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PDI1/YCL043C Single Page Format

This page provides an alternative format to the SGD Locus Summary Page. Note that additional information may be available on or linked from the standard format SGD Locus Summary page.

Contents

Names and Identifiers GO Annotations Pathways Summary Paragraph Mutant Phenotypes Interactions Homologs Protein Info (physical properties, transcript info) PDB Homologs (protein structure info) Motifs Genome-wide Expression (and other large-scale analyses) Locus History (misc. notes) Sequence Retrieval and Analysis Map and Displays Localization Community Annotation Literature Guide

Sequence Coordinates   ChrIII: 50221 to 48653 CDS: 50221 - 48653 Click on map for expanded view SGD ORF map GBrowse

SGD Locus Page

Names and Identifiers [TOP] [NEXT]
Standard Name	Systematic Name	Alias	Feature Type	SGDID
PDI1	YCL043C	MFP1, TRG1	ORF, Verified	S000000548
Description
Protein disulfide isomerase, multifunctional protein resident in the endoplasmic reticulum lumen, essential for the formation of disulfide bonds in secretory and cell-surface proteins, unscrambles non-native disulfide bonds

GO Annotations [TOP] [NEXT]
Molecular Function Annotation(s) Reference(s) Evidence Assigned By isomerase activity DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR005788 , EBI:IPR005792 Assigned on 2007-05-23 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0413 Assigned on 2007-05-23 UniProtKB protein disulfide isomerase activity Norgaard P, et al. (2001) Functional differences in yeast protein disulfide isomerases. J Cell Biol 152(3):553-62        IMP : Inferred from Mutant Phenotype Assigned on 2002-06-06 SGD Kimura T, et al. (2005) Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their Activities. J Biol Chem 280(36):31438-41        IDA : Inferred from Direct Assay Assigned on 2006-08-18 SGD Tian G, et al. (2006) The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Cell 124(1):61-73        IDA : Inferred from Direct Assay Assigned on 2006-02-10 SGD GOA curators and MGI curators (2001) Gene Ontology annotation based on Enzyme Commission mapping.      IEA : Inferred from Electronic Annotation with IUBMB:5.3.4.1 Assigned on 2007-05-23 UniProtKB protein disulfide oxidoreductase activity Solovyov A, et al. (2004) Sulfhydryl oxidation, not disulfide isomerization, is the principal function of protein disulfide isomerase in yeast Saccharomyces cerevisiae. J Biol Chem 279(33):34095-100        IDA : Inferred from Direct Assay Assigned on 2006-08-18 SGD Kimura T, et al. (2005) Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their Activities. J Biol Chem 280(36):31438-41        IDA : Inferred from Direct Assay Assigned on 2006-08-18 SGD
Biological Process Annotation(s) Reference(s) Evidence Assigned By cell redox homeostasis DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR006662 , EBI:IPR013766 , EBI:IPR017936 , EBI:IPR017937 Assigned on 2007-05-23 UniProtKB Huttenhower C and Troyanskaya OG (2009) Prediction of Gene Ontology annotations by integrating high-throughput datasets    RCA : Reviewed Computational Analysis Assigned on 2009-08-06 bioPIXIE_MEFIT cellular carbohydrate metabolic process Huttenhower C and Troyanskaya OG (2009) Prediction of Gene Ontology annotations by integrating high-throughput datasets    RCA : Reviewed Computational Analysis Assigned on 2009-08-06 bioPIXIE_MEFIT protein folding Norgaard P, et al. (2001) Functional differences in yeast protein disulfide isomerases. J Cell Biol 152(3):553-62        IMP : Inferred from Mutant Phenotype Assigned on 2002-06-07 SGD
Cellular Component Annotation(s) Reference(s) Evidence Assigned By endoplasmic reticulum DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR005792 Assigned on 2009-10-01 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0256 Assigned on 2009-10-01 UniProtKB endoplasmic reticulum lumen Gunther R, et al. (1991) The Saccharomyces cerevisiae TRG1 gene is essential for growth and encodes a lumenal endoplasmic reticulum glycoprotein involved in the maturation of vacuolar carboxypeptidase. J Biol Chem 266(36):24557-63      IDA : Inferred from Direct Assay Assigned on 2006-08-18 SGD GOA curators and UniProt curators (2007) Gene Ontology annotation based on Swiss-Prot Subcellular Location vocabulary mapping.      IEA : Inferred from Electronic Annotation with EBI:SL-0096 Assigned on 2008-02-13 UniProtKB

Pathways [TOP] [NEXT]
No pathways available

Summary Paragraph [TOP] [NEXT]
No summary paragraph available

Basic References [TOP]

BASIC INFORMATION REFERENCES forPDI1/YCL043C for PDI1 1) Farquhar R, et al. (1991) Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae. Gene 108(1):81-9      2) Laboissiere MC, et al. (1995) The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J Biol Chem 270(47):28006-9        3) Sevier CS, et al. (2001) A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation. Nat Cell Biol 3(10):874-82        4) Noiva R and Lennarz WJ (1992) Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum. J Biol Chem 267(6):3553-6      5) Mizunaga T, et al. (1990) Purification and characterization of yeast protein disulfide isomerase. J Biochem 108(5):846-51

Mutant Phenotypes [TOP] [NEXT]
Phenotype page for PDI1/YCL043C

Interactions: genetic, physical, and other gene-gene links. [TOP] [NEXT]
Interaction page for PDI1/YCL043C

Homologs [TOP] [NEXT]
Comparison Resources PSI-BLAST Results Ashbya Homologs (AGD) BLASTN vs. fungi BLASTP at NCBI BLASTP vs. fungi Candida Homologs (CGD) Candida Homologs (CandidaDB) Fungal Alignment Fungal Orthogroups Repository Ortholog Search (P-POD) PhylomeDB Synteny Viewer Yeast Gene Order Browser (YGOB) eukarYotic OrtholoGY (YOGY)

Physical Properties and Transcript Information: predicted from sequence [TOP] [NEXT]

Protein Sequence Calculations from Predicted Full length Translation N-term MKFSAGA C-term DAIHDEL Length(aa) 522 MW(Da) 58,227 pI 4.22 Amino Acid Composition (full length) GCG tools: PepPlot, Helical Wheel, PepStruct Transcript Translation Calculations Codon Bias 0.481   Codon Adaptation Index 0.404   Frequency of Optimal Codons 0.695   Hydropathicity of Protein -0.248   Aromaticity Score 0.107

10 20 30 40 50 | | | | | MKFSAGAVLSWSSLLLASSVFAQQEAVAPEDSAVVKLATDSFNEYIQSHD LVLAEFFAPWCGHCKNMAPEYVKAAETLVEKNITLAQIDCTENQDLCMEH NIPGFPSLKIFKNSDVNNSIDYEGPRTAEAIVQFMIKQSQPAVAVVADLP AYLANETFVTPVIVQSGKIDADFNATFYSMANKHFNDYDFVSAENADDDF KLSIYLPSAMDEPVVYNGKKADIADADVFEKWLQVEALPYFGEIDGSVFA QYVESGLPLGYLFYNDEEELEEYKPLFTELAKKNRGLMNFVSIDARKFGR HAGNLNMKEQFPLFAIHDMTEDLKYGLPQLSEEAFDELSDKIVLESKAIE SLVKDFLKGDASPIVKSQEIFENQDSSVFQLVGKNHDEIVNDPKKDVLVL YYAPWCGHCKRLAPTYQELADTYANATSDVLIAKLDHTENDVRGVVIEGY PTIVLYPGGKKSESVVYQGSRSLDSLFDFIKENGHFDVDGKALYEEAQEK AAEEADADAELADEEDAIHDEL*

Protein Structures from PDB: proteins of known structure with sequence similarity to PDI1/YCL043C, based on Smith-Waterman analysis. [TOP] [NEXT]

