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Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 1

Gene

PMT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT2 and more rarely with PMT3 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export. Required for incorporation of proteins in the cell wall.5 Publications

Catalytic activityi

Dolichyl D-mannosyl phosphate + protein = dolichyl phosphate + O-D-mannosylprotein.2 Publications

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.Curated
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

  • ER-associated misfolded protein catabolic process Source: SGD
  • fungal-type cell wall organization Source: GO_Central
  • protein exit from endoplasmic reticulum Source: SGD
  • protein O-linked mannosylation Source: SGD
  • regulation of endoplasmic reticulum unfolded protein response Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:YDL095W-MONOMER.
BRENDAi2.4.1.109. 984.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT39. Glycosyltransferase Family 39.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl-phosphate-mannose--protein mannosyltransferase 1Curated (EC:2.4.1.1092 Publications)
Gene namesi
Name:PMT11 Publication
Ordered Locus Names:YDL095WImported
ORF Names:D2390Imported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL095W.
SGDiS000002253. PMT1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 50Cytoplasmic1 PublicationAdd BLAST49
Transmembranei51 – 70Helical1 PublicationAdd BLAST20
Topological domaini71 – 135Lumenal1 PublicationAdd BLAST65
Transmembranei136 – 154Helical1 PublicationAdd BLAST19
Topological domaini155 – 179Cytoplasmic1 PublicationAdd BLAST25
Transmembranei180 – 200Helical1 PublicationAdd BLAST21
Topological domaini201 – 234Lumenal1 PublicationAdd BLAST34
Transmembranei235 – 259Helical1 PublicationAdd BLAST25
Topological domaini260 – 273Cytoplasmic1 PublicationAdd BLAST14
Transmembranei274 – 291Helical1 PublicationAdd BLAST18
Topological domaini292 – 584Lumenal1 PublicationAdd BLAST293
Transmembranei585 – 605Helical1 PublicationAdd BLAST21
Topological domaini606 – 685Cytoplasmic1 PublicationAdd BLAST80
Transmembranei686 – 710Helical1 PublicationAdd BLAST25
Topological domaini711 – 817Lumenal1 PublicationAdd BLAST107

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Affects glycosylation of chitinase and increases sensitivity to calcofluor white and caffeine.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi64R → A: Reduces mannosyltransferase activity. 1 Publication1
Mutagenesisi77 – 78DE → AA: Impairs mannosyltransferase activity. 1 Publication2
Mutagenesisi78E → A: Decreases substrate-binding and reduces mannosyltransferase activity. 2 Publications1
Mutagenesisi88Y → A: Moderately decreases complex formation with PMT2. 1 Publication1
Mutagenesisi100P → A: Moderately decreases complex formation with PMT2. 1 Publication1
Mutagenesisi138R → A: Impairs complex formation with PMT2. 1 Publication1
Mutagenesisi408L → A: Reduces mannosyltransferase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001214912 – 817Dolichyl-phosphate-mannose--protein mannosyltransferase 1Add BLAST816

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Glycosylationi390N-linked (GlcNAc...)Sequence analysis1
Glycosylationi513N-linked (GlcNAc...)Sequence analysis1
Glycosylationi743N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiP33775.
PRIDEiP33775.

Interactioni

Subunit structurei

PMT1 and PMT2 form a functional heterodimer. The complex interacts with endoplasmic reticulum proteins EMP24, ERV25, ERP1, ERP2, CDC48, HRD1, USA1, YOS9, ERO1, PDI1, UBR1, Cue4, DFM1 and TED1. Forms also a minor complex with PMT3.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PMT2P313824EBI-13567,EBI-13573
PMT3P471903EBI-13567,EBI-13579

Protein-protein interaction databases

BioGridi31966. 161 interactors.
DIPiDIP-7911N.
IntActiP33775. 2 interactors.
MINTiMINT-2787975.

Structurei

3D structure databases

ProteinModelPortaliP33775.
SMRiP33775.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini324 – 378MIR 1PROSITE-ProRule annotationAdd BLAST55
Domaini388 – 448MIR 2PROSITE-ProRule annotationAdd BLAST61
Domaini459 – 514MIR 3PROSITE-ProRule annotationAdd BLAST56

Domaini

The large luminal loop 5 is essential for mannosyltransferase activity but not for PMT1-PMT2 complex formation.1 Publication

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00860000133866.
HOGENOMiHOG000157526.
InParanoidiP33775.
KOiK00728.
OMAiHKVKLPD.
OrthoDBiEOG092C0JF4.

