MP65_CANAL
ID MP65_CANAL Reviewed; 378 AA.
AC Q59XX2; A0A1D8PIN3; Q59XS9;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Cell surface mannoprotein MP65;
DE EC=3.2.1.-;
DE AltName: Full=Mannoprotein of 65 kDa;
DE AltName: Full=Soluble cell wall protein 10;
DE Flags: Precursor;
GN Name=MP65; Synonyms=CMP65, SCW1, SCW10; OrderedLocusNames=CAALFM_C210030CA;
GN ORFNames=CaO19.1779, CaO19.9345;
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).
RN [4]
RP PROTEIN SEQUENCE OF 33-45, SUBCELLULAR LOCATION, GLYCOSYLATION, AND
RP IMMUNOLOGICAL ACTIVITY.
RX PubMed=8698482; DOI=10.1128/iai.64.7.2577-2584.1996;
RA Gomez M.J., Torosantucci A., Arancia S., Maras B., Parisi L., Cassone A.;
RT "Purification and biochemical characterization of a 65-kilodalton
RT mannoprotein (MP65), a main target of anti-Candida cell-mediated immune
RT responses in humans.";
RL Infect. Immun. 64:2577-2584(1996).
RN [5]
RP IDENTIFICATION AS A DOMINANT ANTIGEN.
RX PubMed=8335981; DOI=10.1093/infdis/168.2.427;
RA Torosantucci A., Bromuro C., Gomez M.J., Ausiello C.M., Urbani F.,
RA Cassone A.;
RT "Identification of a 65-kDa mannoprotein as a main target of human cell-
RT mediated immune response to Candida albicans.";
RL J. Infect. Dis. 168:427-435(1993).
RN [6]
RP INDUCTION.
RX PubMed=7738727; DOI=10.1080/02681219480000601;
RA Bromuro C., Torosantucci A., Gomez M.J., Urbani F., Cassone A.;
RT "Differential release of an immunodominant 65 kDa mannoprotein antigen from
RT yeast and mycelial forms of Candida albicans.";
RL J. Med. Vet. Mycol. 32:447-459(1994).
RN [7]
RP IDENTIFICATION AS A DOMINANT ANTIGEN.
RX PubMed=11083795; DOI=10.1128/iai.68.12.6777-6784.2000;
RA La Valle R., Sandini S., Gomez M.J., Mondello F., Romagnoli G., Nisini R.,
RA Cassone A.;
RT "Generation of a recombinant 65-kilodalton mannoprotein, a major antigen
RT target of cell-mediated immune response to Candida albicans.";
RL Infect. Immun. 68:6777-6784(2000).
RN [8]
RP IDENTIFICATION AS AN ANTIGEN.
RX PubMed=11349037; DOI=10.1128/iai.69.6.3728-3736.2001;
RA Nisini R., Romagnoli G., Gomez M.J., La Valle R., Torosantucci A.,
RA Mariotti S., Teloni R., Cassone A.;
RT "Antigenic properties and processing requirements of 65-kilodalton
RT mannoprotein, a major antigen target of anti-Candida human T-cell response,
RT as disclosed by specific human T-cell clones.";
RL Infect. Immun. 69:3728-3736(2001).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=15302828; DOI=10.1128/ec.3.4.955-965.2004;
RA de Groot P.W., de Boer A.D., Cunningham J., Dekker H.L., de Jong L.,
RA Hellingwerf K.J., de Koster C., Klis F.M.;
RT "Proteomic analysis of Candida albicans cell walls reveals covalently bound
RT carbohydrate-active enzymes and adhesins.";
RL Eukaryot. Cell 3:955-965(2004).
RN [10]
RP INDUCTION.
RX PubMed=16455273; DOI=10.1016/j.fgb.2005.12.002;
RA Castillo L., Martinez A.I., Garcera A., Garcia-Martinez J.,
RA Ruiz-Herrera J., Valentin E., Sentandreu R.;
RT "Genomic response programs of Candida albicans following protoplasting and
RT regeneration.";
RL Fungal Genet. Biol. 43:124-134(2006).
RN [11]
RP DIAGNOSTIC TOOL.
RX PubMed=16616453; DOI=10.1016/j.mcp.2006.01.006;
RA Arancia S., Carattoli A., La Valle R., Cassone A., De Bernardis F.;
RT "Use of 65 kDa mannoprotein gene primers in Real Time PCR identification of
RT Candida albicans in biological samples.";
RL Mol. Cell. Probes 20:263-268(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17905924; DOI=10.1128/ec.00285-07;
RA Hiller E., Heine S., Brunner H., Rupp S.;
RT "Candida albicans Sun41p, a putative glycosidase, is involved in
RT morphogenesis, cell wall biogenesis, and biofilm formation.";
RL Eukaryot. Cell 6:2056-2065(2007).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17217426; DOI=10.1111/j.1462-5822.2006.00862.x;
RA Sandini S., La Valle R., De Bernardis F., Macri C., Cassone A.;
RT "The 65 kDa mannoprotein gene of Candida albicans encodes a putative beta-
RT glucanase adhesin required for hyphal morphogenesis and experimental
RT pathogenicity.";
RL Cell. Microbiol. 9:1223-1238(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION IN A COMPLEX WITH PRA1 AND HYR1.