PDB protein structure(s) homologous to PDI1 Homolog Source (per PDB) Protein Alignment: PDI1 vs. Homolog External Links P-Value %Identical %Similar Alignment 3boa ( Chain: A) Crystal structure of yeast protein disulfide isomerase. PDB_Info PDB_Structure Saccharomyces cerevisiae 2.3e-205 100 0 View alignment SCOP MMDB CATH 2b5e ( Chain: A) Crystal structure of yeast protein disulfide isomerase PDB_Info PDB_Structure Saccharomyces cerevisiae 2.3e-205 100 0 View alignment SCOP MMDB CATH 3f8u ( Chain: A, C) Tapasin/erp57 heterodimer PDB_Info PDB_Structure Homo sapiens Chain A = 5.2e-36 30 30 View alignment SCOP MMDB CATH Chain C = 5.2e-36 30 30 View alignment 2djj ( Chain: A) Solution structure of the a' domain of thermophilic fungal protein disulfide isomerase PDB_Info PDB_Structure Humicola insolens 2.4e-17 53 25 View alignment SCOP MMDB CATH 2r2j ( Chain: A) Crystal structure of human erp44 PDB_Info PDB_Structure Homo sapiens 2.1e-16 25 32 View alignment SCOP MMDB CATH 2alb ( Chain: A) Nmr structure of the n-terminal domain a of the glycoprotein chaperone erp57 PDB_Info PDB_Structure Synthetic: yes; other_details: this sequence occurs naturally in humans 1.3e-15 46 29 View alignment SCOP MMDB CATH 2dj2 ( Chain: A) The solution structure of the second thioredoxin domain of mouse protein disulfide-isomerase a4 PDB_Info PDB_Structure Mus musculus 3.4e-15 45 34 View alignment SCOP MMDB CATH 2dmm ( Chain: A) The solution structure of the second thioredoxin domain of human protein disulfide-isomerase a3 PDB_Info PDB_Structure Homo sapiens 2.1e-14 41 33 View alignment SCOP MMDB CATH 1mek ( Chain: A) Human protein disulfide isomerase, nmr, 40 structures PDB_Info PDB_Structure Homo sapiens 2.3e-14 42 33 View alignment SCOP MMDB CATH 2dj3 ( Chain: A) The solution structure of the third thioredoxin domain of mouse protein disulfide-isomerase a4 PDB_Info PDB_Structure Mus musculus 2.6e-14 47 26 View alignment SCOP MMDB CATH 1x5c ( Chain: A) The solution structure of the second thioredoxin-like domain of human protein disulfide-isomerase PDB_Info PDB_Structure Homo sapiens 1.2e-13 41 37 View alignment SCOP MMDB CATH 2djk ( Chain: A) Solution structure of the b' domain of thermophilic fungal protein disulfide isomerase PDB_Info PDB_Structure Humicola insolens 6.1e-13 37 31 View alignment SCOP MMDB CATH 2dj1 ( Chain: A) The solution structure of the first thioredoxin domain of mouse protein disulfide-isomerase a4 PDB_Info PDB_Structure Mus musculus 2.9e-12 41 31 View alignment SCOP MMDB CATH 1x5d ( Chain: A) The solution structure of the second thioredoxin-like domain of human protein disulfide-isomerase a6 PDB_Info PDB_Structure Homo sapiens 1.3e-11 43 31 View alignment SCOP MMDB CATH 2dml ( Chain: A) The solution structure of the first thioredoxin domain of mouse protein disulfide-isomerase a6 PDB_Info PDB_Structure Mus musculus 5.9e-11 43 33 View alignment SCOP MMDB CATH 2diz ( Chain: A) The solution structure of the third thioredoxin domain of human thioredoxin domain-containing protein 5 PDB_Info PDB_Structure Homo sapiens 9.7e-09 40 27 View alignment SCOP MMDB CATH 3ed3 ( Chain: A, B) Crystal structure of the yeast dithiol/disulfide oxidoreductase mpd1p PDB_Info PDB_Structure Saccharomyces cerevisiae Chain A = 9.8e-09 27 28 View alignment SCOP MMDB CATH Chain B = 9.8e-09 27 28 View alignment 2gzy ( Chain: A) Solution structures of the reduced form of thioredoxin from bacillus subtilis PDB_Info PDB_Structure Bacillus subtilis 1.9e-05 33 37 View alignment SCOP MMDB CATH 2gzz ( Chain: A) Solution structures of the oxidized form of thioredoxin from bacillus subtilis PDB_Info PDB_Structure Bacillus subtilis 1.9e-05 33 37 View alignment SCOP MMDB CATH 1syr ( Chain: G, D, K, L, F, A, H, B, J, C, E, I) Initial structural analysis of plasmodium falciparum thioredoxin PDB_Info PDB_Structure Plasmodium falciparum 3D7 Chain G = 2.8e-05 32 42 View alignment SCOP MMDB CATH Chain D = 2.8e-05 32 42 View alignment Chain K = 2.8e-05 32 42 View alignment Chain L = 2.8e-05 32 42 View alignment Chain F = 2.8e-05 32 42 View alignment Chain A = 2.8e-05 32 42 View alignment Chain H = 2.8e-05 32 42 View alignment Chain B = 2.8e-05 32 42 View alignment Chain J = 2.8e-05 32 42 View alignment Chain C = 2.8e-05 32 42 View alignment Chain E = 2.8e-05 32 42 View alignment Chain I = 2.8e-05 32 42 View alignment 2fd3 ( Chain: A, B) Crystal structure of thioredoxin mutant p34h PDB_Info PDB_Structure Escherichia coli Chain A = 3.5e-05 33 36 View alignment SCOP MMDB CATH Chain B = 3.5e-05 33 36 View alignment 1nw2 ( Chain: D, C, E, A, G, H, F, B) The crystal structure of the mutant r82e of thioredoxin from alicyclobacillus acidocaldarius PDB_Info PDB_Structure Alicyclobacillus acidocaldarius Chain D = 5.5e-05 33 35 View alignment SCOP MMDB CATH Chain C = 5.5e-05 33 35 View alignment Chain E = 5.5e-05 33 35 View alignment Chain A = 5.5e-05 33 35 View alignment Chain G = 5.5e-05 33 35 View alignment Chain H = 5.5e-05 33 35 View alignment Chain F = 5.5e-05 33 35 View alignment Chain B = 5.5e-05 33 35 View alignment 1rqm ( Chain: A) Solution structure of the k18g/r82e alicyclobacillus acidocaldarius thioredoxin mutant PDB_Info PDB_Structure Alicyclobacillus acidocaldarius 5.5e-05 33 35 View alignment SCOP MMDB CATH 1x5e ( Chain: A) The solution structure of the thioredoxin-like domain of human thioredoxin-related transmembrane protein PDB_Info PDB_Structure Homo sapiens 6.0e-05 27 35 View alignment SCOP MMDB CATH 1nsw ( Chain: D, A, B, C) The crystal structure of the k18g mutant of the thioredoxin from alicyclobacillus acidocaldarius PDB_Info PDB_Structure Alicyclobacillus acidocaldarius Chain D = 8.6e-05 33 34 View alignment SCOP MMDB CATH Chain A = 8.6e-05 33 34 View alignment Chain B = 8.6e-05 33 34 View alignment Chain C = 8.6e-05 33 34 View alignment 1quw ( Chain: A) Solution structure of the thioredoxin from bacillus acidocaldarius PDB_Info PDB_Structure Alicyclobacillus acidocaldarius 8.6e-05 33 34 View alignment SCOP MMDB CATH 2h72 ( Chain: B, A) Crystal structure of thioredoxin mutant e85d in hexagonal (p61) space group PDB_Info PDB_Structure Escherichia coli Chain B = 8.8e-05 33 35 View alignment SCOP MMDB CATH Chain A = 8.8e-05 33 35 View alignment 2h71 ( Chain: A, B) Crystal structure of thioredoxin mutant d47e in hexagonal (p61) space group PDB_Info PDB_Structure Escherichia coli Chain A = 0.000120 33 35 View alignment SCOP MMDB CATH Chain B = 0.000120 33 35 View alignment 2ipa ( Chain: A) Solution structure of trx-arsc complex PDB_Info PDB_Structure Bacillus subtilis 0.000149 32 37 View alignment SCOP MMDB CATH 1xwc ( Chain: A) Drosophila thioredoxin, reduced, p6522 PDB_Info PDB_Structure Drosophila melanogaster 0.000160 36 37 View alignment SCOP MMDB CATH 1xw9 ( Chain: D, A, B, C) Drospohila thioredoxin, oxidized, p21 PDB_Info PDB_Structure Drosophila melanogaster Chain D = 0.000160 36 37 View alignment SCOP MMDB CATH Chain A = 0.000160 36 37 View alignment Chain B = 0.000160 36 37 View alignment Chain C = 0.000160 36 37 View alignment 1xwb ( Chain: C, A, D, B) Drospohila thioredoxin, oxidized, p42212 PDB_Info PDB_Structure Drosophila melanogaster Chain C = 0.000160 36 37 View alignment SCOP MMDB CATH Chain A = 0.000160 36 37 View alignment Chain D = 0.000160 36 37 View alignment Chain B = 0.000160 36 37 View alignment 1xwa ( Chain: D, C, A, B) Drospohila thioredoxin, oxidized, p41212 PDB_Info PDB_Structure Drosophila melanogaster Chain D = 0.000169 36 37 View alignment SCOP MMDB CATH Chain C = 0.000169 36 37 View alignment Chain A = 0.000169 36 37 View alignment Chain B = 0.000169 36 37 View alignment 2voc ( Chain: A, B) Thioredoxin a active site mutants form mixed disulfide dimers that resemble enzyme-substrate reaction intermediate PDB_Info PDB_Structure Bacillus subtilis Chain A = 0.000169 32 37 View alignment SCOP MMDB CATH Chain B = 0.000169 32 37 View alignment 2ppt ( Chain: A, B) Crystal structure of thioredoxin-2 PDB_Info PDB_Structure Rhodobacter capsulatus Chain A = 0.000169 36 29 View alignment SCOP MMDB CATH Chain B = 0.000169 36 29 View alignment 2h73 ( Chain: A, B) Crystal structure of thioredoxin mutant d43e in hexagonal (p61) space group PDB_Info PDB_Structure Escherichia coli Chain A = 0.000190 32 36 View alignment SCOP MMDB CATH Chain B = 0.000190 32 36 View alignment 3dxb ( Chain: H, A, B, D, E, G, F, C) Structure of the uhm domain of puf60 