ID   PMT1_CANAL              Reviewed;         877 AA.
AC   O74189; A0A1D8PR95; Q3MP65; Q5A5A9;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 1;
DE            Short=Protein mannosyltransferase 1;
DE            EC=2.4.1.109 {ECO:0000250|UniProtKB:P33775};
GN   Name=PMT1; OrderedLocusNames=CAALFM_C702890CA;
GN   ORFNames=CaJ7.0330 {ECO:0000303|PubMed:15937140}, CaO19.12638,
GN   CaO19.5171;
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 [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=CAF3-1;
RX   PubMed=9694829; DOI=10.1074/jbc.273.33.20837;
RA   Timpel C., Strahl-Bolsinger S., Ziegelbauer K., Ernst J.F.;
RT   "Multiple functions of Pmt1p-mediated protein O-mannosylation in the fungal
RT   pathogen Candida albicans.";
RL   J. Biol. Chem. 273:20837-20846(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15937140; DOI=10.1534/genetics.104.034652;
RA   Chibana H., Oka N., Nakayama H., Aoyama T., Magee B.B., Magee P.T.,
RA   Mikami Y.;
RT   "Sequence finishing and gene mapping for Candida albicans chromosome 7 and
RT   syntenic analysis against the Saccharomyces cerevisiae genome.";
RL   Genetics 170:1525-1537(2005).
RN   [3]
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   [4]
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   [5]
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   [6]
RP   FUNCTION.
RX   PubMed=15470244; DOI=10.1128/ec.3.5.1164-1168.2004;
RA   Weber Y., Prill S.K., Ernst J.F.;
RT   "Pmt-mediated O mannosylation stabilizes an essential component of the
RT   secretory apparatus, Sec20p, in Candida albicans.";
RL   Eukaryot. Cell 3:1164-1168(2004).
RN   [7]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=16040968; DOI=10.1128/iai.73.8.4571-4580.2005;
RA   Rouabhia M., Schaller M., Corbucci C., Vecchiarelli A., Prill S.K.,
RA   Giasson L., Ernst J.F.;
RT   "Virulence of the fungal pathogen Candida albicans requires the five
RT   isoforms of protein mannosyltransferases.";
RL   Infect. Immun. 73:4571-4580(2005).
RN   [8]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=15659169; DOI=10.1111/j.1365-2958.2004.04401.x;
RA   Prill S.K., Klinkert B., Timpel C., Gale C.A., Schroppel K., Ernst J.F.;
RT   "PMT family of Candida albicans: five protein mannosyltransferase isoforms
RT   affect growth, morphogenesis and antifungal resistance.";
RL   Mol. Microbiol. 55:546-560(2005).
RN   [9]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=17005840; DOI=10.1128/aac.00606-06;
RA   Peltroche-Llacsahuanga H., Goyard S., d'Enfert C., Prill S.K., Ernst J.F.;
RT   "Protein O-mannosyltransferase isoforms regulate biofilm formation in
RT   Candida albicans.";
RL   Antimicrob. Agents Chemother. 50:3488-3491(2006).
RN   [10]
RP   FUNCTION.
RX   PubMed=20533408; DOI=10.1002/yea.1790;
RA   de Boer A.D., de Groot P.W., Weindl G., Schaller M., Riedel D.,
RA   Diez-Orejas R., Klis F.M., de Koster C.G., Dekker H.L., Gross U., Bader O.,
RA   Weig M.;
RT   "The Candida albicans cell wall protein Rhd3/Pga29 is abundant in the yeast
RT   form and contributes to virulence.";
RL   Yeast 27:611-624(2010).
RN   [11]
RP   INDUCTION.
RX   PubMed=21375589; DOI=10.1111/j.1365-2958.2011.07604.x;
RA   Cantero P.D., Ernst J.F.;
RT   "Damage to the glycoshield activates PMT-directed O-mannosylation via the
RT   Msb2-Cek1 pathway in Candida albicans.";
RL   Mol. Microbiol. 80:715-725(2011).