RX PubMed=17277107; DOI=10.4049/jimmunol.178.4.2038;
RA Soloviev D.A., Fonzi W.A., Sentandreu R., Pluskota E., Forsyth C.B.,
RA Yadav S., Plow E.F.;
RT "Identification of pH-regulated antigen 1 released from Candida albicans as
RT the major ligand for leukocyte integrin alphaMbeta2.";
RL J. Immunol. 178:2038-2046(2007).
RN [15]
RP IDENTIFICATION AS AN ANTIGEN.
RX PubMed=18591233; DOI=10.1128/iai.00669-08;
RA Pietrella D., Lupo P., Rachini A., Sandini S., Ciervo A., Perito S.,
RA Bistoni F., Vecchiarelli A.;
RT "A Candida albicans mannoprotein deprived of its mannan moiety is
RT efficiently taken up and processed by human dendritic cells and induces T-
RT cell activation without stimulating proinflammatory cytokine production.";
RL Infect. Immun. 76:4359-4367(2008).
RN [16]
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=19098294; DOI=10.1093/jac/dkn515;
RA Pierce C.G., Thomas D.P., Lopez-Ribot J.L.;
RT "Effect of tunicamycin on Candida albicans biofilm formation and
RT maintenance.";
RL J. Antimicrob. Chemother. 63:473-479(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21622905; DOI=10.1128/ec.05011-11;
RA Sorgo A.G., Heilmann C.J., Dekker H.L., Bekker M., Brul S., de Koster C.G.,
RA de Koning L.J., Klis F.M.;
RT "Effects of fluconazole on the secretome, the wall proteome, and wall
RT integrity of the clinical fungus Candida albicans.";
RL Eukaryot. Cell 10:1071-1081(2011).
CC -!- FUNCTION: Surface mannoprotein required for hyphal morphogenesis,
CC surface adherence, and pathogenicity. Contributes in a high proportion
CC to the carbohydrate component of the matrix due to high levels of
CC glycosylation and may play important roles during biofilm development
CC and maintenance. Acts as a major antigen target of host cell-mediated
CC immune response. Induces extensive T-cell proliferation of human
CC peripheral blood mononuclear cells. Facilitates host dendritic cells
CC maturation and promotes cytokine production through its glycosylated
CC portion while its protein core is essentially involved in induction of
CC T-cell response. {ECO:0000269|PubMed:17217426}.
CC -!- SUBUNIT: Component of a multiprotein complex of 250 kDa composed of at
CC least HYR1, MP65, and PRA1. {ECO:0000269|PubMed:17277107}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:15302828,
CC ECO:0000269|PubMed:17277107, ECO:0000269|PubMed:17905924,
CC ECO:0000269|PubMed:19098294, ECO:0000269|PubMed:21622905,
CC ECO:0000269|PubMed:8698482}.
CC -!- INDUCTION: Expressed predominantly by the mycelial cells. Also induced
CC during cell wall regeneration and biofilm formation. Repressed by
CC fluconazole. {ECO:0000269|PubMed:16455273, ECO:0000269|PubMed:21622905,
CC ECO:0000269|PubMed:7738727}.
CC -!- PTM: Glycosylated protein with a polysaccharide moiety composed
CC exclusively of mannose and glucose at a ratio of 12.7 to 1. Contributes
CC highly to the carbohydrate component of the matrix. Treatment with
CC tunicamycin impairs glycosylation. {ECO:0000269|PubMed:19098294}.
CC -!- DISRUPTION PHENOTYPE: Impairs germ tube formation and suppresses hyphal
CC formation. Decreases also pathogenicity and adherence to polystyrene
CC plates. {ECO:0000269|PubMed:17217426}.
CC -!- MISCELLANEOUS: The presence of the MP65 gene can be used as a
CC diagnostic marker to distinguish C.albicans from other yeast or Candida
CC species by PCR.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR EMBL; CP017624; AOW27981.1; -; Genomic_DNA.
DR RefSeq; XP_714424.2; XM_709331.2.
DR AlphaFoldDB; Q59XX2; -.
DR SMR; Q59XX2; -.
DR BioGRID; 1227045; 2.
DR STRING; 237561.Q59XX2; -.
DR GeneID; 3643951; -.
DR KEGG; cal:CAALFM_C210030CA; -.
DR CGD; CAL0000177294; MP65.
DR VEuPathDB; FungiDB:C2_10030C_A; -.
DR eggNOG; ENOG502QTKT; Eukaryota.
DR HOGENOM; CLU_2236255_0_0_1; -.
DR OrthoDB; 1247931at2759; -.
DR PRO; PR:Q59XX2; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IBA:GO_Central.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IMP:CGD.
DR GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IMP:CGD.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:CGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; IMP:CGD.
DR GO; GO:0036244; P:cellular response to neutral pH; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036178; P:filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0044416; P:induction by symbiont of host defense response; IDA:CGD.
DR InterPro; IPR000490; Glyco_hydro_17.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00332; Glyco_hydro_17; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell wall; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:8698482"
FT CHAIN 33..378
FT /note="Cell surface mannoprotein MP65"
FT /id="PRO_0000426722"
FT REGION 67..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 316
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
SQ 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
