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O74189

- PMT1_CANAL

UniProt

O74189 - PMT1_CANAL

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Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 1

Gene

PMT1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Protein mannosyltransferase (PMT) involved in hyphal growth and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the protein-O-glycosylation activity, while PMT5 and PMT6 may specifically modulate a much narrower spectrum of target proteins. Accounts for the O-glycosylation of the cell wall proteins KRE9, PIR2, RHD3, and ALS1, as well as the SEC20 t-SNARE component. O-glycosylation of SEC20 is essential for its stability. Required for filamentation and early phases of biofilm formation.6 Publications

Catalytic activityi

Dolichyl D-mannosyl phosphate + protein = dolichyl phosphate + O-D-mannosylprotein.By similarity1 Publication

Pathwayi

GO - Molecular functioni

  1. dolichyl-phosphate-mannose-protein mannosyltransferase activity Source: UniProtKB-EC
  2. mannosyltransferase activity Source: CGD

GO - Biological processi

  1. cell-substrate adhesion Source: CGD
  2. cellular response to drug Source: CGD
  3. cellular response to neutral pH Source: CGD
  4. cellular response to starvation Source: CGD
  5. filamentous growth Source: CGD
  6. filamentous growth of a population of unicellular organisms Source: CGD
  7. filamentous growth of a population of unicellular organisms in response to neutral pH Source: CGD
  8. filamentous growth of a population of unicellular organisms in response to starvation Source: CGD
  9. fungal-type cell wall organization Source: CGD
  10. growth of symbiont in host Source: CGD
  11. negative regulation of proteolysis Source: CGD
  12. pathogenesis Source: CGD
  13. protein O-linked glycosylation Source: CGD
  14. protein O-linked mannosylation Source: CGD
  15. single-species biofilm formation on inanimate substrate Source: CGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.109. 1096.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT39. Glycosyltransferase Family 39.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl-phosphate-mannose--protein mannosyltransferase 1 (EC:2.4.1.109By similarity)
Short name:
Protein mannosyltransferase 1Imported
Gene namesi
Name:PMT1Imported
ORF Names:CaJ7.0330Imported1 Publication, CaO19.12638Imported, CaO19.5171Imported
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
ProteomesiUP000000559: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0002654. PMT1.

Subcellular locationi

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei109 – 12921HelicalSequence AnalysisAdd
BLAST
Transmembranei150 – 17021HelicalSequence AnalysisAdd
BLAST
Transmembranei196 – 21621HelicalSequence AnalysisAdd
BLAST
Transmembranei226 – 24621HelicalSequence AnalysisAdd
BLAST
Transmembranei252 – 27221HelicalSequence AnalysisAdd
BLAST
Transmembranei291 – 31121HelicalSequence AnalysisAdd
BLAST
Transmembranei604 – 62421HelicalSequence AnalysisAdd
BLAST
Transmembranei643 – 66321HelicalSequence AnalysisAdd
BLAST
Transmembranei666 – 68621HelicalSequence AnalysisAdd
BLAST
Transmembranei700 – 72021HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: CGD
  4. plasma membrane Source: CGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Shows altered cell wall composition with a significant decrease in wall mannoproteins. Impairs biofilm formation and shows reduced virulence in a mouse model of hematogenously disseminated candidiasis (HDC) and using reconstituted human epithelium (RHE) or engineered human oral mucosa (EHOM).3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 877877Dolichyl-phosphate-mannose--protein mannosyltransferase 1PRO_0000121498Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi195 – 1951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi400 – 4001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi721 – 7211N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Expressioni

Inductioni

Transcript levels are increased at least twofold by tunicamycin and Congo red. Both MSB2 and CEK1 are required to down-regulate PMT1 transcript levels in cells with intact glycostructures.1 Publication

Interactioni

Subunit structurei

PMT1 and PMT2 form a functional heterodimer.By similarity

Protein-protein interaction databases

STRINGi5476.CAL0002654.