fused to thioredoxin PDB_Info PDB_Structure Escherichia coli O157:H7 Chain H = 0.000200 32 35 View alignment SCOP MMDB CATH Chain A = 0.000200 32 35 View alignment Chain B = 0.000200 32 35 View alignment Chain D = 0.000200 32 35 View alignment Chain E = 0.000200 32 35 View alignment Chain G = 0.000200 32 35 View alignment Chain F = 0.000200 32 35 View alignment Chain C = 0.000200 32 35 View alignment 1dby ( Chain: A) Nmr structures of chloroplast thioredoxin m ch2 from the green alga chlamydomonas reinhardtii PDB_Info PDB_Structure Chlamydomonas reinhardtii 0.000210 35 32 View alignment SCOP MMDB CATH 1x9s ( Chain: B) T7 dna polymerase in complex with a primer/template dna containing a disordered n-2 aminofluorene on the template, crystallized with dideoxy-ctp as the incoming nucleotide. PDB_Info PDB_Structure Enterobacteria phage t7 | Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 1x9w ( Chain: B) T7 dna polymerase in complex with a primer/template dna containing a disordered n-2 aminofluorene on the template, crystallized with dideoxy-atp as the incoming nucleotide. PDB_Info PDB_Structure Enterobacteria phage t7 | Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 2eiq ( Chain: B, A) Design of disulfide-linked thioredoxin dimers and multimers through analysis of crystal contacts PDB_Info PDB_Structure Escherichia coli Chain B = 0.000219 32 36 View alignment SCOP MMDB CATH Chain A = 0.000219 32 36 View alignment 1zyq ( Chain: B) T7 dna polymerase in complex with 8og and incoming ddatp PDB_Info PDB_Structure Enterobacteria phage t7 | Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 1skr ( Chain: B) T7 dna polymerase complexed to dna primer/template and ddatp PDB_Info PDB_Structure Enterobacteria phage t7 | Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 2h74 ( Chain: A, B) Crystal structure of thioredoxin mutant d2e in hexagonal (p61) space group PDB_Info PDB_Structure Escherichia coli Chain A = 0.000219 32 36 View alignment SCOP MMDB CATH Chain B = 0.000219 32 36 View alignment 2ajq ( Chain: B, I) Strucuture of replicative dna polymerase provides insigts into the mechanisms for processivity, frameshifting and editing PDB_Info PDB_Structure Enterobacteria phage t7 | Escherichia coli Chain B = 0.000219 32 36 View alignment SCOP MMDB CATH Chain I = 0.000219 32 36 View alignment 2eio ( Chain: C, A, B, D) Design of disulfide-linked thioredoxin dimers and multimers through analysis of crystal contacts PDB_Info PDB_Structure Escherichia coli Chain C = 0.000219 32 36 View alignment SCOP MMDB CATH Chain A = 0.000219 32 36 View alignment Chain B = 0.000219 32 36 View alignment Chain D = 0.000219 32 36 View alignment 1xoa ( Chain: A) Thioredoxin (oxidized disulfide form), nmr, 20 structures PDB_Info PDB_Structure Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 2h6y ( Chain: A, B) Crystal structure of thioredoxin mutant e48d in hexagonal (p61) space group PDB_Info PDB_Structure Escherichia coli Chain A = 0.000219 32 36 View alignment SCOP MMDB CATH Chain B = 0.000219 32 36 View alignment 2h70 ( Chain: B, A) Crystal structure of thioredoxin mutant d9e in hexagonal (p61) space group PDB_Info PDB_Structure Escherichia coli Chain B = 0.000219 32 36 View alignment SCOP MMDB CATH Chain A = 0.000219 32 36 View alignment 1x9m ( Chain: B) T7 dna polymerase in complex with an n-2- acetylaminofluorene-adducted dna PDB_Info PDB_Structure Enterobacteria phage t7 | Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 2trx ( Chain: B, A) Crystal structure of thioredoxin from escherichia coli at 1.68 angstroms resolution PDB_Info PDB_Structure Escherichia coli Chain B = 0.000219 32 36 View alignment SCOP MMDB CATH Chain A = 0.000219 32 36 View alignment 2h6x ( Chain: B, A) Crystal structure of thioredoxin wild type in hexagonal (p61) space group PDB_Info PDB_Structure Escherichia coli Chain B = 0.000219 32 36 View alignment SCOP MMDB CATH Chain A = 0.000219 32 36 View alignment 1sl1 ( Chain: B) Binary 5' complex of t7 dna polymerase with a dna primer/template containing a cis-syn thymine dimer on the template PDB_Info PDB_Structure Enterobacteria phage t7 | Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 1tkd ( Chain: B) T7 dna polymerase ternary complex with 8 oxo guanosine and dcmp at the elongation site PDB_Info PDB_Structure Enterobacteria phage t7 | Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 1tk5 ( Chain: B) T7 dna polymerase binary complex with 8 oxo guanosine in the templating strand PDB_Info PDB_Structure Enterobacteria phage t7 | Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 1sl2 ( Chain: B) Ternary 5' complex of t7 dna polymerase with a dna primer/template containing a cis-syn thymine dimer on the template and an incoming nucleotide PDB_Info PDB_Structure Enterobacteria phage t7 | Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 2eir ( Chain: D, A, C, B) Design of disulfide-linked thioredoxin dimers and multimers through analysis of crystal contacts PDB_Info PDB_Structure Escherichia coli Chain D = 0.000219 32 36 View alignment SCOP MMDB CATH Chain A = 0.000219 32 36 View alignment Chain C = 0.000219 32 36 View alignment Chain B = 0.000219 32 36 View alignment 1sl0 ( Chain: B, D) Ternary 3' complex of t7 dna polymerase with a dna primer/template containing a disordered cis-syn thymine dimer on the template and an incoming nucleotide PDB_Info PDB_Structure Enterobacteria phage t7 | Escherichia coli Chain B = 0.000219 32 36 View alignment SCOP MMDB CATH Chain D = 0.000219 32 36 View alignment 1t8e ( Chain: B) T7 dna polymerase ternary complex with dctp at the insertion site. PDB_Info PDB_Structure Enterobacteria phage t7 | Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 1tk8 ( Chain: B) T7 dna polymerase ternary complex with 8 oxo guanosine and damp at the elongation site PDB_Info PDB_Structure Enterobacteria phage t7 | Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 1sks ( Chain: B) Binary 3' complex of t7 dna polymerase with a dna primer/template containing a cis-syn thymine dimer on the template PDB_Info PDB_Structure Enterobacteria phage t7 | Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 1xob ( Chain: A) Thioredoxin (reduced dithio form), nmr, 20 structures PDB_Info PDB_Structure Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 1t7p ( Chain: B) T7 dna polymerase complexed to dna primer/template,a nucleoside triphosphate, and its processivity factor thioredoxin PDB_Info PDB_Structure Enterobacteria phage t7 | Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 1skw ( Chain: B) Binary 3' complex of t7 dna polymerase with a dna primer/template containing a disordered cis-syn thymine dimer on the template PDB_Info PDB_Structure Enterobacteria phage t7 | Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 2bto ( Chain: T) Structure of btuba from prosthecobacter dejongeii PDB_Info PDB_Structure Prosthecobacter dejongeii | Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 1tk0 ( Chain: B) T7 dna polymerase ternary complex with 8 oxo guanosine and ddctp at the insertion site PDB_Info PDB_Structure Enterobacteria phage t7 | Escherichia coli 0.000219 32 36 View alignment SCOP MMDB CATH 2h6z ( Chain: A, B) Crystal structure of thioredoxin mutant e44d in hexagonal (p61) space group PDB_Info PDB_Structure Escherichia coli Chain A = 0.000289 32 35 View alignment SCOP MMDB CATH Chain B = 0.000289 32 35 View alignment 2h75 ( Chain: A, B) Crystal structure of thioredoxin mutant d13e in hexagonal (p61) space group PDB_Info PDB_Structure Escherichia coli Chain A = 0.000289 32 36 View alignment SCOP MMDB CATH Chain B = 0.000289 32 36 View alignment 3dyr ( Chain: B, A) Crystal structure of e. coli thioredoxin mutant i76t in its oxidized form PDB_Info PDB_Structure Escherichia coli Chain B = 0.000299 32 35 View alignment SCOP MMDB CATH Chain A = 0.000299 32 35 View alignment 3h79 ( Chain: A) Thioredoxin-like protei PDB_Info PDB_Structure Unknown 0.000360 32 28 View alignment SCOP MMDB CATH 2j23 ( Chain: B, A) Cross-reactivity and crystal structure of malassezia sympodialis thioredoxin (mala s 13), a member of a new pan- allergen family PDB_Info PDB_Structure Malassezia sympodialis Chain B = 0.000390 25 39 View alignment SCOP MMDB CATH Chain A = 0.000390 25 39 View alignment 1zzy ( Chain: A, B) Crystal structure of thioredoxin mutant l7v PDB_Info PDB_Structure Escherichia coli Chain A = 0.000390 31 37 View alignment SCOP MMDB CATH Chain B = 0.000390 31 37 View alignment 2yzu ( Chain: A) Crystal structure of oxidized thioredoxin from thermus thermophilus hb8 PDB_Info PDB_Structure Thermus thermophilus HB8 0.000400 26 36 View alignment SCOP MMDB CATH 2cvk ( Chain: A) Crystal structure of thermus thermophilus thioredoxin PDB_Info PDB_Structure Thermus thermophilus 0.000400 26 36 View alignment SCOP MMDB CATH 2tir ( Chain: A) Crystal structure analysis of a mutant escherichia coli thioredoxin in which lysine 36 is replaced by glutamic acid PDB_Info PDB_Structure Escherichia coli 0.000460 31 37 View alignment SCOP MMDB CATH 1gl8 ( Chain: A) Solution structure of thioredoxin m from spinach, oxidized form PDB_Info PDB_Structure Spinacia oleracea 0.000510 31 34 View alignment SCOP MMDB CATH 1fb0 ( Chain: B, A) Crystal structure of thioredoxin m from spinach chloroplast (reduced form) PDB_Info PDB_Structure Spinacia oleracea Chain B = 0.000510 31 34 View alignment SCOP MMDB CATH Chain A = 0.000510 31 34 View alignment 1fb6 ( Chain: A, B) Crystal structure of thioredoxin m from spinach chloroplast (oxidized form) PDB_Info PDB_Structure Spinacia oleracea Chain A = 0.000510 31 34 View alignment SCOP MMDB CATH Chain B = 0.000510 31 34 View alignment 2h76 ( Chain: B, A) Crystal structure of thioredoxin mutant d10e in hexagonal (p61) space group PDB_Info PDB_Structure Escherichia coli Chain B = 0.000529 31 37 View alignment SCOP MMDB CATH Chain A = 0.000529 31 37 View alignment 2hsy ( Chain: A) Solution structure of thioredoxin 2 from saccharomyces cerevisiae PDB_Info PDB_Structure Saccharomyces cerevisiae 0.000590 36 28 View alignment SCOP MMDB CATH 2fa4 ( Chain: A, B) Crystal structure of oxidized form from saccharomyces cerevisiae PDB_Info PDB_Structure Saccharomyces cerevisiae Chain A = 0.000640 36 28 View alignment SCOP MMDB CATH Chain B = 0.000640 36 28 View alignment 1f9m ( Chain: A, B) Crystal structure of thioredoxin f from spinach chloroplast (short form) PDB_Info PDB_Structure Spinacia oleracea Chain A = 0.000649 33 28 View alignment SCOP MMDB CATH Chain B = 0.000649 33 28 View alignment 2fch ( Chain: F, E, C, D, A, B, G) Crystal structure of thioredoxin mutant g74s PDB_Info PDB_Structure Escherichia coli Chain F = 0.000720 31 37 View alignment SCOP MMDB CATH Chain E = 0.000720 31 37 View alignment Chain C = 0.000720 31 37 View alignment Chain D = 0.000720 31 37 View alignment Chain A = 0.000720 31 37 View alignment Chain B = 0.000720 31 37 View alignment Chain G = 0.000720 31 37 View alignment 1faa ( Chain: A) Crystal structure of thioredoxin f from spinach chloroplast (long form) PDB_Info PDB_Structure Spinacia oleracea 0.000739 33 28 View alignment SCOP MMDB CATH 2i1u ( Chain: A) Mycobacterium tuberculosis thioredoxin c PDB_Info PDB_Structure Mycobacterium tuberculosis 0.000830 30 32 View alignment SCOP MMDB CATH 1srx ( Chain: A) Three-dimensional structure of escherichia coli thioredoxin- s2 to 2.8 angstroms resolution PDB_Info PDB_Structure Escherichia coli B 0.000959 30 37 View alignment SCOP MMDB CATH 1tho ( Chain: A) Crystal structure of a mutant escherichia coli thioredoxin with an arginine insertion in the active site PDB_Info PDB_Structure Escherichia coli 0.000979 32 36 View alignment SCOP MMDB CATH 2e0q ( Chain: A) Crystal structure of k53e thioredoxin from sulfolobus tokodaii strain7 PDB_Info PDB_Structure Sulfolobus tokodaii 0.001400 25 41 View alignment SCOP MMDB CATH 1t00 ( Chain: A) The structure of thioredoxin from s. coelicolor PDB_Info PDB_Structure Streptomyces coelicolor A3(2) 0.001400 28 39 View alignment SCOP MMDB CATH 1txx ( Chain: A) Active-site variant of e.coli thioredoxin PDB_Info PDB_Structure Escherichia coli 0.001500 31 36 View alignment SCOP MMDB CATH 1keb ( Chain: B, A) Crystal structure of double mutant m37l,p40s e.coli thioredoxin PDB_Info PDB_Structure Escherichia coli Chain B = 0.001500 31 36 View alignment SCOP MMDB CATH Chain A = 0.001500 31 36 View alignment 1f6m ( Chain: D, C, H, G) Crystal structure of a complex between thioredoxin reductase, thioredoxin, and the nadp+ analog, aadp+ PDB_Info PDB_Structure Escherichia coli Chain D = 0.001700 31 36 View alignment SCOP MMDB CATH Chain C = 0.001700 31 36 View alignment Chain H = 0.001700 31 36 View alignment Chain G = 0.001700 31 36 View alignment 1w89 ( Chain: F, E, C, A, B, D) Structure of the reduced form of human thioredoxin 2 PDB_Info PDB_Structure Homo sapiens Chain F = 0.001999 25 37 View alignment SCOP MMDB CATH Chain E = 0.001999 25 37 View alignment Chain C = 0.001999 25 37 View alignment Chain A = 0.001999 25 37 View alignment Chain B = 0.001999 25 37 View alignment Chain D = 0.001999 25 37 View alignment 1uvz ( Chain: A, D, F, B, E, C) Structure of human thioredoxin 2 PDB_Info PDB_Structure Homo sapiens Chain A = 0.001999 25 37 View alignment SCOP MMDB CATH Chain D = 0.001999 25 37 View alignment Chain F = 0.001999 25 37 View alignment Chain B = 0.001999 25 37 View alignment Chain E = 0.001999 25 37 View alignment Chain C = 0.001999 25 37 View alignment 2o87 ( Chain: A) S. aureus thioredoxin p31s mutant PDB_Info PDB_Structure Staphylococcus aureus 0.001999 36 30 View alignment SCOP MMDB CATH 1m7t ( Chain: A) Solution structure and dynamics of the human-escherichia coli thioredoxin chimera: insights into thermodynamic stability PDB_Info PDB_Structure Homo sapiens, escherichia coli 0.001999 35 33 View alignment SCOP MMDB CATH 1w4v ( Chain: A, C, E, F, D, B) Structure of the oxidised form of human thioredoxin 2 PDB_Info PDB_Structure Homo sapiens Chain A = 0.001999 25 37 View alignment SCOP MMDB CATH Chain C = 0.001999 25 37 View alignment Chain E = 0.001999 25 37 View alignment Chain F = 0.001999 25 37 View alignment Chain D = 0.001999 25 37 View alignment Chain B = 0.001999 25 37 View alignment 2o8v ( Chain: B) Paps reductase in a covalent complex with thioredoxin c35a PDB_Info PDB_Structure Escherichia coli 0.002200 31 36 View alignment SCOP MMDB CATH 2o7k ( Chain: A) S. aureus thioredoxin PDB_Info PDB_Structure Staphylococcus aureus 0.002299 36 30 View alignment SCOP MMDB CATH 2o85 ( Chain: A) S. aureus thioredoxin p31t mutant PDB_Info PDB_Structure Staphylococcus aureus 0.002299 36 30 View alignment SCOP MMDB CATH 2i9h ( Chain: A) Nmr solution structure of the reduced form of thioredoxin 1 from yeast (trx1) PDB_Info PDB_Structure Saccharomyces cerevisiae 0.004001 32 32 View alignment SCOP MMDB CATH 2puk ( Chain: G, C) Crystal srtucture of the binary complex between ferredoxin: thioredoxin reductase and thioredoxin m PDB_Info PDB_Structure Synechocystis sp. | Spinacia oleracea Chain G = 0.004198 30 34 View alignment SCOP MMDB CATH Chain C = 0.004198 30 34 View alignment 2pvo ( Chain: C) Crystal srtucture of the ternary complex between thioredoxin f, ferredoxin, and ferredoxin: thioredoxin reductase PDB_Info PDB_Structure Synechocystis sp. | Spinacia oleracea 0.005097 32 28 View alignment SCOP MMDB CATH 2pu9 ( Chain: C) Crystal srtucture of the binary complex between ferredoxin: thioredoxin reductase and thioredoxin f PDB_Info PDB_Structure Synechocystis sp. | Spinacia oleracea 0.005097 32 28 View alignment SCOP MMDB CATH 1zcp ( Chain: B, D, C, A) Crystal structure of a catalytic site mutant e. coli trxa (caca) PDB_Info PDB_Structure Escherichia coli Chain B = 0.006697 30 37 View alignment SCOP MMDB CATH Chain D = 0.006697 30 37 View alignment Chain C = 0.006697 30 37 View alignment Chain A = 0.006697 30 37 View alignment 2oe1 ( Chain: B, A) Crystal structure of mitochondrial thioredoxin 3 from saccharomyces cerevisiae (reduced form) PDB_Info PDB_Structure Saccharomyces cerevisiae Chain B = 0.007197 23 42 View alignment SCOP MMDB CATH Chain A = 0.007197 23 42 View alignment 2oe0 ( Chain: A, B) Crystal structure of mitochondrial thioredoxin 3 from saccharomyces cerevisiae PDB_Info PDB_Structure Saccharomyces cerevisiae Chain A = 0.007197 23 42 View alignment SCOP MMDB CATH Chain B = 0.007197 23 42 View alignment 2oe3 ( Chain: B, A) Crystal structure of mitochondrial thioredoxin 3 from saccharomyces cerevisiae (oxidized form) PDB_Info PDB_Structure Saccharomyces cerevisiae Chain B = 0.007197 23 42 View alignment SCOP MMDB CATH Chain A = 0.007197 23 42 View alignment 2vim ( Chain: A) X-ray structure of fasciola hepatica thioredoxin PDB_Info PDB_Structure Fasciola hepatica 0.008599 29 42 View alignment SCOP MMDB CATH

Genome-wide Expression and Other Large-Scale Analyses [TOP] [NEXT]
Functional Analysis Expression Connection Summary Cell cycle and metabolic oscillation Cell cycle transcript profile Cyclebase Genevestigator GermOnline SPELL Microarray Search YGAC Triples Yeast Microarray Global Viewer YeastFunc	You can also search multiple datasets simultaneously using Expression Connection for expression studies or Function Junction for other large scale analyses.

Locus History (misc. notes) [TOP] [NEXT]

Nomenclature History

Standard Name	Reference
PDI1	SGD (2007) Information without a citation in SGD

Mapping Notes

Date	Note
1998-11-10	Edition 15: PDI1 has also been called YCL313 Cherry JM, et al. (1998) "Genetic and Physical Maps of Saccharomyces cerevisiae (Edition 15)". Pp. 414-420 in 1998 Yeast Genetics and Molecular Biology Meeting Program and Abstracts. Bethesda, MD: The Genetics Society of America

Sequence Retrieval [TOP] [NEXT]
Sequence Type	Output Format
Genomic DNA	GCG | FASTA | NoHeader
Genomic DNA with 1 kb up and downstream	GCG | FASTA | NoHeader
DNA coding sequence (without introns, without flanking regions)	GCG | FASTA | NoHeader
Protein Translation of ORF	GCG | FASTA | NoHeader
6-Frame Translation(with Restriction Map)	GCG
Restriction Fragment Sizes	GCG
Sequence Analysis Tools BLASTP BLASTN Design Primers FASTA aa FASTA nt Restriction Fragment Map Restriction Fragment Sizes Six-Frame Translation

Sequence from other databases
Sequence ID	Source
YCL043C	SGD Systematic Sequence
850314	NCBI: Gene ID
NP_009887.1	NCBI: RefSeq protein version ID
NP_009887.1	NCBI: RefSeq protein version ID
6319806	NCBI: NCBI protein GI

Map and Displays [TOP] [NEXT]
Physical, Genetic Maps:	Chromosomal Feature Map	GBrowse	Combined Physical and Genetic Map	Genetic Distance vs. Physical Distance Ratios
Similarity Viewers:	Synteny Viewer	Genomic Stripe View	SAGE Results Map

Localization [TOP] [NEXT]
Localization Resources YeastRC Localization (Seattle) Organelle DB (UMich) YGAC Triples YPL.db at Uni Graz YeastGFP DB (UCSF) at SGD

Community Annotation [TOP] [NEXT]
No community annotation available.

Literature Guide: papers categorized by topic. [TOP]
Topics	Reference	Other Genes Addressed
92 curated references; 0 references not yet curated
Mutants/Phenotypes Protein-protein Interactions Strains/Constructs	Clerc S, et al. (2009) Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum. J Cell Biol 184(1):159-72	|ALG12 |ALG3 |ALG8 |ALG9 |MNL1 |MNS1 |PRC1 |ROT2 |YOS9
Reviews	Hatahet F, et al. (2009) Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation. Antioxid Redox Signal 11(11):2807-50	|EPS1 |EUG1 |MPD1 |MPD2
Protein Processing/Modification/Regulation	Karhumaa K, et al. (2009) Proteome analysis of the xylose-fermenting mutant yeast strain TMB 3400. Yeast 26(7):371-82	|ALD4 |ALD6 |CYT1 |ENO2 |ILV5 |MEC1 |MRP8 |PDC1 |QCR2 |TDH1 |TIF34 |TKL1 |XYL2
Genetic Interactions Large-scale genetic interaction Mutants/Phenotypes Protein Sequence Features Regulation of	Kim JH, et al. (2009) The unfolded protein response is necessary but not sufficient to compensate for defects in disulfide isomerization. J Biol Chem 284(16):10400-8	|ALG8 |APM3 |APS3 |ARL1 |AVL9 |CCZ1 |CDC50 |COG8 |EPS1 |ERV41 |ERV46 |EUG1 |FLD1 |GCS1 |MORE
Fungal Related Genes/Proteins Non-Fungal Related Genes/Proteins Protein Sequence Features	Marino SM and Gladyshev VN (2009) A structure-based approach for detection of thiol oxidoreductases and their catalytic redox-active cysteine residues. PLoS Comput Biol 5(5):e1000383	|AHP1 |BET3 |CAP2 |DOT5 |EPS1 |ERO1 |ERV1 |ERV2 |EUG1 |GLR1 |GPX1 |GPX2 |GRX1 |GRX2 |MORE
Large-scale protein detection	Picotti P, et al. (2009) Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics. Cell 138(4):795-806	|ACH1 |ACO1 |ADH1 |ADH2 |ADH4 |ALD6 |ASP1 |CCT7 |CCT8 |CDC7 |CIT1 |CIT2 |CMR2 |ENO1 |MORE
Mutants/Phenotypes Protein Processing/Modification/Regulation Protein-protein Interactions Regulation of Strains/Constructs	Sakoh-Nakatogawa M, et al. (2009) Roles of Protein-disulfide Isomerase-mediated Disulfide Bond Formation of Yeast Mnl1p in Endoplasmic Reticulum-associated Degradation. J Biol Chem 284(18):11815-25	|MNL1
Mutants/Phenotypes Strains/Constructs	Breslow DK, et al. (2008) A comprehensive strategy enabling high-resolution functional analysis of the yeast genome. Nat Methods 5(8):711-8	|AAR2 |ABD1 |ABF1 |ACC1 |ACP1 |ADE13 |AFG2 |ALA1 |ALG1 |ALG13 |ALG14 |ALG2 |ALG7 |ALR1 |MORE
Protein Processing/Modification/Regulation	Kho CW, et al. (2008) Gpx3-dependent Responses Against Oxidative Stress in Saccharomyces cerevisiae. J Microbiol Biotechnol 18(2):270-82	|AHP1 |ARG1 |ASP1 |CCT5 |CIN2 |CSM4 |DAK1 |EFB1 |FRM2 |GPM3 |GUK1 |HYR1 |PEP4 |PUP3 |MORE
Protein-protein Interactions	Lee PY, et al. (2008) Interactome analysis of yeast glutathione peroxidase 3. J Microbiol Biotechnol 18(8):1364-7	|CAD1 |DAK1 |GLN1 |GRX2 |HYR1 |MXR1 |PTR3 |TDH2 |TFA1 |THI3 |YBP1
Protein Processing/Modification/Regulation Regulation of	Lee RE, et al. (2008) A non-death role of the yeast metacaspase: Yca1p alters cell cycle dynamics. PLoS ONE 3(8):e2956	|CDC19 |LIA1 |MCA1 |MRP8 |PEP4 |PST2 |PUP2 |RAD23 |SGT2 |TIF2
Protein-protein Interactions	Li Z, et al. (2008) Cdc34p Ubiquitin-Conjugating Enzyme Is a Component of the Tombusvirus Replicase Complex and Ubiquitinates p33 Replication Protein. J Virol 82(14):6911-26	|ALA1 |ARP8 |BFR1 |BUD21 |CDC34 |DBP3 |DDR48 |DOT1 |EFB1 |ELF1 |EMI2 |ERB1 |ERR2 |FMP40 |MORE
Mutants/Phenotypes Strains/Constructs	Merksamer PI, et al. (2008) Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions. Cell 135(5):933-47	|CYC1 |ERO1 |HAC1 |HRD1 |IRE1 |KAR2 |PRC1 |SEC61
Genetic Interactions	Mesecke N, et al. (2008) A Novel Group of Glutaredoxins in the cis-Golgi Critical for Oxidative Stress Resistance. Mol Biol Cell 19(6):2673-80	|ERO1 |GRX6 |GRX7 |GRX8
Function/Process Mutants/Phenotypes Protein Physical Properties Protein Sequence Features Protein/Nucleic Acid Structure Strains/Constructs	Tian G, et al. (2008) The Catalytic Activity of Protein-disulfide Isomerase Requires a Conformationally Flexible Molecule. J Biol Chem 283(48):33630-40
RNA Levels and Processing	Trott A, et al. (2008) Activation of Heat Shock and Antioxidant Responses by the Natural Product Celastrol: Transcriptional Signatures of a Thiol-targeted Molecule. Mol Biol Cell 19(3):1104-12	|AAD14 |AAD15 |AAD16 |AAD3 |AAD4 |AAD6 |ADH5 |ADH6 |AHP1 |ALD3 |ALD4 |ALD6 |ARI1 |ATR1 |MORE
Fungal Related Genes/Proteins Protein Sequence Features Protein/Nucleic Acid Structure	Vitu E, et al. (2008) Yeast Mpd1p reveals the structural diversity of the protein disulfide isomerase family. J Mol Biol 384(3):631-40	|MPD1
Non-Fungal Related Genes/Proteins Protein Processing/Modification/Regulation	Wang L, et al. (2008) Expression, purification and characterization of yeast protein disulfide isomerase produced by a recombinant baculovirus-mediated silkworm, Bombyx mori, pupae expression system. Biotechnol Lett 30(4):625-30
Regulation of Transcription	Zhang H, et al. (2008) The effect of calnexin deletion on the expression level of PDI in Saccharomyces cerevisiae under heat stress conditions. Cell Mol Biol Lett 13(1):38-48	|CNE1
Cross-species Expression Fungal Related Genes/Proteins	Gasser B, et al. (2007) Monitoring of transcriptional regulation in Pichia pastoris under protein production conditions. BMC Genomics 8:179	|HAC1
Cross-species Expression Fungal Related Genes/Proteins Industrial Applications Strains/Constructs	Gasser B, et al. (2007) Transcriptomics-based identification of novel factors enhancing heterologous protein secretion in yeasts. Appl Environ Microbiol 73(20):6499-507	|BFR2 |BMH2 |COG6 |COY1 |CUP5 |ERO1 |HAC1 |IMH1 |KAR2 |KIN2 |SEC31 |SSA4 |SSE1 |SSO2
Function/Process Mutants/Phenotypes Substrates/Ligands/Cofactors	Powers SL and Robinson AS (2007) PDI improves secretion of redox-inactive beta-glucosidase. Biotechnol Prog 23(2):364-9
Reviews	Boyce M and Yuan J (2006) Cellular response to endoplasmic reticulum stress: a matter of life or death. Cell Death Differ 13(3):363-73	|CDC48 |CUE1 |DER1 |GCN2 |GCN4 |HAC1 |HRD1 |HRD3 |IRE1 |KAR2 |SEC61 |UBC1 |UBC6 |UBC7
RNA Levels and Processing	Cullen PJ, et al. (2006) Genome-wide analysis of the response to protein glycosylation deficiency in yeast. FEMS Yeast Res 6(8):1264-73	|ACS1 |ADR1 |ALD6 |AMS1 |CHS1 |CHS3 |CHS7 |CLB1 |CLB2 |CLN1 |CLN2 |CLN3 |CTT1 |DER1 |MORE
Cross-species Expression Function/Process Techniques and Reagents	Gasser B, et al. (2006) Engineering of Pichia pastoris for improved production of antibody fragments. Biotechnol Bioeng 94(2):353-61	|HAC1
Reviews	Gruber CW, et al. (2006) Protein disulfide isomerase: the structure of oxidative folding. Trends Biochem Sci 31(8):455-64	|EPS1 |ERO1 |ERV2 |EUG1 |MPD1 |MPD2
Function/Process Mutants/Phenotypes Protein Sequence Features	Heiligenstein S, et al. (2006) Retrotranslocation of a viral A/B toxin from the yeast endoplasmic reticulum is independent of ubiquitination and ERAD. EMBO J 25(20):4717-27	|CDC48 |DSK2 |HRD1 |JEM1 |KAR2 |NPL4 |PMR1 |RAD23 |RSP5 |SCJ1 |SPF1 |UBC1 |UBC4 |UBC6 |MORE
Techniques and Reagents	Le Moan N, et al. (2006) The Saccharomyces cerevisiae proteome of oxidized protein thiols: contrasted functions for the thioredoxin and glutathione pathways. J Biol Chem 281(15):10420-30	|ACO1 |ADH1 |ADO1 |AHP1 |ALD6 |ASC1 |CCS1 |CDC19 |CDC48 |CPR1 |CPR6 |CYS4 |EFB1 |ENO1 |MORE
Strains/Constructs Techniques and Reagents	Rakestraw A and Wittrup KD (2006) Contrasting secretory processing of simultaneously expressed heterologous proteins in Saccharomyces cerevisiae. Biotechnol Bioeng 93(5):896-905	|AGA2 |HAC1 |KAR2
Regulation of Transcription	Takemori Y, et al. (2006) Stress-induced transcription of the endoplasmic reticulum oxidoreductin gene ERO1 in the yeast Saccharomyces cerevisiae. Mol Genet Genomics 275(1):89-96	|ERO1 |HAC1 |HSF1 |IRE1
Function/Process Protein Physical Properties Protein Sequence Features Protein/Nucleic Acid Structure	Tian G, et al. (2006) The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Cell 124(1):61-73
Cross-species Expression	Zhang W, et al. (2006) Enhanced Secretion of Heterologous Proteins in Pichia pastoris Following Overexpression of Saccharomyces cerevisiae Chaperone Proteins. Biotechnol Prog 22(4):1090-5	|KAR2 |SEC63 |SSA1 |YDJ1
Protein/Nucleic Acid Structure	Kimura T, et al. (2005) Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their Activities. J Biol Chem 280(36):31438-41	|CNE1 |EPS1 |EUG1 |KAR2 |MPD1 |MPD2
Fungal Related Genes/Proteins	Lodi T, et al. (2005) Secretion of human serum albumin by Kluyveromyces lactis overexpressing KlPDI1 and KlERO1. Appl Environ Microbiol 71(8):4359-63	|ERO1
Regulation of Transcription	Matsumoto R, et al. (2005) The stress response against denatured proteins in the deletion of cytosolic chaperones SSA1/2 is different from heat-shock response in Saccharomyces cerevisiae. BMC Genomics 6():141	|CTT1 |DER1 |ERO1 |HSP104 |HSP26 |HSP78 |KAR2 |MRP8 |MRPL10 |PRE1 |RPL25 |RPL37A |RPL8B |RPN12 |MORE
Genetic Interactions Mutants/Phenotypes Strains/Constructs Techniques and Reagents	Schuldiner M, et al. (2005) Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile. Cell 123(3):507-19	|ALG12 |ALG3 |ALG5 |ALG6 |ALG8 |ALG9 |API2 |APL5 |APL6 |APM3 |APS3 |ARL1 |ARL3 |ARV1 |MORE
Function/Process Protein Physical Properties Substrates/Ligands/Cofactors	Wilkinson B, et al. (2005) A structural disulfide of yeast protein-disulfide isomerase destabilizes the active site disulfide of the N-terminal thioredoxin domain. J Biol Chem 280(12):11483-7
Genetic Interactions Mutants/Phenotypes Strains/Constructs	Xu P, et al. (2005) Analysis of unfolded protein response during single-chain antibody expression in Saccaromyces cerevisiae reveals different roles for BiP and PDI in folding. Metab Eng 7(4):269-79	|IRE1 |KAR2
Function/Process Mutants/Phenotypes Non-Fungal Related Genes/Proteins Protein Physical Properties Protein Sequence Features Strains/Constructs Substrates/Ligands/Cofactors	Kimura T, et al. (2004) Functional differences between human and yeast protein disulfide isomerase family proteins. Biochem Biophys Res Commun 320(2):359-65	|EUG1 |MPD1 |MPD2
Fungal Related Genes/Proteins	Lahav R, et al. (2004) Alterations in protein synthesis and levels of heat shock 70 proteins in response to salt stress of the halotolerant yeast Rhodotorula mucilaginosa. Antonie Van Leeuwenhoek 85(4):259-69	|KAR2 |SSB1 |SSB2
Fungal Related Genes/Proteins	Saloheimo M, et al. (2004) Characterization of secretory genes ypt1/yptA and nsf1/nsfA from two filamentous fungi: induction of secretory pathway genes of Trichoderma reesei under secretion stress conditions. Appl Environ Microbiol 70(1):459-67	|SAR1 |YPT1
Function/Process Mutants/Phenotypes Protein Physical Properties Strains/Constructs	Solovyov A, et al. (2004) Sulfhydryl oxidation, not disulfide isomerization, is the principal function of protein disulfide isomerase in yeast Saccharomyces cerevisiae. J Biol Chem 279(33):34095-100
Cross-species Expression Mutants/Phenotypes Non-Fungal Related Genes/Proteins Protein Physical Properties Strains/Constructs	Xiao R, et al. (2004) The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum. J Biol Chem 279(48):49780-6	|EPS1 |EUG1 |MPD1 |MPD2
DNA/RNA Sequence Features Regulation of Transcription	Norgaard P, et al. (2003) Gene regulation in response to protein disulphide isomerase deficiency. Yeast 20(7):645-52	|ERO1 |KAR2 |MPD1 |MPD2
Regulation of Transcription	Song Y, et al. (2002) Different effects of calnexin deletion in Saccharomyces cerevisiae on the secretion of two glycosylated amyloidogenic lysozymes. FEBS Lett 512(1-3):213-7	|CNE1 |KAR2
RNA Levels and Processing Regulation of	Alexandre H, et al. (2001) Global gene expression during short-term ethanol stress in Saccharomyces cerevisiae. FEBS Lett 498(1):98-103	|AHP1 |ALD2 |ALD4 |APJ1 |ATG8 |CCC2 |CDC19 |CIT1 |CIT2 |CPR6 |CTT1 |DAK1 |EMI2 |ERO1 |MORE
Function/Process Protein Sequence Features	Fetrow JS, et al. (2001) Genomic-scale comparison of sequence- and structure-based methods of function prediction: does structure provide additional insight? Protein Sci 10(5):1005-14	|CDD1 |EPS1 |ERF2 |EUG1 |GRX1 |GRX2 |GRX3 |GRX4 |GRX5 |GRX6 |GRX7 |GRX8 |LEU5 |MPD1 |MORE
Fungal Related Genes/Proteins Genetic Interactions Mutants/Phenotypes Strains/Constructs	Nakanishi H, et al. (2001) Hut1 proteins identified in Saccharomyces cerevisiae and Schizosaccharomyces pombe are functional homologues involved in the protein-folding process at the endoplasmic reticulum. Yeast 18(6):543-54	|ERO1 |HUT1 |MPD1 |MPD2
Alias Cellular Location Function/Process Protein Sequence Features Substrates/Ligands/Cofactors	Norgaard P and Winther JR (2001) Mutation of yeast Eug1p CXXS active sites to CXXC results in a dramatic increase in protein disulphide isomerase activity. Biochem J 358(Pt 1):269-74	|EUG1
Function/Process Fungal Related Genes/Proteins Genetic Interactions Mutants/Phenotypes Strains/Constructs	Norgaard P, et al. (2001) Functional differences in yeast protein disulfide isomerases. J Cell Biol 152(3):553-62	|EPS1 |EUG1 |MPD1 |MPD2
Function/Process	Sevier CS, et al. (2001) A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation. Nat Cell Biol 3(10):874-82	|ERO1 |ERV2
Function/Process RNA Levels and Processing Regulation of	Song Y, et al. (2001) Effects of calnexin deletion in Saccharomyces cerevisiae on the secretion of glycosylated lysozymes. J Biochem 130(6):757-64	|CNE1 |KAR2
Cross-species Expression	Xiao R, et al. (2001) Combinations of protein-disulfide isomerase domains show that there is little correlation between isomerase activity and wild-type growth. J Biol Chem 276(30):27975-80
Fungal Related Genes/Proteins	Bao WG, et al. (2000) Protein disulphide isomerase genes of Kluyveromyces lactis. Yeast 16(4):329-41	|EUG1 |MPD1
RNA Levels and Processing Regulation of	Casagrande R, et al. (2000) Degradation of proteins from the ER of S. cerevisiae requires an intact unfolded protein response pathway. Mol Cell 5(4):729-35	|ERO1 |HAC1 |IRE1 |KAR2 |LHS1
Function/Process	Frand AR and Kaiser CA (2000) Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum. Mol Biol Cell 11(9):2833-43	|ERO1
Non-Fungal Related Genes/Proteins	Monnat J, et al. (2000) Identification of a novel saturable endoplasmic reticulum localization mechanism mediated by the C-terminus of a Dictyostelium protein disulfide isomerase. Mol Biol Cell 11(10):3469-84
Non-Fungal Related Genes/Proteins	Ngiam C, et al. (2000) Characterization of a foldase, protein disulfide isomerase A, in the protein secretory pathway of Aspergillus niger. Appl Environ Microbiol 66(2):775-82
Regulation of	Travers KJ, et al. (2000) Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101(3):249-58	|ERO1 |EUG1 |FPR2 |INO1 |IRE1 |KAR2 |LHS1 |OPI1
Function/Process Genetic Interactions Substrates/Ligands/Cofactors	Tu BP, et al. (2000) Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 290(5496):1571-4	|ERO1 |FAD1
