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P32474

- EUG1_YEAST

UniProt

P32474 - EUG1_YEAST

Protein

Protein disulfide-isomerase EUG1

Gene

EUG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Probably interacts with nascent polypeptides in the endoplasmic reticulum. It is an essential gene only in the absence of PDI. Its native disulfide isomerase activity is very low.1 Publication

    Catalytic activityi

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

    GO - Molecular functioni

    1. protein binding Source: SGD
    2. protein disulfide isomerase activity Source: SGD
    3. protein disulfide oxidoreductase activity Source: SGD
    4. protein-disulfide reductase (glutathione) activity Source: SGD
    5. unfolded protein binding 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:YDR518W-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein disulfide-isomerase EUG1 (EC:5.3.4.1)
    Short name:
    PDI
    Alternative name(s):
    Endoplasmic reticulum protein EUG1
    Gene namesi
    Name:EUG1
    Ordered Locus Names:YDR518W
    ORF Names:D9719.23
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR518w.
    SGDiS000002926. EUG1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi65 – 651S → C: Increases PDI activity. 1 Publication
    Mutagenesisi408 – 4081S → C: Increases PDI activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 517488Protein disulfide-isomerase EUG1PRO_0000034219Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi159 – 1591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi174 – 1741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi462 – 4621N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    May have O-linked mannose residues.

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiP32474.
    PaxDbiP32474.
    PeptideAtlasiP32474.

    Expressioni

    Gene expression databases

    GenevestigatoriP32474.

    Interactioni

    Subunit structurei

    Interacts with EPS1.1 Publication

    Protein-protein interaction databases

    BioGridi32569. 117 interactions.
    IntActiP32474. 1 interaction.
    MINTiMINT-4811793.
    STRINGi4932.YDR518W.

    Structurei

    3D structure databases

    ProteinModelPortaliP32474.
    SMRiP32474. Positions 24-496.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 141112Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini355 – 487133Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi514 – 5174Prevents secretion from ER

    Sequence similaritiesi

    Belongs to the protein disulfide isomerase family.Curated
    Contains 2 thioredoxin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG0526.
    GeneTreeiENSGT00740000115037.
    HOGENOMiHOG000162459.
    KOiK09580.
    OrthoDBiEOG71CFZN.

    Family and domain databases

    Gene3Di3.40.30.10. 2 hits.
    InterProiIPR005792. Prot_disulphide_isomerase.
    IPR012336. Thioredoxin-like_fold.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PfamiPF00085. Thioredoxin. 2 hits.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 4 hits.
    TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS51352. THIOREDOXIN_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P32474-1 [UniParc]FASTAAdd to Basket

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    MQVTTRFISA IVSFCLFASF TLAENSARAT PGSDLLVLTE KKFKSFIESH    50
    PLVLVEFFAP WCLHSQILRP HLEEAASILK EHNVPVVQID CEANSMVCLQ 100
    QTINTYPTLK IFKNGRIFDG QVYRGVKITD EITQYMIQLY EASVIYLNSE 150
    DEIQPYLENA TLPVVINRGL TGLNETYQEV ALDLAEDYVF LSLLDSEDKS 200
    LSIHLPNTTE PILFDGNVDS LVGNSVALTQ WLKVVILPYF TDIEPDLFPK 250
    YISSNLPLAY FFYTSEEELE DYTDLFTQLG KENRGQINFI ALNSTMFPHH 300
    VRFLNMREQF PLFAIHNMIN NLKYGLPQLP EEEYAKLEKP QPLDRDMIVQ 350
    LVKDYREGTA KPIVKSEEIP KEQKSNVYKI VGKTHDDIVH DDDKDVLVKY 400
    YATWCIHSKR FAPIYEEIAN VLASDESVRD KILIAEVDSG ANDILSFPVT 450
    GYPTIALYPA GNNSKPIIFN KIRNLEDVFE FIKESGTHHI DGQAIYDKLH 500
    QAKDSEVSTE DTVHDEL 517
    Length:517
    Mass (Da):58,982
    Last modified:October 1, 1993 - v1
    Checksum:i5F78AD770A6A4083
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti364 – 3641V → G in AAT92989. (PubMed:17322287)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84796 Unassigned DNA. Translation: AAA18226.1.
    U33057 Genomic DNA. Translation: AAB64959.1.
    AY692970 Genomic DNA. Translation: AAT92989.1.
    BK006938 Genomic DNA. Translation: DAA12349.1.
    PIRiA44483.
    RefSeqiNP_010806.1. NM_001180826.1.

    Genome annotation databases

    EnsemblFungiiYDR518W; YDR518W; YDR518W.
    GeneIDi852130.
    KEGGisce:YDR518W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84796 Unassigned DNA. Translation: AAA18226.1 .
    U33057 Genomic DNA. Translation: AAB64959.1 .
    AY692970 Genomic DNA. Translation: AAT92989.1 .
    BK006938 Genomic DNA. Translation: DAA12349.1 .
    PIRi A44483.
    RefSeqi NP_010806.1. NM_001180826.1.

    3D structure databases

    ProteinModelPortali P32474.
    SMRi P32474. Positions 24-496.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32569. 117 interactions.
    IntActi P32474. 1 interaction.
    MINTi MINT-4811793.
    STRINGi 4932.YDR518W.

    Proteomic databases

    MaxQBi P32474.
    PaxDbi P32474.
    PeptideAtlasi P32474.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR518W ; YDR518W ; YDR518W .
    GeneIDi 852130.
    KEGGi sce:YDR518W.

    Organism-specific databases

    CYGDi YDR518w.
    SGDi S000002926. EUG1.

    Phylogenomic databases

    eggNOGi COG0526.
    GeneTreei ENSGT00740000115037.
    HOGENOMi HOG000162459.
    KOi K09580.
    OrthoDBi EOG71CFZN.

    Enzyme and pathway databases

    BioCyci YEAST:YDR518W-MONOMER.

    Miscellaneous databases

    NextBioi 970528.
    PROi P32474.

    Gene expression databases

    Genevestigatori P32474.

    Family and domain databases

    Gene3Di 3.40.30.10. 2 hits.
    InterProi IPR005792. Prot_disulphide_isomerase.
    IPR012336. Thioredoxin-like_fold.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00085. Thioredoxin. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 4 hits.
    TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS51352. THIOREDOXIN_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase."
      Tachibana C., Stevens T.H.
      Mol. Cell. Biol. 12:4601-4611(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "Mutation of yeast Eug1p CXXS active sites to CXXC results in a dramatic increase in protein disulphide isomerase activity."
      Noergaard P., Winther J.R.
      Biochem. J. 358:269-274(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF PDI ACTIVITY, MUTAGENESIS OF SER-65 AND SER-408.
    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 EPS1.

    Entry informationi

    Entry nameiEUG1_YEAST
    AccessioniPrimary (citable) accession number: P32474
    Secondary accession number(s): D6VTD9, E9P901
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3