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Q03103

- ERO1_YEAST

UniProt

Q03103 - ERO1_YEAST

Protein

Endoplasmic oxidoreductin-1

Gene

ERO1

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 120 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI1 to transfer oxidizing equivalent. Also able to oxidize directly the PDI related protein MPD2. Does not oxidize all PDI related proteins, suggesting that it can discriminate between PDI1 and related proteins. Reoxidation of ERO1 probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress.5 Publications

    Cofactori

    FAD.1 Publication

    Enzyme regulationi

    Enzyme activity is tightly regulated to prevent the accumulation of reactive oxygen species in the endoplasmic reticulum. Reversibly down-regulated by the formation of disulfide bonds between Cys-150 and Cys-295.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei187 – 1871FAD1 Publication
    Binding sitei189 – 1891FAD1 Publication
    Binding sitei200 – 2001FAD1 Publication
    Binding sitei228 – 2281FAD1 Publication
    Binding sitei231 – 2311FAD1 Publication
    Binding sitei260 – 2601FAD1 Publication
    Active sitei352 – 3521Nucleophile
    Active sitei355 – 3551

    GO - Molecular functioni

    1. oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: InterPro
    2. protein disulfide isomerase activity Source: SGD
    3. thiol oxidase activity Source: SGD

    GO - Biological processi

    1. oxidation-reduction process Source: SGD
    2. protein folding Source: SGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Transport

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16234.
    YEAST:G3O-32708-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoplasmic oxidoreductin-1 (EC:1.8.4.-)
    Alternative name(s):
    Endoplasmic reticulum oxidoreductase protein 1
    Gene namesi
    Name:ERO1
    Ordered Locus Names:YML130C
    ORF Names:YM4987.05C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYML130c.
    SGDiS000004599. ERO1.

    Subcellular locationi

    Endoplasmic reticulum membrane 3 Publications; Peripheral membrane protein 3 Publications; Lumenal side 3 Publications

    GO - Cellular componenti

    1. endoplasmic reticulum Source: SGD
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi90 – 901C → A: No effect. 2 Publications
    Mutagenesisi100 – 1001C → A: Impairs the capture of mixed-disulfide with PDI1 thereby blocking its function. Loss of activity; when associated with A-105. 2 Publications
    Mutagenesisi105 – 1051C → A: Loss of activity. 2 Publications
    Mutagenesisi143 – 1431C → A: No effect; when associated with A-166. 1 Publication
    Mutagenesisi150 – 1501C → A: Loss of regulatory disulfide bond and strongly increased activity towards PDI; when associated with A-295. 1 Publication
    Mutagenesisi166 – 1661C → A: No effect; when associated with A-143. 1 Publication
    Mutagenesisi208 – 2081C → A: No effect. 1 Publication
    Mutagenesisi229 – 2291G → S in ERO1-1; induces defective folding of disulfide proteins. 1 Publication
    Mutagenesisi231 – 2311H → Y in ERO1-2; induces defective folding of disulfide proteins. 1 Publication
    Mutagenesisi295 – 2951C → A: Loss of regulatory disulfide bond and strongly increased activity towards PDI; when associated with A-150. 1 Publication
    Mutagenesisi349 – 3491C → A: Does not affect activity but increases by twofold the amount of protein found in mixed disulfide with PDI1 or MPD2. 1 Publication
    Mutagenesisi352 – 3521C → A: Loss of activity. Prevents its reoxidation thereby blocking its function. 2 Publications
    Mutagenesisi355 – 3551C → A: Loss of activity. Prevents its reoxidation thereby blocking its function. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 563545Endoplasmic oxidoreductin-1PRO_0000008429Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi21 – 211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi35 – 351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi90 ↔ 349
    Disulfide bondi100 ↔ 105Redox-active
    Glycosylationi130 – 1301N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi143 ↔ 166
    Disulfide bondi150 ↔ 295
    Glycosylationi342 – 3421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi352 ↔ 355Redox-active
    Glycosylationi425 – 4251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The Cys-100/Cys-105 and Cys-352/Cys-355 disulfide bonds constitute the redox-active center. The Cys-100/Cys-105 disulfide bond may accept electron from PDI1 and funnel them to the active site disulfide Cys-352/Cys-355.
    N-glycosylated.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ03103.
    PaxDbiQ03103.
    PeptideAtlasiQ03103.