Family and domain databases

InterProiIPR027005. GlyclTrfase_39-like.
IPR003342. Glyco_trans_39/83.
IPR016093. MIR_motif.
IPR027004. PMT1/PTM5.
IPR032421. PMT_4TMC.
[Graphical view]
PANTHERiPTHR10050. PTHR10050. 1 hit.
PTHR10050:SF28. PTHR10050:SF28. 1 hit.
PfamiPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
PF16192. PMT_4TMC. 1 hit.
[Graphical view]
SMARTiSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMiSSF82109. SSF82109. 1 hit.
PROSITEiPS50919. MIR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P33775-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEEKTYKRV EQDDPVPELD IKQGPVRPFI VTDPSAELAS LRTMVTLKEK
60 70 80 90 100
LLVACLAVFT AVIRLHGLAW PDSVVFDEVH FGGFASQYIR GTYFMDVHPP
110 120 130 140 150
LAKMLYAGVA SLGGFQGDFD FENIGDSFPS TTPYVLMRFF SASLGALTVI
160 170 180 190 200
LMYMTLRYSG VRMWVALMSA ICFAVENSYV TISRYILLDA PLMFFIAAAV
210 220 230 240 250
YSFKKYEMYP ANSLNAYKSL LATGIALGMA SSSKWVGLFT VTWVGLLCIW
260 270 280 290 300
RLWFMIGDLT KSSKSIFKVA FAKLAFLLGV PFALYLVFFY IHFQSLTLDG
310 320 330 340 350
DGASFFSPEF RSTLKNNKIP QNVVADVGIG SIISLRHLST MGGYLHSHSH
360 370 380 390 400
NYPAGSEQQQ STLYPHMDAN NDWLLELYNA PGESLTTFQN LTDGTKVRLF
410 420 430 440 450
HTVTRCRLHS HDHKPPVSES SDWQKEVSCY GYSGFDGDAN DDWVVEIDKK
460 470 480 490 500
NSAPGVAQER VIALDTKFRL RHAMTGCYLF SHEVKLPAWG FEQQEVTCAS
510 520 530 540 550
SGRHDLTLWY VENNSNPLLP EDTKRISYKP ASFISKFIES HKKMWHINKN
560 570 580 590 600
LVEPHVYESQ PTSWPFLLRG ISYWGENNRN VYLLGNAIVW WAVTAFIGIF
610 620 630 640 650
GLIVITELFS WQLGKPILKD SKVVNFHVQV IHYLLGFAVH YAPSFLMQRQ
660 670 680 690 700
MFLHHYLPAY YFGILALGHA LDIIVSYVFR SKRQMGYAVV ITFLAASVYF
710 720 730 740 750
FKSFSPIIYG TPWTQELCQK SQWLSGWDYN CNTYFSSLEE YKNQTLTKRE
760 770 780 790 800
SQPAATSTVE EITIEGDGPS YEDLMNEDGK KIFKDTEGNE LDPEVVKKML
810
EEEGANILKV EKRAVLE
Length:817
Mass (Da):92,675
Last modified:February 1, 1994 - v1
Checksum:i6309BBA71BAD8D21
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19169 Unassigned DNA. Translation: AAA02928.1.
X95644 Genomic DNA. Translation: CAA64917.1.
Z74144 Genomic DNA. Translation: CAA98663.1.
BK006938 Genomic DNA. Translation: DAA11764.1.
PIRiA47716.
RefSeqiNP_010188.1. NM_001180154.1.

Genome annotation databases

EnsemblFungiiYDL095W; YDL095W; YDL095W.
GeneIDi851462.
KEGGisce:YDL095W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19169 Unassigned DNA. Translation: AAA02928.1.
X95644 Genomic DNA. Translation: CAA64917.1.
Z74144 Genomic DNA. Translation: CAA98663.1.
BK006938 Genomic DNA. Translation: DAA11764.1.
PIRiA47716.
RefSeqiNP_010188.1. NM_001180154.1.

3D structure databases

ProteinModelPortaliP33775.
SMRiP33775.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31966. 161 interactors.
DIPiDIP-7911N.
IntActiP33775. 2 interactors.
MINTiMINT-2787975.

Protein family/group databases

CAZyiGT39. Glycosyltransferase Family 39.

Proteomic databases

MaxQBiP33775.
PRIDEiP33775.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL095W; YDL095W; YDL095W.
GeneIDi851462.
KEGGisce:YDL095W.

Organism-specific databases

EuPathDBiFungiDB:YDL095W.
SGDiS000002253. PMT1.

Phylogenomic databases

GeneTreeiENSGT00860000133866.
HOGENOMiHOG000157526.
InParanoidiP33775.
KOiK00728.
OMAiHKVKLPD.
OrthoDBiEOG092C0JF4.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciYEAST:YDL095W-MONOMER.
BRENDAi2.4.1.109. 984.

Miscellaneous databases

PROiP33775.

Family and domain databases

InterProiIPR027005. GlyclTrfase_39-like.
IPR003342. Glyco_trans_39/83.
IPR016093. MIR_motif.
IPR027004. PMT1/PTM5.
IPR032421. PMT_4TMC.
[Graphical view]
PANTHERiPTHR10050. PTHR10050. 1 hit.
PTHR10050:SF28. PTHR10050:SF28. 1 hit.
PfamiPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
PF16192. PMT_4TMC. 1 hit.
[Graphical view]
SMARTiSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMiSSF82109. SSF82109. 1 hit.
PROSITEiPS50919. MIR. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPMT1_YEAST
AccessioniPrimary (citable) accession number: P33775
Secondary accession number(s): D6VRQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 30, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 41500 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.