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O74189 (PMT1_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dolichyl-phosphate-mannose--protein mannosyltransferase 1

EC=2.4.1.109
Gene names
Name:PMT1
ORF Names:CaJ7.0330, CaO19.12638, CaO19.5171
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length877 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.

Catalytic activity

Dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the glycosyltransferase 39 family.

Contains 3 MIR domains.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   DomainRepeat
Transmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell-substrate adhesion

Inferred from mutant phenotype Ref.1. Source: CGD

cellular response to drug

Inferred from mutant phenotype PubMed 10809683PubMed 15659169Ref.1. Source: CGD

cellular response to neutral pH

Inferred from mutant phenotype PubMed 15659169. Source: CGD

cellular response to starvation

Inferred from mutant phenotype PubMed 10809683Ref.1. Source: CGD

filamentous growth

Inferred from mutant phenotype PubMed 10809683PubMed 15659169Ref.1. Source: CGD

filamentous growth of a population of unicellular organisms

Inferred from mutant phenotype PubMed 15659169. Source: CGD

filamentous growth of a population of unicellular organisms in response to neutral pH

Inferred from mutant phenotype PubMed 15659169. Source: CGD

filamentous growth of a population of unicellular organisms in response to starvation

Inferred from mutant phenotype PubMed 10809683Ref.1. Source: CGD

fungal-type cell wall organization

Inferred from mutant phenotype PubMed 10672182PubMed 15659169Ref.1. Source: CGD

growth of symbiont in host

Inferred from mutant phenotype Ref.1. Source: CGD

negative regulation of proteolysis

Inferred from mutant phenotype PubMed 15470244. Source: CGD

pathogenesis

Inferred from mutant phenotype PubMed 10809683PubMed 15659169Ref.1. Source: CGD

protein O-linked glycosylation

Inferred from mutant phenotype Ref.1. Source: CGD

protein O-linked mannosylation

Inferred from mutant phenotype PubMed 15470244. Source: CGD

single-species biofilm formation on inanimate substrate

Inferred from mutant phenotype PubMed 17005840. Source: CGD

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from sequence or structural similarity PubMed 10809683Ref.1. Source: CGD

membrane

Inferred from direct assay PubMed 16534748. Source: CGD

plasma membrane

Inferred from direct assay PubMed 19824013. Source: CGD

   Molecular_functiondolichyl-phosphate-mannose-protein mannosyltransferase activity

Inferred from sequence or structural similarity PubMed 15659169. Source: CGD

mannosyltransferase activity

Inferred from mutant phenotype PubMed 15470244Ref.1. Source: CGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 877877Dolichyl-phosphate-mannose--protein mannosyltransferase 1
PRO_0000121498

Regions

Transmembrane109 – 12921Helical; Potential
Transmembrane150 – 17021Helical; Potential
Transmembrane196 – 21621Helical; Potential
Transmembrane226 – 24621Helical; Potential
Transmembrane252 – 27221Helical; Potential
Transmembrane291 – 31121Helical; Potential
Transmembrane604 – 62421Helical; Potential
Transmembrane643 – 66321Helical; Potential
Transmembrane666 – 68621Helical; Potential
Transmembrane700 – 72021Helical; Potential
Domain340 – 39455MIR 1
Domain403 – 46260MIR 2
Domain472 – 52857MIR 3

Amino acid modifications

Glycosylation831N-linked (GlcNAc...) Potential
Glycosylation1951N-linked (GlcNAc...) Potential
Glycosylation3951N-linked (GlcNAc...) Potential
Glycosylation4001N-linked (GlcNAc...) Potential
Glycosylation7211N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O74189 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 3B0F6ED9C96DCC16

FASTA87799,935
        10         20         30         40         50         60 
MAKKPVTPAS KVAAKQAAVR SRHQEDVFTL DPLIDPIFQK GELRSYLVTE PSPSVLKKRS 

        70         80         90        100        110        120 
IHTKEYWMLS SLLLIAFYVR MYNLSNPNSV VFDEVHFGGF ARKYILGTFF MDVHPPLAKM 

