PMT1_CANAL
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 03-AUG-2022, entry version 141.
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, 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 PRIDE; O74189; -.
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; TLSVKWV; -.
DR OrthoDB; 203029at2759; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; IPR027004; PMT1/PTM5.
DR InterPro; IPR032421; PMT_4TMC.
DR PANTHER; PTHR10050; PTHR10050; 1.
DR PANTHER; PTHR10050:SF50; PTHR10050:SF50; 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; SSF82109; 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
