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Protein

Protein disulfide-isomerase MPD1

Gene

MPD1

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

Participates in the folding of proteins containing disulfide bonds.1 Publication

Catalytic activityi

Catalyzes the rearrangement of -S-S- bonds in proteins.

GO - Molecular functioni

  • protein disulfide isomerase activity Source: SGD
  • protein disulfide oxidoreductase activity Source: SGD
  • protein-disulfide reductase (glutathione) activity Source: SGD

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • oxidation-reduction process Source: GOC
  • protein folding Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BioCyciYEAST:YOR288C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase MPD1 (EC:5.3.4.1)
Gene namesi
Name:MPD1
Ordered Locus Names:YOR288C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XV

Organism-specific databases

CYGDiYOR288c.
EuPathDBiFungiDB:YOR288C.
SGDiS000005814. MPD1.

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 318297Protein disulfide-isomerase MPD1PRO_0000034220Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi47 – 471N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi59 ↔ 62Redox-activePROSITE-ProRule annotation
Glycosylationi307 – 3071N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ12404.
PaxDbiQ12404.
PeptideAtlasiQ12404.

Interactioni

Subunit structurei

Interacts with CNE1 and EPS1.1 Publication

Protein-protein interaction databases

BioGridi34675. 27 interactions.
DIPiDIP-4085N.
IntActiQ12404. 3 interactions.
MINTiMINT-479800.
STRINGi4932.YOR288C.

Structurei

Secondary structure

1
318
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 438Combined sources
Beta strandi45 – 484Combined sources
Beta strandi50 – 556Combined sources
Helixi60 – 634Combined sources
Helixi66 – 7510Combined sources
Turni76 – 794Combined sources
Beta strandi80 – 867Combined sources
Turni90 – 923Combined sources
Helixi93 – 986Combined sources
Beta strandi103 – 1119Combined sources
Beta strandi132 – 1354Combined sources
Helixi142 – 1509Combined sources
Beta strandi157 – 1593Combined sources
Helixi163 – 1653Combined sources
Helixi166 – 1705Combined sources
Beta strandi174 – 18613Combined sources
Helixi189 – 1979Combined sources
Beta strandi202 – 2087Combined sources
Helixi209 – 2113Combined sources
Helixi226 – 23914Combined sources
Beta strandi246 – 2516Combined sources
Turni252 – 2554Combined sources
Beta strandi256 – 2594Combined sources
Helixi267 – 27812Combined sources
Beta strandi283 – 2853Combined sources
Helixi289 – 29911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ED3X-ray2.00A/B23-310[»]
ProteinModelPortaliQ12404.
SMRiQ12404. Positions 22-301.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12404.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 158137ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi315 – 3184Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00730000110455.
HOGENOMiHOG000248396.
InParanoidiQ12404.
KOiK09584.
OMAiRDENIME.
OrthoDBiEOG71CFZN.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q12404-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFLNIIKLL LGLFIMNEVK AQNFYDSDPH ISELTPKSFD KAIHNTNYTS
60 70 80 90 100
LVEFYAPWCG HCKKLSSTFR KAAKRLDGVV QVAAVNCDLN KNKALCAKYD
110 120 130 140 150
VNGFPTLMVF RPPKIDLSKP IDNAKKSFSA HANEVYSGAR TLAPIVDFSL
160 170 180 190 200
SRIRSYVKKF VRIDTLGSLL RKSPKLSVVL FSKQDKISPV YKSIALDWLG
210 220 230 240 250
KFDFYSISNK KLKQLTDMNP TYEKTPEIFK YLQKVIPEQR QSDKSKLVVF
260 270 280 290 300
DADKDKFWEY EGNSINKNDI SKFLRDTFSI TPNEGPFSRR SEYIAYLKTG
310
KKPIKKNHSS SGNKHDEL
Length:318
Mass (Da):36,408
Last modified:November 1, 1996 - v1
Checksum:i3F96477E8182DC5C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D34633 Genomic DNA. Translation: BAA07015.1.
X89633 Genomic DNA. Translation: CAA61791.1.
Z75196 Genomic DNA. Translation: CAA99515.1.
BK006948 Genomic DNA. Translation: DAA11052.1.
PIRiS67190.
RefSeqiNP_014931.3. NM_001183707.3.

Genome annotation databases

EnsemblFungiiYOR288C; YOR288C; YOR288C.
GeneIDi854462.
KEGGisce:YOR288C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D34633 Genomic DNA. Translation: BAA07015.1.
X89633 Genomic DNA. Translation: CAA61791.1.
Z75196 Genomic DNA. Translation: CAA99515.1.
BK006948 Genomic DNA. Translation: DAA11052.1.
PIRiS67190.
RefSeqiNP_014931.3. NM_001183707.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ED3X-ray2.00A/B23-310[»]
ProteinModelPortaliQ12404.
SMRiQ12404. Positions 22-301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34675. 27 interactions.
DIPiDIP-4085N.
IntActiQ12404. 3 interactions.
MINTiMINT-479800.
STRINGi4932.YOR288C.

Proteomic databases

MaxQBiQ12404.
PaxDbiQ12404.
PeptideAtlasiQ12404.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR288C; YOR288C; YOR288C.
GeneIDi854462.
KEGGisce:YOR288C.

Organism-specific databases

CYGDiYOR288c.
EuPathDBiFungiDB:YOR288C.
SGDiS000005814. MPD1.

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00730000110455.
HOGENOMiHOG000248396.
InParanoidiQ12404.
KOiK09584.
OMAiRDENIME.
OrthoDBiEOG71CFZN.

Enzyme and pathway databases

BioCyciYEAST:YOR288C-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ12404.
NextBioi976742.
PROiQ12404.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion."
    Tachikawa H., Takeuchi Y., Funahashi W., Miura T., Gao X.D., Fujimoto D., Mizunaga T., Onodera K.
    FEBS Lett. 369:212-216(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of Saccharomyces cerevisiae."
    Cheret G., Bernardi A., Sor F.J.
    Yeast 12:1059-1064(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities."
    Kimura T., Hosoda Y., Sato Y., Kitamura Y., Ikeda T., Horibe T., Kikuchi M.
    J. Biol. Chem. 280:31438-31441(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CNE1 AND EPS1.

Entry informationi

Entry nameiMPD1_YEAST
AccessioniPrimary (citable) accession number: Q12404
Secondary accession number(s): D6W2Y6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 128 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 830 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3

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 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.