Function/Process Fungal Related Genes/Proteins Mutants/Phenotypes Strains/Constructs Substrates/Ligands/Cofactors	Frand AR and Kaiser CA (1999) Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol Cell 4(4):469-77	|ERO1 |EUG1 |MPD2
Function/Process Mutants/Phenotypes Strains/Constructs Substrates/Ligands/Cofactors	Gillece P, et al. (1999) Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase. J Cell Biol 147(7):1443-56	|KAR2 |SEC61
Regulation of	Takewaka T, et al. (1999) Null mutation in IRE1 gene inhibits overproduction of microsomal cytochrome P450Alk1 (CYP 52A3) and proliferation of the endoplasmic reticulum in Saccharomyces cerevisiae. J Biochem 125(3):507-14	|IRE1 |KAR2
Fungal Related Genes/Proteins	Wang Q and Chang A (1999) Eps1, a novel PDI-related protein involved in ER quality control in yeast. EMBO J 18(21):5972-82	|EPS1 |GAS1 |KAR2 |PMA1 |SHR3 |UBC6
Mutants/Phenotypes Non-Fungal Related Genes/Proteins Protein Sequence Features Strains/Constructs Substrates/Ligands/Cofactors	Westphal V, et al. (1999) Functional properties of the two redox-active sites in yeast protein disulphide isomerase in vitro and in vivo. J Mol Biol 286(4):1229-39
Function/Process Fungal Related Genes/Proteins Genetic Interactions Mutants/Phenotypes	Frand AR and Kaiser CA (1998) The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell 1(2):161-70	|ERO1
Function/Process Mutants/Phenotypes Non-Fungal Related Genes/Proteins Protein Sequence Features Strains/Constructs	Luz JM and Lennarz WJ (1998) The nonactive site cysteine residues of yeast protein disulfide isomerase are not required for cell viability. Biochem Biophys Res Commun 248(3):621-7
DNA/RNA Sequence Features Protein-Nucleic Acid Interactions Regulation of	Mori K, et al. (1998) Palindrome with spacer of one nucleotide is characteristic of the cis-acting unfolded protein response element in Saccharomyces cerevisiae. J Biol Chem 273(16):9912-20	|EUG1 |FPR2 |HAC1 |KAR2 |LHS1 |SCJ1
Non-Fungal Related Genes/Proteins	Westphal V, et al. (1998) Kinetic analysis of the mechanism and specificity of protein-disulfide isomerase using fluorescence-quenched peptides. J Biol Chem 273(39):24992-9
Genetic Interactions Mutants/Phenotypes Strains/Constructs	Holst B, et al. (1997) Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. J Cell Biol 138(6):1229-38	|EUG1
Mutants/Phenotypes Non-Fungal Related Genes/Proteins Regulatory Role	Laboissiere MC, et al. (1997) Protein disulfide isomerase in spore germination and cell division. Biol Chem 378(5):431-7
Genetic Interactions	Tachikawa H, et al. (1997) Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner. Biochem Biophys Res Commun 239(3):710-4	|MPD2
Regulation of Transcription	Welihinda AA, et al. (1997) Gene induction in response to unfolded protein in the endoplasmic reticulum is mediated through Ire1p kinase interaction with a transcriptional coactivator complex containing Ada5p. Proc Natl Acad Sci U S A 94(9):4289-94	|ADA2 |GCN5 |IRE1 |NGG1 |SPT20
Non-Fungal Related Genes/Proteins Protein Sequence Features	Chivers PT, et al. (1996) The CXXC motif: imperatives for the formation of native disulfide bonds in the cell. EMBO J 15(11):2659-67
Regulation of	Elrod-Erickson MJ and Kaiser CA (1996) Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations. Mol Biol Cell 7(7):1043-58	|BST1 |BST3 |EMP24 |KAR2 |SEC13
Function/Process Mutants/Phenotypes Strains/Constructs	Dunn A, et al. (1995) Protein disulphide isomerase (PDI) is required for the secretion of a native disulphide-bonded protein from Saccharomyces cerevisiae. Biochem Soc Trans 23(1):78S
Function/Process Mutants/Phenotypes Protein Sequence Features Strains/Constructs Substrates/Ligands/Cofactors	Hayano T, et al. (1995) Protein disulfide isomerase mutant lacking its isomerase activity accelerates protein folding in the cell. FEBS Lett 377(3):505-11
Cross-species Expression Function/Process Non-Fungal Related Genes/Proteins	Laboissiere MC, et al. (1995) The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J Biol Chem 270(47):28006-9
Non-Fungal Related Genes/Proteins Reviews	Mager WH and De Kruijff AJ (1995) Stress-induced transcriptional activation. Microbiol Rev 59(3):506-31	|ACE2 |BCY1 |CAD1 |CLN1 |CLN2 |CLN3 |CTT1 |CUP1-1 |CUP1-2 |CYR1 |DDR2 |ENA1 |GAC1 |GCN2 |MORE
Genetic Interactions Mutants/Phenotypes	Tachikawa H, et al. (1995) Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion. FEBS Lett 369(2-3):212-6	|MPD1
Regulation of Transcription	Cox JS, et al. (1993) Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73(6):1197-206	|IRE1 |KAR2
Alias Cross-species Expression Mutants/Phenotypes Non-Fungal Related Genes/Proteins	Gunther R, et al. (1993) Functional replacement of the Saccharomyces cerevisiae Trg1/Pdi1 protein by members of the mammalian protein disulfide isomerase family. J Biol Chem 268(11):7728-32
Function/Process Mutants/Phenotypes Protein Sequence Features Strains/Constructs Substrates/Ligands/Cofactors	LaMantia ML and Lennarz WJ (1993) The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity. Cell 74(5):899-908
Reviews	Noiva R and Lennarz WJ (1992) Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum. J Biol Chem 267(6):3553-6
DNA/RNA Sequence Features Mutants/Phenotypes Strains/Constructs	Scherens B, et al. (1992) The complete sequence of a 9,543 bp segment on the left arm of chromosome III reveals five open reading frames including glucokinase and the protein disulfide isomerase. Yeast 8(7):577-85	|EMC1 |GID7 |GLK1 |MGR1
Fungal Related Genes/Proteins Genetic Interactions	Tachibana C and Stevens TH (1992) The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol Cell Biol 12(10):4601-11	|EUG1
DNA/RNA Sequence Features Mutants/Phenotypes Protein Physical Properties Protein Sequence Features RNA Levels and Processing Strains/Constructs	Farquhar R, et al. (1991) Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae. Gene 108(1):81-9
Alias Cellular Location DNA/RNA Sequence Features Function/Process Mapping Mutants/Phenotypes Non-Fungal Related Genes/Proteins Protein Sequence Features RNA Levels and Processing Strains/Constructs Techniques and Reagents	Gunther R, et al. (1991) The Saccharomyces cerevisiae TRG1 gene is essential for growth and encodes a lumenal endoplasmic reticulum glycoprotein involved in the maturation of vacuolar carboxypeptidase. J Biol Chem 266(36):24557-63
Alias Cellular Location Function/Process Mutants/Phenotypes Protein Sequence Features Strains/Constructs Techniques and Reagents	LaMantia M, et al. (1991) Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast. Proc Natl Acad Sci U S A 88(10):4453-7
Alias DNA/RNA Sequence Features Function/Process Mutants/Phenotypes Non-Fungal Related Genes/Proteins Protein Sequence Features Strains/Constructs	Scherens B, et al. (1991) Determination of the sequence of the yeast YCL313 gene localized on chromosome III. Homology with the protein disulfide isomerase (PDI gene product) of other organisms. Yeast 7(2):185-93
DNA/RNA Sequence Features Mapping Mutants/Phenotypes Non-Fungal Related Genes/Proteins Protein Sequence Features Strains/Constructs	Tachikawa H, et al. (1991) Molecular structure of a yeast gene, PDI1, encoding protein disulfide isomerase that is essential for cell growth. J Biochem 110(2):306-13
Function/Process Protein Physical Properties	Mizunaga T, et al. (1990) Purification and characterization of yeast protein disulfide isomerase. J Biochem 108(5):846-51

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