Structurei

3D structure databases

ProteinModelPortaliO74189.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini340 – 39455MIR 1PROSITE-ProRule annotationAdd
BLAST
Domaini403 – 46260MIR 2PROSITE-ProRule annotationAdd
BLAST
Domaini472 – 52857MIR 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 39 family.Curated
Contains 3 MIR domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1928.
InParanoidiO74189.
KOiK00728.
OrthoDBiEOG7BP89X.

Family and domain databases

InterProiIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
IPR027004. PMT1/PTM5.
[Graphical view]
PANTHERiPTHR10050. PTHR10050. 1 hit.
PTHR10050:SF28. PTHR10050:SF28. 1 hit.
PfamiPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view]
SMARTiSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMiSSF82109. SSF82109. 1 hit.
PROSITEiPS50919. MIR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O74189-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKKPVTPAS KVAAKQAAVR SRHQEDVFTL DPLIDPIFQK GELRSYLVTE
60 70 80 90 100
PSPSVLKKRS IHTKEYWMLS SLLLIAFYVR MYNLSNPNSV VFDEVHFGGF
110 120 130 140 150
ARKYILGTFF MDVHPPLAKM LFGAVGAIGG FKGDFEFKSI GDKFPDSTPY
160 170 180 190 200
IFMRQFPALL GVGTVILCYL TLRQSGVRPI IAYITTFLLI IENSNVTISR
210 220 230 240 250
YILLDSPLIF FIAAAIYAWK KFEIQIPFTF GWYRSLLATG IALGLALSSK
260 270 280 290 300
WVGLFTVAWV GFLCIYQLWF LIGDLSVSTK KIWGHFFARG IILLGVPIAL
310 320 330 340 350
YLGFFAIHFQ LLNKEGDGGA FMSSAFRAGL QGNKIPRDIT EQVGLGSVVT
360 370 380 390 400
IRHVDTQGGY LHSHEHFYQT GSKQQQITLY PHLDSNNKWL IEPYNGTIHN
410 420 430 440 450
ETFVPLINGM KIRLKHINTG RRLHSHDEKP PVSERDWQKE CSCYGYDGFA
460 470 480 490 500
GDANDDWVVE IVNYRSQKGE AQTFVKAINT IFRLRHAMTG HYLFSSEVKL
510 520 530 540 550
PEWGFGQQEV TSASQGKRAL THWYIETNEN SILPPSEAKI INYPKLSLWQ
560 570 580 590 600
KVVESHKRMW KINQGLTSHH HWQSSPSEWP LLLRGINYWN KEHKQVYLLG
610 620 630 640 650
NAVTWWAATL SIITFGTYVL VTVFRWHLGT PLSTNKHVFN FNVQTFSYVL
660 670 680 690 700
GWALHYLPFF IMGRQLFLHH YLPALYFGIL ALGHFFEIFT GYLTSRSKYF
710 720 730 740 750
QQVAFVLVGL FSILSLVFYV NYSSLIYGTP WTKASCELTK PFSGWDYNCG
760 770 780 790 800
TFFDTLGEYD IQEKSLASES EIPTETVVVE AKQTPKAEPK LAKQDDHIES
810 820 830 840 850
PAAAEPVEEK EVKEEVEQLA PPLAVDFEEE TPKVEDPQVA DVDASSNDEK
860 870
SVEEKQQQEQ QQEQEQVEDE SVHQVQQ
Length:877
Mass (Da):99,935
Last modified:November 1, 1998 - v1
Checksum:i3B0F6ED9C96DCC16
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF000232 Genomic DNA. Translation: AAC31119.1.
AP006852 Genomic DNA. Translation: BAE44795.1.
AACQ01000061 Genomic DNA. Translation: EAK97943.1.
AACQ01000060 Genomic DNA. Translation: EAK98013.1.
RefSeqiXP_716926.1. XM_711833.1.
XP_716993.1. XM_711900.1.
XP_888898.1. XM_883805.1.