    Expressioni

    Inductioni

    By unfolded protein response (UPR).2 Publications

    Gene expression databases

    GenevestigatoriQ03103.

    Interactioni

    Subunit structurei

    May function both as a monomer and a homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi35075. 45 interactions.
    DIPiDIP-4515N.
    IntActiQ03103. 11 interactions.
    MINTiMINT-503775.
    STRINGi4932.YML130C.

    Structurei

    Secondary structure

    1
    563
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi56 – 7318
    Turni77 – 793
    Beta strandi80 – 867
    Beta strandi91 – 933
    Beta strandi95 – 984
    Turni102 – 1054
    Beta strandi109 – 1113
    Helixi113 – 1153
    Helixi118 – 1203
    Helixi122 – 1254
    Turni130 – 1323
    Beta strandi133 – 1353
    Beta strandi137 – 1393
    Helixi141 – 1433
    Helixi146 – 1494
    Turni152 – 1543
    Beta strandi159 – 1613
    Helixi165 – 1684
    Beta strandi176 – 1805
    Turni181 – 1833
    Helixi193 – 20513
    Helixi216 – 24025
    Beta strandi241 – 2433
    Turni245 – 2473
    Helixi254 – 2607
    Turni261 – 2633
    Helixi265 – 28521
    Helixi286 – 2883
    Helixi297 – 31115
    Helixi316 – 3194
    Turni325 – 3273
    Helixi330 – 34617
    Helixi347 – 3493
    Helixi353 – 37624
    Helixi381 – 3899
    Helixi393 – 42432

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RP4X-ray2.20A56-424[»]
    1RQ1X-ray2.80A56-424[»]
    3M31X-ray1.85A56-424[»]
    3NVJX-ray3.20A56-424[»]
    ProteinModelPortaliQ03103.
    SMRiQ03103. Positions 55-424.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ03103.

    Family & Domainsi

    Domaini

    The C-terminal part (437-563) is required for the association with the endoplasmic reticulum lumen membrane.1 Publication

    Sequence similaritiesi

    Belongs to the EROs family.Curated

    Keywords - Domaini

    Redox-active center, Signal

    Phylogenomic databases

    eggNOGiCOG5061.
    GeneTreeiENSGT00390000007753.
    HOGENOMiHOG000158050.
    OMAiCDRCRLW.
    OrthoDBiEOG7SV15N.

    Family and domain databases

    InterProiIPR007266. Ero1.
    [Graphical view]
    PANTHERiPTHR12613. PTHR12613. 1 hit.
    PfamiPF04137. ERO1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF017205. ERO1. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q03103-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRLRTAIATL CLTAFTSATS NNSYIATDQT QNAFNDTHFC KVDRNDHVSP    50
    SCNVTFNELN AINENIRDDL SALLKSDFFK YFRLDLYKQC SFWDANDGLC 100
    LNRACSVDVV EDWDTLPEYW QPEILGSFNN DTMKEADDSD DECKFLDQLC 150
    QTSKKPVDIE DTINYCDVND FNGKNAVLID LTANPERFTG YGGKQAGQIW 200
    STIYQDNCFT IGETGESLAK DAFYRLVSGF HASIGTHLSK EYLNTKTGKW 250
    EPNLDLFMAR IGNFPDRVTN MYFNYAVVAK ALWKIQPYLP EFSFCDLVNK 300
    EIKNKMDNVI SQLDTKIFNE DLVFANDLSL TLKDEFRSRF KNVTKIMDCV 350
    QCDRCRLWGK IQTTGYATAL KILFEINDAD EFTKQHIVGK LTKYELIALL 400
    QTFGRLSESI ESVNMFEKMY GKRLNGSENR LSSFFQNNFF NILKEAGKSI 450
    RYTIENINST KEGKKKTNNS QSHVFDDLKM PKAEIVPRPS NGTVNKWKKA 500
    WNTEVNNVLE AFRFIYRSYL DLPRNIWELS LMKVYKFWNK FIGVADYVSE 550
    ETREPISYKL DIQ 563
    Length:563
    Mass (Da):65,033
    Last modified:November 1, 1997 - v1
    Checksum:i928CE700AE6137EF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti555 – 5551P → L in AAT93069. (PubMed:17322287)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z50178 Genomic DNA. Translation: CAA90553.1.
    AY693050 Genomic DNA. Translation: AAT93069.1.
    BK006946 Genomic DNA. Translation: DAA09769.1.
    PIRiS58198.
    RefSeqiNP_013576.1. NM_001182493.1.

