PMT1 dolichyl-phosphate-mannose-protein mannosyltransferase PMT1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: PMT1
Official Full Name: dolichyl-phosphate-mannose-protein mannosyltransferase PMT1
Primary source: SGD:S000002253
Locus tag: YDL095W
See related: AllianceGenome:SGD:S000002253; FungiDB:YDL095W; VEuPathDB:YDL095W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables dolichyl-phosphate-mannose-protein mannosyltransferase activity. Involved in several processes, including ERAD pathway; protein O-linked mannosylation; and protein exit from endoplasmic reticulum. Located in endoplasmic reticulum. Part of dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt2p dimer complex and dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt3p dimer complex. [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See PMT1 in Genome Data Viewer

Location:: chromosome: IV

Exon count:: 1

Sequence:: Chromosome: IV; NC_001136.10 (287059..289512)

Chromosome IV - NC_001136.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001136.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Maximal Pmt1 expression depends on both, transcriptional activation of Pmt1 under cell stress conditions as well as elevated translation efficiency mediated by Bfr1. The fine-tuned coordination of Pmt1 protein abundance with ER stress further implies that O-mannosylation and protein folding must be balanced to ensure functionality of canonical target proteins and unfolded protein O-mannosylation.
Title: Translational Regulation of Pmt1 and Pmt2 by Bfr1 Affects Unfolded Protein O-Mannosylation.
Cryo-EM structures of the Saccharomyces cerevisiae Pmt1-Pmt2 complex bound to a donor and an acceptor peptide at 3.2-A resolution, showing that each subunit contains 11 transmembrane helices and a lumenal beta-trefoil fold termed the MIR domain. The transmembrane domains of Pmt1 and Pmt2 share a structural fold with the catalytic subunits of oligosaccharyltransferases.
Title: Structure of the eukaryotic protein O-mannosyltransferase Pmt1-Pmt2 complex.
Translational effects of Dom34 required the 5'-UTR of the PMT1 transcript, which bound recombinant Dom34 directly at a CA/AC-rich sequence and regulated in vitro translation. Polysomal profiling revealed that Dom34 stimulates general translation moderately, but that it is especially required for translation of transcripts encoding Pmt isoforms 1, 4 and 6.
Title: Dom34 Links Translation to Protein O-mannosylation.
PMT1 deficiency enhances basal activity of the ER UPR and extends the RLS of yeast mother cells through a mechanism that requires both IRE1 and HAC1.
Title: PMT1 deficiency enhances basal UPR activity and extends replicative lifespan of Saccharomyces cerevisiae.
Pmt1-Pmt2 Complexes Are Associated with the Translocon Complex in Vivo.
Title: Protein O-mannosyltransferases associate with the translocon to modify translocating polypeptide chains.
Mtl1 O-mannosylation mediated by both Pmt1 and Pmt2 is important for cell survival under oxidative conditions and TOR blockade.
Title: Mtl1 O-mannosylation mediated by both Pmt1 and Pmt2 is important for cell survival under oxidative conditions and TOR blockade.
Gas1*p is a substrate for the Pmt1p-Pmt2p complex and is degraded by the ER-associated protein degradation pathway.
Title: Protein O-mannosyltransferases participate in ER protein quality control.

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Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables dolichyl-phosphate-mannose-protein mannosyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables dolichyl-phosphate-mannose-protein mannosyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables dolichyl-phosphate-mannose-protein mannosyltransferase activity	IEA Inferred from Electronic Annotation more info
enables dolichyl-phosphate-mannose-protein mannosyltransferase activity	IGI Inferred from Genetic Interaction more info	PubMed
enables dolichyl-phosphate-mannose-protein mannosyltransferase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables glycosyltransferase activity	IEA Inferred from Electronic Annotation more info
enables mannosyltransferase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in ERAD pathway	IGI Inferred from Genetic Interaction more info	PubMed
involved_in ERAD pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein O-linked glycosylation	IEA Inferred from Electronic Annotation more info
involved_in protein O-linked mannosylation	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein O-linked mannosylation	IDA Inferred from Direct Assay more info	PubMed
involved_in protein O-linked mannosylation	IGI Inferred from Genetic Interaction more info	PubMed
involved_in protein O-linked mannosylation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein exit from endoplasmic reticulum	IGI Inferred from Genetic Interaction more info	PubMed
involved_in protein glycosylation	IEA Inferred from Electronic Annotation more info
involved_in regulation of endoplasmic reticulum unfolded protein response	IGI Inferred from Genetic Interaction more info	PubMed
involved_in regulation of endoplasmic reticulum unfolded protein response	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt2p dimer complex	IDA Inferred from Direct Assay more info	PubMed
part_of dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt2p dimer complex	IPI Inferred from Physical Interaction more info	PubMed
part_of dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt3p dimer complex	IDA Inferred from Direct Assay more info	PubMed
located_in endoplasmic reticulum	HDA more info	PubMed
is_active_in endoplasmic reticulum	IBA Inferred from Biological aspect of Ancestor more info
located_in endoplasmic reticulum	IEA Inferred from Electronic Annotation more info
located_in endoplasmic reticulum membrane	IEA Inferred from Electronic Annotation more info
located_in membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: dolichyl-phosphate-mannose-protein mannosyltransferase PMT1

NP_010188.1

EC 2.4.1.109

Protein O-mannosyltransferase of the ER membrane; transfers mannose from dolichyl phosphate-D-mannose to protein serine and threonine residues; 1 of 7 related proteins involved in O-glycosylation which is essential for cell wall rigidity; functions as a heterodimer with Pmt2p but can also pair with Pmt3p; involved in ER quality control; amino terminus faces cytoplasm, carboxyl terminus faces ER lumen

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001136.10 Reference assembly

Range

287059..289512

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001180154.1 → NP_010188.1 TPA: dolichyl-phosphate-mannose-protein mannosyltransferase PMT1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_010188.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VRQ4, P33775

UniProtKB/TrEMBL

G2WC68

Conserved Domains (1) summary

COG1928
Location:26 → 733

PMT1; Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones]