MPD2/YOL088C 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

ChrXV: 154745 to 153912
CDS: 154745 - 153912

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

MPD2 YOL088C ORF, Verified S000005448

Description
Member of the protein disulfide isomerase (PDI) family, exhibits chaperone activity; overexpression suppresses the lethality of a pdi1 deletion but does not complement all Pdi1p functions; undergoes oxidation by Ero1p

GO Annotations [TOP] [NEXT]
Molecular Function
Annotation(s) Reference(s) Evidence Assigned By
isomerase activity 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
       IGI : Inferred from Genetic Interaction with SGD:PDI1
ISS : Inferred from Sequence or structural Similarity with SGD:PDI1
TAS : Traceable Author Statement
IMP : Inferred from Mutant Phenotype
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
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 Norgaard P, et al. (2001) Functional differences in yeast protein disulfide isomerases. J Cell Biol 152(3):553-62
       IGI : Inferred from Genetic Interaction with SGD:PDI1
ISS : Inferred from Sequence or structural Similarity with SGD:PDI1
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:IPR013766 , EBI:IPR017936
Assigned on 2009-01-12 UniProtKB
protein folding Norgaard P, et al. (2001) Functional differences in yeast protein disulfide isomerases. J Cell Biol 152(3):553-62
       IGI : Inferred from Genetic Interaction with SGD:PDI1
Assigned on 2002-11-08 SGD
Cellular Component
Annotation(s) Reference(s) Evidence Assigned By
endoplasmic reticulum 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
       IGI : Inferred from Genetic Interaction with SGD:PDI1
Assigned on 2006-08-18 SGD
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
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-0095
Assigned on 2009-10-01 UniProtKB

Pathways [TOP] [NEXT]
No pathways available

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

Basic References [TOP]
BASIC INFORMATION REFERENCES forMPD2/YOL088C for MPD2
1) 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

2) 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

3) Kimura T, et al. (2004) Functional differences between human and yeast protein disulfide isomerase family proteins. Biochem Biophys Res Commun 320(2):359-65

Mutant Phenotypes [TOP] [NEXT]
Phenotype page for MPD2/YOL088C

Interactions: genetic, physical, and other gene-gene links. [TOP] [NEXT]
Interaction page for MPD2/YOL088C

Homologs [TOP] [NEXT]

Comparison Resources

Physical Properties and Transcript Information: predicted from sequence [TOP] [NEXT]
Protein Sequence Calculations
from Predicted Full length Translation

N-term MKLHGFL

C-term TSSHDEL

Length(aa) 277

MW(Da) 32,401

pI 6.51

Amino Acid Composition (full length)

GCG tools: PepPlot, Helical Wheel, PepStruct

Transcript Translation Calculations

Codon Bias 0.120

Codon Adaptation Index 0.174

Frequency of Optimal Codons 0.480

Hydropathicity of Protein -0.477

Aromaticity Score 0.101

10 20 30 40 50 | | | | | MKLHGFLFSVLSTCVVILPALAYSEAVTMVKSIEQYFDICNRNDSYTMIK YYTSWCQHCKTLAPVYEELGELYAKKANKDDTPINFLEVNCEFFGPTLCT DLPGFPIIELVKPRTKPLVLPKLDWSSMKFHERLWQRIKTWFNNPKYQLD TSRVVRFEGSRNLKSLSNFIDTVRSKDTEERFIEHIFDDSRNCNEELRSQ QLLCKAGKEYYSDTLSKLYGDVNGLEKERRRLEALIKQNGDDLSKEVKEK LKIIRLQLSLLSHIEDQLEDTSSHDEL*

Protein Structures from PDB: proteins of known structure with sequence similarity to MPD2/YOL088C, based on Smith-Waterman analysis. [TOP] [NEXT]
PDB protein structure(s) homologous to MPD2 Homolog Source (per PDB) Protein Alignment: MPD2 vs. Homolog External Links
P-Value %Identical %Similar Alignment
2djj ( Chain: A)
Solution structure of the a' domain of thermophilic fungal protein disulfide isomerase
PDB_Info
PDB_Structure
Humicola insolens 9.3e-06 37 27 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 0.000670 29 30 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 = 0.002099 31 26 View alignment SCOP
MMDB
CATH
Chain B = 0.002099 31 26 View alignment
2dmm ( Chain: A)
The solution structure of the second thioredoxin domain of human protein disulfide-isomerase a3
PDB_Info
PDB_Structure
Homo sapiens 0.002600 34 24 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 0.002900 33 29 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 0.004897 34 30 View alignment SCOP
MMDB
CATH
3f8u ( Chain: A, C)
Tapasin/erp57 heterodimer
PDB_Info
PDB_Structure
Homo sapiens Chain A = 0.009400 34 24 View alignment SCOP
MMDB
CATH
Chain C = 0.009400 34 24 View alignment

Genome-wide Expression and Other Large-Scale Analyses [TOP] [NEXT]

Functional Analysis
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
MPD2 SGD (2007) Information without a citation in SGD

Standard Name	Reference
MPD2	SGD (2007) Information without a citation in SGD

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
Sequence from other databases

Sequence ID Source

YOL088C SGD Systematic Sequence

854065 NCBI: Gene ID

NP_014553.1 NCBI: RefSeq protein version ID

NP_014553.1 NCBI: RefSeq protein version ID

6324484 NCBI: NCBI protein GI

Sequence from other databases
Sequence ID	Source
YOL088C	SGD Systematic Sequence
854065	NCBI: Gene ID
NP_014553.1	NCBI: RefSeq protein version ID
NP_014553.1	NCBI: RefSeq protein version ID
6324484	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

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

Literature Guide: papers categorized by topic. [TOP]
Topics Reference Other Genes Addressed
17 curated references; 0 references not yet curated
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 |PDI1
Mutants/Phenotypes
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
Mutants/Phenotypes
McCue PP and Phang JM (2008) Identification of Human Intracellular Targets of the Medicinal Herb St. John's Wort by Chemical-Genetic Profiling in Yeast. J Agric Food Chem 56(22):11011-11017
       |ABD1 |ACS1 |ADP1 |AHC1 |APN2 |ASR1 |ATP5 |BCK2 |BFR1 |CBP6 |CHK1 |CIN8 |CRR1 |CTF19 |MORE
Mapping
Marullo P, et al. (2007) Efficient use of DNA molecular markers to construct industrial yeast strains. FEMS Yeast Res 7(8):1295-1306
       |ADH1 |ATG19 |DUF1 |HAL9 |IRA2 |PAD1 |PHM7 |YOL083W
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 |PDI1
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 |PDI1
Function/Process
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 |PDI1
Function/Process
Genetic Interactions
Mutants/Phenotypes
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 |PDI1
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 |PDI1
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
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 |PDI1
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 |PDI1
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 |PDI1
Large-scale phenotype analysis
Mutants/Phenotypes
Strains/Constructs
Rieger KJ, et al. (1999) Chemotyping of yeast mutants using robotics. Yeast 15(10B):973-86
       |ADY3 |AIM22 |AIM6 |AMA1 |AQR1 |AZR1 |BIT61 |CAF40 |CSH1 |CST26 |CUS2 |CYK3 |DGK1 |DLS1 |MORE
Mutants/Phenotypes
Strains/Constructs
Techniques and Reagents
Pearson BM, et al. (1998) Construction of PCR-ligated long flanking homology cassettes for use in the functional analysis of six unknown open reading frames from the left and right arms of Saccharomyces cerevisiae chromosome XV. Yeast 14(4):391-9
       |DGK1 |DUF1 |HSH49 |LDB19 |SPO21
Genetic Interactions
Mutants/Phenotypes
Protein Processing/Modification/Regulation
Protein Sequence Features
Strains/Constructs
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
       |PDI1

Return to SGD

SGD^tm pages Database Copyright © 1997-2010 The Board of Trustees of Leland Stanford Junior University. Permission to use the information contained in this database was given by the researchers/institutes who contributed or published the information. Users of the database are solely responsible for compliance with any copyright restrictions, including those applying to the author abstracts. Documents from this server are provided "AS-IS" without any warranty, expressed or implied. The SGD project at Stanford University is supported by a Genome Research Resource Grant from the US National Human Genome Research Institute, part of the US National Institutes of Health.