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    PDI1 protein disulfide isomerase PDI1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 850314, updated on 9-Dec-2024

    Summary

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    Official Symbol
    PDI1
    Official Full Name
    protein disulfide isomerase PDI1
    Primary source
    SGD:S000000548
    Locus tag
    YCL043C
    See related
    AllianceGenome:SGD:S000000548; FungiDB:YCL043C; VEuPathDB:YCL043C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Also known as
    MFP1; TRG1
    Summary
    Enables protein disulfide isomerase activity; protein-disulfide reductase activity; and unfolded protein binding activity. Involved in mannose trimming involved in glycoprotein ERAD pathway and protein folding. Located in endoplasmic reticulum lumen. Human ortholog(s) of this gene implicated in Cole-Carpenter syndrome and autoimmune hepatitis. Orthologous to several human genes including PDIA3 (protein disulfide isomerase family A member 3). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See PDI1 in Genome Data Viewer
    Location:
    chromosome: III
    Exon count:
    1
    Sequence:
    Chromosome: III; NC_001135.5 (48653..50221, complement)

    Chromosome III - NC_001135.5Genomic Context describing neighboring genes Neighboring gene Emc1p Neighboring gene Mgr1p Neighboring gene uncharacterized protein Neighboring gene glucokinase Neighboring gene glucose-induced degradation complex subunit GID7

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001135.5

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Tian G, et al. Cell, 2006 Jan 13. PMID 16413482
    2. Functional analysis of the CXXC motif using phage antibodies that cross-react with protein disulphide-isomerase family proteins. Kimura T, et al. Biochem J, 2004 Aug 15. PMID 15137910, Free PMC Article
    3. Combination of the human prolyl isomerase FKBP12 with unrelated chaperone domains leads to chimeric folding enzymes with high activity. Geitner AJ, et al. J Mol Biol, 2012 Jul 20. PMID 22542528
    4. Studies on the function of yeast protein disulfide isomerase in renaturation of proteins. Katiyar S, et al. Biochim Biophys Acta, 2001 Jul 9. PMID 11451437
    5. Sulfhydryl oxidation, not disulfide isomerization, is the principal function of protein disulfide isomerase in yeast Saccharomyces cerevisiae. Solovyov A, et al. J Biol Chem, 2004 Aug 13. PMID 15175335

    See all (132) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The results suggest that PDI flexibility enables it to interact with many different partner molecules of widely different sizes and shapes.
      Title: The flexibility and dynamics of protein disulfide isomerase.
    2. Data show that binding of mannosidase Htm1 to protein disulfide isomerase Pdi1 is required for endoplasmic reticulum (ER)-associated protein degradation (ERAD).
      Title: A Complex of Htm1 and the Oxidoreductase Pdi1 Accelerates Degradation of Misfolded Glycoproteins.
    3. ERO1 is enzymatically active even with its regulatory disulfides intact, and further activation of ERO1 by reduction of the regulatory disulfides requires the reduction of non-catalytic Cys(90)-Cys(97)disulfide in PDI1.
      Title: Novel Roles of the Non-catalytic Elements of Yeast Protein-disulfide Isomerase in Its Interplay with Endoplasmic Reticulum Oxidoreductin 1.
    4. Coexpression of Kar2p, Pdi1p and Ero1p gave a synergistic effect on CPY expression
      Title: Effects of signal sequences and folding accessory proteins on extracellular expression of carboxypeptidase Y in recombinant Saccharomyces cerevisiae.
    5. Pdi1p is the key regulator of Ero1p activity.
      Title: Balanced Ero1 activation and inactivation establishes ER redox homeostasis.
    6. analysis of the oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum
      Title: Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum.
    7. The introduction of PDI improves secretory proteins in Pichia pastoris secretion 4-7 times, which may act synergistically to increase recombinant protein yields.
      Title: Enhanced secretion of heterologous proteins in Pichia pastoris following overexpression of Saccharomyces cerevisiae chaperone proteins.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables isomerase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein disulfide isomerase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables protein disulfide isomerase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein disulfide isomerase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein disulfide isomerase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables protein-disulfide reductase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables unfolded protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in mannose trimming involved in glycoprotein ERAD pathway IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in mannose trimming involved in glycoprotein ERAD pathway IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in mannose trimming involved in glycoprotein ERAD pathway IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein alpha-1,2-demannosylation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein folding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein folding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in response to endoplasmic reticulum stress IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Component Evidence Code Pubs
    located_in endoplasmic reticulum HDA 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 lumen IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in endoplasmic reticulum lumen IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    protein disulfide isomerase PDI1
    NP_009887.1
    • Protein disulfide isomerase; multifunctional oxidoreductase of the ER lumen, essential for disulfide bond formation in secretory and cell-surface proteins, processing of non-native disulfide bonds; Ero1p activator; complexes with exomannosidase, Mnl1p to facilitate the recognition of misfolded glycoproteins and the trimming of glycan Man8GlcNAc2 to Man7GlcNAc2 on substrates, thereby accelerating ERAD; PDI1 has a paralog, EUG1, that arose from the whole genome duplication

    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

    1. NC_001135.5 Reference assembly

      Range
      48653..50221 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001178688.1 → NP_009887.1  TPA: protein disulfide isomerase PDI1 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_009887.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VQX3, P17967
      UniProtKB/TrEMBL
      B3LU41, N1P7R5
      Conserved Domains (1) summary
      TIGR01130
      Location:32 → 492
      ER_PDI_fam; protein disulfide isomerase, eukaryotic
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P17967.2

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