Genome annotation databases

GeneIDi3641393.
3641443.
3703892.
KEGGical:CaO19.12638.
cal:CaO19.5171.
cal:CaO19_5171.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF000232 Genomic DNA. Translation: AAC31119.1 .
AP006852 Genomic DNA. Translation: BAE44795.1 .
AACQ01000061 Genomic DNA. Translation: EAK97943.1 .
AACQ01000060 Genomic DNA. Translation: EAK98013.1 .
RefSeqi XP_716926.1. XM_711833.1.
XP_716993.1. XM_711900.1.
XP_888898.1. XM_883805.1.

3D structure databases

ProteinModelPortali O74189.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5476.CAL0002654.

Chemistry

BindingDBi O74189.
ChEMBLi CHEMBL3534.

Protein family/group databases

CAZyi GT39. Glycosyltransferase Family 39.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3641393.
3641443.
3703892.
KEGGi cal:CaO19.12638.
cal:CaO19.5171.
cal:CaO19_5171.

Organism-specific databases

CGDi CAL0002654. PMT1.

Phylogenomic databases

eggNOGi COG1928.
InParanoidi O74189.
KOi K00728.
OrthoDBi EOG7BP89X.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 2.4.1.109. 1096.

Family and domain databases

InterProi IPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
IPR027004. PMT1/PTM5.
[Graphical view ]
PANTHERi PTHR10050. PTHR10050. 1 hit.
PTHR10050:SF28. PTHR10050:SF28. 1 hit.
Pfami PF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view ]
SMARTi SM00472. MIR. 3 hits.
[Graphical view ]
SUPFAMi SSF82109. SSF82109. 1 hit.
PROSITEi PS50919. MIR. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Multiple functions of Pmt1p-mediated protein O-mannosylation in the fungal pathogen Candida albicans."
    Timpel C., Strahl-Bolsinger S., Ziegelbauer K., Ernst J.F.
    J. Biol. Chem. 273:20837-20846(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: CAF3-1.
  2. "Sequence finishing and gene mapping for Candida albicans chromosome 7 and syntenic analysis against the Saccharomyces cerevisiae genome."
    Chibana H., Oka N., Nakayama H., Aoyama T., Magee B.B., Magee P.T., Mikami Y.
    Genetics 170:1525-1537(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SC5314 / ATCC MYA-2876.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SC5314 / ATCC MYA-2876.
  4. "Pmt-mediated O mannosylation stabilizes an essential component of the secretory apparatus, Sec20p, in Candida albicans."
    Weber Y., Prill S.K., Ernst J.F.
    Eukaryot. Cell 3:1164-1168(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Virulence of the fungal pathogen Candida albicans requires the five isoforms of protein mannosyltransferases."
    Rouabhia M., Schaller M., Corbucci C., Vecchiarelli A., Prill S.K., Giasson L., Ernst J.F.
    Infect. Immun. 73:4571-4580(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  6. "PMT family of Candida albicans: five protein mannosyltransferase isoforms affect growth, morphogenesis and antifungal resistance."
    Prill S.K., Klinkert B., Timpel C., Gale C.A., Schroppel K., Ernst J.F.
    Mol. Microbiol. 55:546-560(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  7. "Protein O-mannosyltransferase isoforms regulate biofilm formation in Candida albicans."
    Peltroche-Llacsahuanga H., Goyard S., d'Enfert C., Prill S.K., Ernst J.F.
    Antimicrob. Agents Chemother. 50:3488-3491(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  8. "The Candida albicans cell wall protein Rhd3/Pga29 is abundant in the yeast form and contributes to virulence."
    de Boer A.D., de Groot P.W., Weindl G., Schaller M., Riedel D., Diez-Orejas R., Klis F.M., de Koster C.G., Dekker H.L., Gross U., Bader O., Weig M.
    Yeast 27:611-624(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Damage to the glycoshield activates PMT-directed O-mannosylation via the Msb2-Cek1 pathway in Candida albicans."
    Cantero P.D., Ernst J.F.
    Mol. Microbiol. 80:715-725(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiPMT1_CANAL
AccessioniPrimary (citable) accession number: O74189
Secondary accession number(s): Q3MP65, Q5A5A9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: November 26, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3