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Cell surface mannoprotein MP65 (EC 3.2.1.-) (Mannoprotein of 65 kDa) (Soluble cell wall protein 10)

 MP65_CANAL              Reviewed;         378 AA.
Q59XX2; A0A1D8PIN3; Q59XS9;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
15-MAR-2017, sequence version 3.
22-NOV-2017, entry version 68.
RecName: Full=Cell surface mannoprotein MP65;
EC=3.2.1.-;
AltName: Full=Mannoprotein of 65 kDa;
AltName: Full=Soluble cell wall protein 10;
Flags: Precursor;
Name=MP65; Synonyms=CMP65, SCW1, SCW10;
OrderedLocusNames=CAALFM_C210030CA; ORFNames=CaO19.1779, CaO19.9345;
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 33-45, SUBCELLULAR LOCATION, GLYCOSYLATION, AND
IMMUNOLOGICAL ACTIVITY.
PubMed=8698482;
Gomez M.J., Torosantucci A., Arancia S., Maras B., Parisi L.,
Cassone A.;
"Purification and biochemical characterization of a 65-kilodalton
mannoprotein (MP65), a main target of anti-Candida cell-mediated
immune responses in humans.";
Infect. Immun. 64:2577-2584(1996).
[5]
IDENTIFICATION AS A DOMINANT ANTIGEN.
PubMed=8335981; DOI=10.1093/infdis/168.2.427;
Torosantucci A., Bromuro C., Gomez M.J., Ausiello C.M., Urbani F.,
Cassone A.;
"Identification of a 65-kDa mannoprotein as a main target of human
cell-mediated immune response to Candida albicans.";
J. Infect. Dis. 168:427-435(1993).
[6]
INDUCTION.
PubMed=7738727;
Bromuro C., Torosantucci A., Gomez M.J., Urbani F., Cassone A.;
"Differential release of an immunodominant 65 kDa mannoprotein antigen
from yeast and mycelial forms of Candida albicans.";
J. Med. Vet. Mycol. 32:447-459(1994).
[7]
IDENTIFICATION AS A DOMINANT ANTIGEN.
PubMed=11083795; DOI=10.1128/IAI.68.12.6777-6784.2000;
La Valle R., Sandini S., Gomez M.J., Mondello F., Romagnoli G.,
Nisini R., Cassone A.;
"Generation of a recombinant 65-kilodalton mannoprotein, a major
antigen target of cell-mediated immune response to Candida albicans.";
Infect. Immun. 68:6777-6784(2000).
[8]
IDENTIFICATION AS AN ANTIGEN.
PubMed=11349037; DOI=10.1128/IAI.69.6.3728-3736.2001;
Nisini R., Romagnoli G., Gomez M.J., La Valle R., Torosantucci A.,
Mariotti S., Teloni R., Cassone A.;
"Antigenic properties and processing requirements of 65-kilodalton
mannoprotein, a major antigen target of anti-Candida human T-cell
response, as disclosed by specific human T-cell clones.";
Infect. Immun. 69:3728-3736(2001).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=15302828; DOI=10.1128/EC.3.4.955-965.2004;
de Groot P.W., de Boer A.D., Cunningham J., Dekker H.L., de Jong L.,
Hellingwerf K.J., de Koster C., Klis F.M.;
"Proteomic analysis of Candida albicans cell walls reveals covalently
bound carbohydrate-active enzymes and adhesins.";
Eukaryot. Cell 3:955-965(2004).
[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]
DIAGNOSTIC TOOL.
PubMed=16616453; DOI=10.1016/j.mcp.2006.01.006;
Arancia S., Carattoli A., La Valle R., Cassone A., De Bernardis F.;
"Use of 65 kDa mannoprotein gene primers in Real Time PCR
identification of Candida albicans in biological samples.";
Mol. Cell. Probes 20:263-268(2006).
[12]
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).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17217426; DOI=10.1111/j.1462-5822.2006.00862.x;
Sandini S., La Valle R., De Bernardis F., Macri C., Cassone A.;
"The 65 kDa mannoprotein gene of Candida albicans encodes a putative
beta-glucanase adhesin required for hyphal morphogenesis and
experimental pathogenicity.";
Cell. Microbiol. 9:1223-1238(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
IDENTIFICATION IN A COMPLEX WITH PRA1 AND HYR1.
PubMed=17277107; DOI=10.4049/jimmunol.178.4.2038;
Soloviev D.A., Fonzi W.A., Sentandreu R., Pluskota E., Forsyth C.B.,
Yadav S., Plow E.F.;
"Identification of pH-regulated antigen 1 released from Candida
albicans as the major ligand for leukocyte integrin alphaMbeta2.";
J. Immunol. 178:2038-2046(2007).
[15]
IDENTIFICATION AS AN ANTIGEN.
PubMed=18591233; DOI=10.1128/IAI.00669-08;
Pietrella D., Lupo P., Rachini A., Sandini S., Ciervo A., Perito S.,
Bistoni F., Vecchiarelli A.;
"A Candida albicans mannoprotein deprived of its mannan moiety is
efficiently taken up and processed by human dendritic cells and
induces T-cell activation without stimulating proinflammatory cytokine
production.";
Infect. Immun. 76:4359-4367(2008).
[16]
SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=19098294; DOI=10.1093/jac/dkn515;
Pierce C.G., Thomas D.P., Lopez-Ribot J.L.;
"Effect of tunicamycin on Candida albicans biofilm formation and
maintenance.";
J. Antimicrob. Chemother. 63:473-479(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, AND SUBCELLULAR
LOCATION.
