|PubMed:17030992,
ECO:0000269|PubMed:19837954, ECO:0000269|PubMed:24260489}.
-!- MISCELLANEOUS: As a major cell surface protein expressed during
infection, HWP1 detection can be used for diagnosis of invasive
candidiasis. HWP1 epitopes can also be used to develop vaccines
for protection against candidiasis.
-!- SIMILARITY: Belongs to the HWP1 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U64206; AAC96368.1; -; Genomic_DNA.
EMBL; AF001978; AAB64014.1; -; Genomic_DNA.
EMBL; CP017626; AOW29115.1; -; Genomic_DNA.
EMBL; U29369; AAC49209.1; -; mRNA.
RefSeq; XP_709961.2; XM_704869.2.
PRIDE; P46593; -.
GeneID; 3645372; -.
KEGG; cal:CAALFM_C403570WA; -.
CGD; CAL0000200504; HWP1.
InParanoid; P46593; -.
OrthoDB; EOG092C4VN7; -.
PRO; PR:P46593; -.
Proteomes; UP000000559; Chromosome 4.
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; IEA:UniProtKB-KW.
GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
GO; GO:0005937; C:mating projection; IDA:CGD.
GO; GO:0050839; F:cell adhesion molecule binding; IMP:CGD.
GO; GO:0044406; P:adhesion of symbiont to host; IMP:CGD.
GO; GO:0007155; P:cell adhesion; IMP:CGD.
GO; GO:0043708; P:cell adhesion involved in biofilm formation; IMP:CGD.
GO; GO:0043707; P:cell adhesion involved in single-species biofilm formation in or on host organism; IMP:CGD.
GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
GO; GO:0044117; P:growth of symbiont in host; IMP:CGD.
GO; GO:0009405; P:pathogenesis; IMP:CGD.
GO; GO:0016337; P:single organismal cell-cell adhesion; IMP:CGD.
GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IGI:CGD.
InterPro; IPR025928; Flocculin_t3_rpt.
Pfam; PF13928; Flocculin_t3; 2.
1: Evidence at protein level;
Cell adhesion; Cell wall; Complete proteome; Glycoprotein; GPI-anchor;
Lipoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal;
Virulence.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 613 Hyphal wall protein 1.
/FTId=PRO_0000084097.
PROPEP 614 634 Removed in mature form.
/FTId=PRO_0000425596.
REPEAT 46 58 1; approximate.
REPEAT 59 69 2; approximate.
REPEAT 70 81 3; approximate.
REPEAT 82 91 4.
REPEAT 92 101 5.
REPEAT 102 111 6.
REPEAT 112 121 7.
REPEAT 122 131 8.
REPEAT 132 141 9.
REPEAT 142 151 10.
REPEAT 152 161 11.
REPEAT 162 171 12.
REPEAT 172 179 13; truncated.
REPEAT 180 187 14; truncated.
REGION 46 187 14 X 10 AA tandem repeats of [EVIQ]-P-
[CDT]-D-[YNW]-P-[PQ]-[QI]-[QP]-[QDN].
COMPBIAS 53 58 Poly-Gln.
COMPBIAS 65 69 Poly-Gln.
COMPBIAS 204 207 Poly-Thr.
COMPBIAS 208 220 Poly-Ser.
COMPBIAS 291 294 Poly-Thr.
COMPBIAS 304 307 Poly-Thr.
COMPBIAS 398 401 Poly-Val.
LIPID 613 613 GPI-anchor amidated glycine.
{ECO:0000269|PubMed:14651643}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 286 286 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 601 601 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 613 613 G->D,N,S: Still allows localization to
the cell surface.
{ECO:0000269|PubMed:14651643}.
MUTAGEN 613 613 G->E,Q,R,T: Impairs cell surface
localization and localizes exclusively to
internal ER-like structures.
{ECO:0000269|PubMed:14651643}.
CONFLICT 142 142 V -> I (in Ref. 1; AAC96368 and 2;
AAB64014). {ECO:0000305}.
CONFLICT 142 142 V -> VPCDNPPQPDI (in Ref. 6; AAC49209).
{ECO:0000305}.
CONFLICT 152 152 V -> I (in Ref. 1; AAC96368, 2; AAB64014
and 6; AAC49209). {ECO:0000305}.
CONFLICT 296 296 A -> T (in Ref. 1; AAC96368).
{ECO:0000305}.
CONFLICT 441 441 P -> S (in Ref. 1; AAC96368).
{ECO:0000305}.
CONFLICT 492 492 S -> P (in Ref. 1; AAC96368).
{ECO:0000305}.
SEQUENCE 634 AA; 65314 MW; D48F1FD5C659EAC1 CRC64;
MRLSTAQLIA IAYYMLSIGA TVPQVDGQGE TEEALIQKRS YDYYQEPCDD YPQQQQQQEP
CDYPQQQQQE EPCDYPQQQP QEPCDYPQQP QEPCDYPQQP QEPCDYPQQP QEPCDNPPQP
DVPCDNPPQP DVPCDNPPQP DVPCDNPPQP DVPCDNPPQP DQPDDNPPIP NIPTDWIPNI
PTDWIPDIPE KPTTPATTPN IPATTTTSES SSSSSSSSSS TTPKTSASTT PESSVPATTP
NTSVPTTSSE STTPATSPES SVPVTSGSSI LATTSESSSA PATTPNTSVP TTTTEAKSSS
TPLTTTTEHD TTVVTVTSCS NSVCTESEVT TGVIVITSKD TIYTTYCPLT ETTPVSTAPA
TETPTGTVST STEQSTTVIT VTSCSESSCT ESEVTTGVVV VTSEETVYTT FCPLTENTPG
TDSTPEASIP PMETIPAGSE PSMPAGETSP AVPKSDVPAT ESAPVPEMTP AGSQPSIPAG
ETSPAVPKSD VSATESAPAP EMTPAGTETK PAAPKSSAPA TEPSPVAPGT ESAPAGPGAS
SSPKSSVLAS ETSPIAPGAE TAPAGSSGAI TIPESSAVVS TTEGAIPTTL ESVPLMQPSA
NYSSVAPIST FEGAGNNMRL TFGAAIIGIA AFLI


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