CC   -!- FUNCTION: Protein mannosyltransferase (PMT) involved in hyphal growth
CC       and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or
CC       Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the
CC       protein-O-glycosylation activity, while PMT5 and PMT6 may specifically
CC       modulate a much narrower spectrum of target proteins. Accounts for the
CC       O-glycosylation of the cell wall proteins KRE9, PIR2, RHD3, and ALS1,
CC       as well as the SEC20 t-SNARE component. O-glycosylation of SEC20 is
CC       essential for its stability. Required for filamentation and early
CC       phases of biofilm formation. {ECO:0000269|PubMed:15470244,
CC       ECO:0000269|PubMed:15659169, ECO:0000269|PubMed:16040968,
CC       ECO:0000269|PubMed:17005840, ECO:0000269|PubMed:20533408,
CC       ECO:0000269|PubMed:9694829}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-
CC         O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+);
CC         Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC         Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC         ChEBI:CHEBI:137321; EC=2.4.1.109;
CC         Evidence={ECO:0000250|UniProtKB:P33775, ECO:0000303|PubMed:15659169};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] =
CC         3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate +
CC         H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC         Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC         ChEBI:CHEBI:137323; EC=2.4.1.109;
CC         Evidence={ECO:0000250|UniProtKB:P33775, ECO:0000303|PubMed:15659169};
CC   -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC   -!- SUBUNIT: PMT1 and PMT2 form a functional heterodimer.
CC       {ECO:0000250|UniProtKB:P33775}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:P33775}.
CC   -!- INDUCTION: Transcript levels are increased at least twofold by
CC       tunicamycin and Congo red. Both MSB2 and CEK1 are required to down-
CC       regulate PMT1 transcript levels in cells with intact glycostructures.
CC       {ECO:0000269|PubMed:21375589}.
CC   -!- DISRUPTION PHENOTYPE: Shows altered cell wall composition with a
CC       significant decrease in wall mannoproteins. Impairs biofilm formation
CC       and shows reduced virulence in a mouse model of hematogenously
CC       disseminated candidiasis (HDC) and using reconstituted human epithelium
CC       (RHE) or engineered human oral mucosa (EHOM).
CC       {ECO:0000269|PubMed:15659169, ECO:0000269|PubMed:16040968,
CC       ECO:0000269|PubMed:17005840}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC       {ECO:0000305}.
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DR   EMBL; AF000232; AAC31119.1; -; Genomic_DNA.
DR   EMBL; AP006852; BAE44795.1; -; Genomic_DNA.
DR   EMBL; CP017629; AOW30636.1; -; Genomic_DNA.
DR   RefSeq; XP_716993.1; XM_711900.2.
DR   AlphaFoldDB; O74189; -.
DR   SMR; O74189; -.
DR   BioGRID; 1224487; 3.
DR   STRING; 237561.O74189; -.
DR   BindingDB; O74189; -.
DR   ChEMBL; CHEMBL3534; -.
DR   CAZy; GT39; Glycosyltransferase Family 39.
DR   GlyCosmos; O74189; 5 sites, No reported glycans.
DR   EnsemblFungi; C7_02890C_A-T; C7_02890C_A-T-p1; C7_02890C_A.
DR   GeneID; 3641393; -.
DR   KEGG; cal:CAALFM_C702890CA; -.
DR   CGD; CAL0000192847; PMT1.
DR   VEuPathDB; FungiDB:C7_02890C_A; -.
DR   eggNOG; KOG3359; Eukaryota.
DR   HOGENOM; CLU_008438_2_0_1; -.
DR   InParanoid; O74189; -.
DR   OMA; KNVTPRL; -.
DR   OrthoDB; 5489060at2759; -.
DR   BRENDA; 2.4.1.109; 1096.
DR   UniPathway; UPA00378; -.
DR   PHI-base; PHI:451; -.
DR   PRO; PR:O74189; -.
DR   Proteomes; UP000000559; Chromosome 7.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR   GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000030; F:mannosyltransferase activity; IMP:CGD.