       130        140        150        160        170        180 
LFGAVGAIGG FKGDFEFKSI GDKFPDSTPY IFMRQFPALL GVGTVILCYL TLRQSGVRPI 

       190        200        210        220        230        240 
IAYITTFLLI IENSNVTISR YILLDSPLIF FIAAAIYAWK KFEIQIPFTF GWYRSLLATG 

       250        260        270        280        290        300 
IALGLALSSK WVGLFTVAWV GFLCIYQLWF LIGDLSVSTK KIWGHFFARG IILLGVPIAL 

       310        320        330        340        350        360 
YLGFFAIHFQ LLNKEGDGGA FMSSAFRAGL QGNKIPRDIT EQVGLGSVVT IRHVDTQGGY 

       370        380        390        400        410        420 
LHSHEHFYQT GSKQQQITLY PHLDSNNKWL IEPYNGTIHN ETFVPLINGM KIRLKHINTG 

       430        440        450        460        470        480 
RRLHSHDEKP PVSERDWQKE CSCYGYDGFA GDANDDWVVE IVNYRSQKGE AQTFVKAINT 

       490        500        510        520        530        540 
IFRLRHAMTG HYLFSSEVKL PEWGFGQQEV TSASQGKRAL THWYIETNEN SILPPSEAKI 

       550        560        570        580        590        600 
INYPKLSLWQ KVVESHKRMW KINQGLTSHH HWQSSPSEWP LLLRGINYWN KEHKQVYLLG 

       610        620        630        640        650        660 
NAVTWWAATL SIITFGTYVL VTVFRWHLGT PLSTNKHVFN FNVQTFSYVL GWALHYLPFF 

       670        680        690        700        710        720 
IMGRQLFLHH YLPALYFGIL ALGHFFEIFT GYLTSRSKYF QQVAFVLVGL FSILSLVFYV 

       730        740        750        760        770        780 
NYSSLIYGTP WTKASCELTK PFSGWDYNCG TFFDTLGEYD IQEKSLASES EIPTETVVVE 

       790        800        810        820        830        840 
AKQTPKAEPK LAKQDDHIES PAAAEPVEEK EVKEEVEQLA PPLAVDFEEE TPKVEDPQVA 

       850        860        870 
DVDASSNDEK SVEEKQQQEQ QQEQEQVEDE SVHQVQQ 

« Hide

References

« Hide 'large scale' references
[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].
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]"The diploid genome sequence of Candida albicans."
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.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF000232 Genomic DNA. Translation: AAC31119.1.
AP006852 Genomic DNA. Translation: BAE44795.1.
AACQ01000061 Genomic DNA. Translation: EAK97943.1.
AACQ01000060 Genomic DNA. Translation: EAK98013.1.
RefSeqXP_716926.1. XM_711833.1.
XP_716993.1. XM_711900.1.
XP_888898.1. XM_883805.1.

3D structure databases

ProteinModelPortalO74189.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5476.CAL0002654.

Chemistry

BindingDBO74189.
ChEMBLCHEMBL3534.

Protein family/group databases

CAZyGT39. Glycosyltransferase Family 39.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3641393.
3641443.
3703892.
KEGGcal:CaO19.12638.
cal:CaO19.5171.
cal:CaO19_5171.

Organism-specific databases

CGDCAL0002654. PMT1.

Phylogenomic databases

eggNOGCOG1928.
KOK00728.
OrthoDBEOG7BP89X.

Enzyme and pathway databases

BRENDA2.4.1.109. 1096.
UniPathwayUPA00378.

Family and domain databases

InterProIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
IPR027004. PMT1/PTM5.
[Graphical view]
PANTHERPTHR10050. PTHR10050. 1 hit.
PTHR10050:SF28. PTHR10050:SF28. 1 hit.
PfamPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view]
SMARTSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMSSF82109. SSF82109. 1 hit.
PROSITEPS50919. MIR. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePMT1_CANAL
AccessionPrimary (citable) accession number: O74189
Secondary accession number(s): Q3MP65, Q5A5A9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: June 11, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Candida albicans

Candida albicans: entries and gene names