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Q99316

- MPD2_YEAST

UniProt

Q99316 - MPD2_YEAST

Protein

Protein disulfide isomerase MPD2

Gene

MPD2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    1. protein disulfide isomerase activity Source: SGD
    2. protein disulfide oxidoreductase activity Source: SGD

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. oxidation-reduction process Source: GOC
    3. protein folding Source: SGD

    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: Chromosome XV

    Organism-specific databases

    CYGDiYOL088c.
    SGDiS000005448. MPD2.

    Subcellular locationi

    Endoplasmic reticulum 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum Source: SGD

    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.

    Expressioni

    Gene expression databases

    GenevestigatoriQ99316.

    Interactioni

    Protein-protein interaction databases

    BioGridi34314. 41 interactions.
    DIPiDIP-1451N.
    IntActiQ99316. 5 interactions.
    MINTiMINT-392339.
    STRINGi4932.YOL088C.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99316.
    SMRiQ99316. Positions 24-110.
    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.
    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

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    MKLHGFLFSV LSTCVVILPA LAYSEAVTMV KSIEQYFDIC NRNDSYTMIK    50
    YYTSWCQHCK TLAPVYEELG ELYAKKANKD DTPINFLEVN CEFFGPTLCT 100
    DLPGFPIIEL VKPRTKPLVL PKLDWSSMKF HERLWQRIKT WFNNPKYQLD 150
    TSRVVRFEGS RNLKSLSNFI DTVRSKDTEE RFIEHIFDDS RNCNEELRSQ 200
    QLLCKAGKEY YSDTLSKLYG DVNGLEKERR RLEALIKQNG DDLSKEVKEK 250
    LKIIRLQLSL LSHIEDQLED TSSHDEL 277
    Length:277
    Mass (Da):32,401
    Last modified:November 1, 1996 - v1
    Checksum:iECCEA7C6CBB10488
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi S57381.
    RefSeqi NP_014553.1. NM_001183342.1.

    3D structure databases

    ProteinModelPortali Q99316.
    SMRi Q99316. Positions 24-110.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34314. 41 interactions.
    DIPi DIP-1451N.
    IntActi Q99316. 5 interactions.
    MINTi MINT-392339.
    STRINGi 4932.YOL088C.

    Proteomic databases

    MaxQBi Q99316.
    PaxDbi Q99316.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOL088C ; YOL088C ; YOL088C .
    GeneIDi 854065.
    KEGGi sce:YOL088C.

    Organism-specific databases

    CYGDi YOL088c.
    SGDi S000005448. MPD2.

    Phylogenomic databases

    eggNOGi NOG314639.
    HOGENOMi HOG000113635.
    OMAi YTVVKYY.
    OrthoDBi EOG71CFZN.

    Enzyme and pathway databases

    BioCyci YEAST:YOL088C-MONOMER.

    Miscellaneous databases

    NextBioi 975674.

    Gene expression databases

    Genevestigatori Q99316.

    Family and domain databases

    Gene3Di 3.40.30.10. 2 hits.
    InterProi IPR012336. Thioredoxin-like_fold.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00085. Thioredoxin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 1 hit.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 108 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