DR   GO; GO:0051701; P:biological process involved in interaction with host; IMP:CGD.
DR   GO; GO:0031589; P:cell-substrate adhesion; IMP:CGD.
DR   GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR   GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR   GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR   GO; GO:0045861; P:negative regulation of proteolysis; IMP:CGD.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IMP:CGD.
DR   GO; GO:0035269; P:protein O-linked mannosylation; IMP:CGD.
DR   GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
DR   Gene3D; 2.80.10.50; -; 1.
DR   InterPro; IPR027005; GlyclTrfase_39-like.
DR   InterPro; IPR003342; Glyco_trans_39/83.
DR   InterPro; IPR036300; MIR_dom_sf.
DR   InterPro; IPR016093; MIR_motif.
DR   InterPro; IPR032421; PMT_4TMC.
DR   PANTHER; PTHR10050; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR10050:SF50; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE 1-RELATED; 1.
DR   Pfam; PF02815; MIR; 1.
DR   Pfam; PF02366; PMT; 1.
DR   Pfam; PF16192; PMT_4TMC; 1.
DR   SMART; SM00472; MIR; 3.
DR   SUPFAM; SSF82109; MIR domain; 1.
DR   PROSITE; PS50919; MIR; 3.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW   Reference proteome; Repeat; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..877
FT                   /note="Dolichyl-phosphate-mannose--protein
FT                   mannosyltransferase 1"
FT                   /id="PRO_0000121498"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        604..624
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        643..663
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        666..686
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        700..720
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          340..394
FT                   /note="MIR 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          403..462
FT                   /note="MIR 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   DOMAIN          472..528
FT                   /note="MIR 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT   REGION          778..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        786..817
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..870
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        395
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        400
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        721
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   877 AA;  99935 MW;  3B0F6ED9C96DCC16 CRC64;
     MAKKPVTPAS KVAAKQAAVR SRHQEDVFTL DPLIDPIFQK GELRSYLVTE PSPSVLKKRS
     IHTKEYWMLS SLLLIAFYVR MYNLSNPNSV VFDEVHFGGF ARKYILGTFF MDVHPPLAKM
     LFGAVGAIGG FKGDFEFKSI GDKFPDSTPY IFMRQFPALL GVGTVILCYL TLRQSGVRPI
     IAYITTFLLI IENSNVTISR YILLDSPLIF FIAAAIYAWK KFEIQIPFTF GWYRSLLATG
     IALGLALSSK WVGLFTVAWV GFLCIYQLWF LIGDLSVSTK KIWGHFFARG IILLGVPIAL
     YLGFFAIHFQ LLNKEGDGGA FMSSAFRAGL QGNKIPRDIT EQVGLGSVVT IRHVDTQGGY
     LHSHEHFYQT GSKQQQITLY PHLDSNNKWL IEPYNGTIHN ETFVPLINGM KIRLKHINTG
     RRLHSHDEKP PVSERDWQKE CSCYGYDGFA GDANDDWVVE IVNYRSQKGE AQTFVKAINT
     IFRLRHAMTG HYLFSSEVKL PEWGFGQQEV TSASQGKRAL THWYIETNEN SILPPSEAKI
     INYPKLSLWQ KVVESHKRMW KINQGLTSHH HWQSSPSEWP LLLRGINYWN KEHKQVYLLG
     NAVTWWAATL SIITFGTYVL VTVFRWHLGT PLSTNKHVFN FNVQTFSYVL GWALHYLPFF
     IMGRQLFLHH YLPALYFGIL ALGHFFEIFT GYLTSRSKYF QQVAFVLVGL FSILSLVFYV
     NYSSLIYGTP WTKASCELTK PFSGWDYNCG TFFDTLGEYD IQEKSLASES EIPTETVVVE
     AKQTPKAEPK LAKQDDHIES PAAAEPVEEK EVKEEVEQLA PPLAVDFEEE TPKVEDPQVA
     DVDASSNDEK SVEEKQQQEQ QQEQEQVEDE SVHQVQQ
//