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Protein

Protein disulfide isomerase MPD2

Gene

MPD2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Non essential disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May be involved in glycosylation, prolyl hydroxylation and triglyceride transfer. Able to fold proteins by being directly oxidized by ERO1.1 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

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:YOL088C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide isomerase MPD2 (EC:5.3.4.1)
Gene namesi
Name:MPD2
Ordered Locus Names:YOL088C
ORF Names:O0941
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XV

Organism-specific databases

CYGDiYOL088c.
EuPathDBiFungiDB:YOL088C.
SGDiS000005448. MPD2.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561C → S: Loss of function; when associated with S-59. 1 Publication
Mutagenesisi59 – 591C → S: Loss of function; when associated with S-56. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 277255Protein disulfide isomerase MPD2PRO_0000034182Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 ↔ 59Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ99316.
PaxDbiQ99316.

Interactioni

Protein-protein interaction databases

BioGridi34314. 40 interactions.
DIPiDIP-1451N.
IntActiQ99316. 5 interactions.
MINTiMINT-392339.

Structurei

3D structure databases

ProteinModelPortaliQ99316.
SMRiQ99316. Positions 24-141.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 172146ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi274 – 2774Prevents 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

eggNOGiNOG314639.
HOGENOMiHOG000113635.
InParanoidiQ99316.
OMAiYTVVKYY.
OrthoDBiEOG71CFZN.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00014. ER_TARGET. 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.

Q99316-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLHGFLFSV LSTCVVILPA LAYSEAVTMV KSIEQYFDIC NRNDSYTMIK
60 70 80 90 100
YYTSWCQHCK TLAPVYEELG ELYAKKANKD DTPINFLEVN CEFFGPTLCT
110 120 130 140 150
DLPGFPIIEL VKPRTKPLVL PKLDWSSMKF HERLWQRIKT WFNNPKYQLD
160 170 180 190 200
TSRVVRFEGS RNLKSLSNFI DTVRSKDTEE RFIEHIFDDS RNCNEELRSQ
210 220 230 240 250
QLLCKAGKEY YSDTLSKLYG DVNGLEKERR RLEALIKQNG DDLSKEVKEK
260 270
LKIIRLQLSL LSHIEDQLED TSSHDEL
Length:277
Mass (Da):32,401
Last modified:November 1, 1996 - v1
Checksum:iECCEA7C6CBB10488
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D34634 Genomic DNA. Translation: BAA22222.1.
X83121 Genomic DNA. Translation: CAA58191.1.
Z74830 Genomic DNA. Translation: CAA99100.1.
BK006948 Genomic DNA. Translation: DAA10696.1.
PIRiS57381.
RefSeqiNP_014553.1. NM_001183342.1.

Genome annotation databases

EnsemblFungiiYOL088C; YOL088C; YOL088C.
GeneIDi854065.
KEGGisce:YOL088C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D34634 Genomic DNA. Translation: BAA22222.1.
X83121 Genomic DNA. Translation: CAA58191.1.
Z74830 Genomic DNA. Translation: CAA99100.1.
BK006948 Genomic DNA. Translation: DAA10696.1.
PIRiS57381.
RefSeqiNP_014553.1. NM_001183342.1.

3D structure databases

ProteinModelPortaliQ99316.
SMRiQ99316. Positions 24-141.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34314. 40 interactions.
DIPiDIP-1451N.
IntActiQ99316. 5 interactions.
MINTiMINT-392339.

Proteomic databases

MaxQBiQ99316.
PaxDbiQ99316.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL088C; YOL088C; YOL088C.
GeneIDi854065.
KEGGisce:YOL088C.

Organism-specific databases

CYGDiYOL088c.
EuPathDBiFungiDB:YOL088C.
SGDiS000005448. MPD2.

Phylogenomic databases

eggNOGiNOG314639.
HOGENOMiHOG000113635.
InParanoidiQ99316.
OMAiYTVVKYY.
OrthoDBiEOG71CFZN.

Enzyme and pathway databases

BioCyciYEAST:YOL088C-MONOMER.

Miscellaneous databases

NextBioi975674.
PROiQ99316.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner."
    Tachikawa H., Funahashi W., Takeuchi Y., Nakanishi H., Nishihara R., Katoh S., Gao X.D., Mizunaga T., Fujimoto D.
    Biochem. Biophys. Res. Commun. 239:710-714(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF CYS-56 AND CYS-59.
  2. "A 29.425 kb segment on the left arm of yeast chromosome XV contains more than twice as many unknown as known open reading frames."
    Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.
    Yeast 11:975-986(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  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. "Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum."
    Frand A.R., Kaiser C.A.
    Mol. Cell 4:469-477(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: OXIDATION BY ERO1.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMPD2_YEAST
AccessioniPrimary (citable) accession number: Q99316
Secondary accession number(s): D6W1Y0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 113 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 1520 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. 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.