PubMed=21622905; DOI=10.1128/EC.05011-11;
Sorgo A.G., Heilmann C.J., Dekker H.L., Bekker M., Brul S.,
de Koster C.G., de Koning L.J., Klis F.M.;
"Effects of fluconazole on the secretome, the wall proteome, and wall
integrity of the clinical fungus Candida albicans.";
Eukaryot. Cell 10:1071-1081(2011).
-!- FUNCTION: Surface mannoprotein required for hyphal morphogenesis,
surface adherence, and pathogenicity. Contributes in a high
proportion to the carbohydrate component of the matrix due to high
levels of glycosylation and may play important roles during
biofilm development and maintenance. Acts as a major antigen
target of host cell-mediated immune response. Induces extensive T-
cell proliferation of human peripheral blood mononuclear cells.
Facilitates host dendritic cells maturation and promotes cytokine
production through its glycosylated portion while its protein core
is essentially involved in induction of T-cell response.
{ECO:0000269|PubMed:17217426}.
-!- SUBUNIT: Component of a multiprotein complex of 250 kDa composed
of at least HYR1, MP65, and PRA1. {ECO:0000269|PubMed:17277107}.
-!- SUBCELLULAR LOCATION: Secreted, cell wall
{ECO:0000269|PubMed:15302828, ECO:0000269|PubMed:17277107,
ECO:0000269|PubMed:17905924, ECO:0000269|PubMed:19098294,
ECO:0000269|PubMed:21622905, ECO:0000269|PubMed:8698482}.
-!- INDUCTION: Expressed predominantly by the mycelial cells. Also
induced during cell wall regeneration and biofilm formation.
Repressed by fluconazole. {ECO:0000269|PubMed:16455273,
ECO:0000269|PubMed:21622905, ECO:0000269|PubMed:7738727}.
-!- PTM: Glycosylated protein with a polysaccharide moiety composed
exclusively of mannose and glucose at a ratio of 12.7 to 1.
Contributes highly to the carbohydrate component of the matrix.
Treatment with tunicamycin impairs glycosylation.
{ECO:0000269|PubMed:19098294}.
-!- DISRUPTION PHENOTYPE: Impairs germ tube formation and suppresses
hyphal formation. Decreases also pathogenicity and adherence to
polystyrene plates. {ECO:0000269|PubMed:17217426}.
-!- MISCELLANEOUS: The presence of the MP65 gene can be used as a
diagnostic marker to distinguish C.albicans from other yeast or
Candida species by PCR.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CP017624; AOW27981.1; -; Genomic_DNA.
RefSeq; XP_714424.2; XM_709331.2.
SMR; Q59XX2; -.
BioGrid; 1227045; 1.
PRIDE; Q59XX2; -.
EnsemblFungi; AOW27981; AOW27981; CAALFM_C210030CA.
GeneID; 3643951; -.
KEGG; cal:CAALFM_C210030CA; -.
CGD; CAL0000177294; MP65.
OrthoDB; EOG092C20DF; -.
PRO; PR:Q59XX2; -.
Proteomes; UP000000559; Chromosome 2.
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:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; IMP:CGD.
GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IMP:CGD.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0031589; P:cell-substrate adhesion; IMP:CGD.
GO; GO:0042149; P:cellular response to glucose starvation; IMP:CGD.
GO; GO:0036244; P:cellular response to neutral pH; IMP:CGD.
GO; GO:0030447; P:filamentous growth; IMP:CGD.
GO; GO:0036178; P:filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
GO; GO:0044416; P:induction by symbiont of host defense response; IDA:CGD.
GO; GO:0009405; P:pathogenesis; IMP:CGD.
InterPro; IPR000490; Glyco_hydro_17.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF00332; Glyco_hydro_17; 1.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
1: Evidence at protein level;
Cell adhesion; Cell wall; Cell wall biogenesis/degradation;
Complete proteome; Direct protein sequencing; Glycoprotein;
Glycosidase; Hydrolase; Reference proteome; Secreted; Signal;
Virulence.
SIGNAL 1 32 {ECO:0000269|PubMed:8698482}.
CHAIN 33 378 Cell surface mannoprotein MP65.
/FTId=PRO_0000426722.
ACT_SITE 316 316 Nucleophile. {ECO:0000250}.
ACT_SITE 370 370 Proton donor. {ECO:0000250}.
SEQUENCE 378 AA; 39264 MW; 95D903DFA54C63A5 CRC64;
MLFKSFVTFT VLANALAAPL AHQHHQHKEE KRAVHVVTTT NVVVVTIGNG DQTTTFAAPS
VAAESSVSVS VNTEPPQNHP TTTQDVASAS TYPSSTDGSA ASSSAAASSS SQAGSEPSGG
VGSGGAKGIT YSPYSDNGGC KSESQIASEI AQLSGFDVIR LYGVDCSQVE AVLKAKTSSQ
KIFAGIFDVS SITSGIESLA EAVKSCGSWD DIYTVSIGNE LVNAGSATPS QIKAYVEEGR
KALKAAGYTG PVVSVDTFIA VINNPDLCDY SDYMAVNAHA FFDGHVVAEN SGAWVLQQIQ
RVWTACGGKK NVLITETGWP SRGDSNGVAV PSKSNQQAAI SSIKSSCGAS AILFTAFNDL
WKADGPYNAE KYWGIYSN


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