    Genome annotation databases

    EnsemblFungiiYML130C; YML130C; YML130C.
    GeneIDi854909.
    KEGGisce:YML130C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z50178 Genomic DNA. Translation: CAA90553.1 .
    AY693050 Genomic DNA. Translation: AAT93069.1 .
    BK006946 Genomic DNA. Translation: DAA09769.1 .
    PIRi S58198.
    RefSeqi NP_013576.1. NM_001182493.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RP4 X-ray 2.20 A 56-424 [» ]
    1RQ1 X-ray 2.80 A 56-424 [» ]
    3M31 X-ray 1.85 A 56-424 [» ]
    3NVJ X-ray 3.20 A 56-424 [» ]
    ProteinModelPortali Q03103.
    SMRi Q03103. Positions 55-424.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35075. 45 interactions.
    DIPi DIP-4515N.
    IntActi Q03103. 11 interactions.
    MINTi MINT-503775.
    STRINGi 4932.YML130C.

    Proteomic databases

    MaxQBi Q03103.
    PaxDbi Q03103.
    PeptideAtlasi Q03103.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YML130C ; YML130C ; YML130C .
    GeneIDi 854909.
    KEGGi sce:YML130C.

    Organism-specific databases

    CYGDi YML130c.
    SGDi S000004599. ERO1.

    Phylogenomic databases

    eggNOGi COG5061.
    GeneTreei ENSGT00390000007753.
    HOGENOMi HOG000158050.
    OMAi CDRCRLW.
    OrthoDBi EOG7SV15N.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-16234.
    YEAST:G3O-32708-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q03103.
    NextBioi 977902.

    Gene expression databases

    Genevestigatori Q03103.

    Family and domain databases

    InterProi IPR007266. Ero1.
    [Graphical view ]
    PANTHERi PTHR12613. PTHR12613. 1 hit.
    Pfami PF04137. ERO1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF017205. ERO1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum."
      Frand A.R., Kaiser C.A.
      Mol. Cell 1:161-170(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, INDUCTION.
    5. "Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum."
      Pollard M.G., Travers K.J., Weissman J.S.
      Mol. Cell 1:171-182(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, INDUCTION, MUTAGENESIS OF HIS-231.
    6. "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: FUNCTION.
    7. "Biochemical basis of oxidative protein folding in the endoplasmic reticulum."
      Tu B.P., Ho-Schleyer S.C., Travers K.J., Weissman J.S.
      Science 290:1571-1574(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR.
    8. "Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum."
      Frand A.R., Kaiser C.A.
      Mol. Biol. Cell 11:2833-2843(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-90; CYS-100; CYS-105; CYS-208; CYS-349; CYS-352 AND CYS-355.
    9. "The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function."
      Pagani M., Pilati S., Bertoli G., Valsasina B., Sitia R.
      FEBS Lett. 508:117-120(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DOMAIN.
    10. "The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum."
      Tu B.P., Weissman J.S.
      Mol. Cell 10:983-994(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Oxidative protein folding in eukaryotes: mechanisms and consequences."
      Tu B.P., Weissman J.S.
      J. Cell Biol. 164:341-346(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    12. "Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1."
      Sevier C.S., Qu H., Heldman N., Gross E., Fass D., Kaiser C.A.
      Cell 129:333-344(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, DISULFIDE BONDS, MUTAGENESIS OF CYS-90; CYS-100; CYS-105; CYS-143; CYS-150; CYS-166; CYS-295; CYS-352 AND CYS-355.
    13. "Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell."
      Gross E., Kastner D.B., Kaiser C.A., Fass D.
      Cell 117:601-610(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 56-424 IN COMPLEX WITH FAD, POTENTIAL HOMODIMERIZATION, DISULFIDE BONDS, MUTAGENESIS OF GLY-229.

    Entry informationi

    Entry nameiERO1_YEAST
    AccessioniPrimary (citable) accession number: Q03103
    Secondary accession number(s): D6W0F5, E9P913
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 120 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

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

    External Data

    Dasty 3