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ERO1 ER oxidoreductin [ Saccharomyces cerevisiae S288C ]

Gene ID: 854909, updated on 23-Apr-2026
Official Symbol
ERO1
Official Full Name
ER oxidoreductin
Primary source
SGD:S000004599
Locus tag
YML130C
See related
AllianceGenome:SGD:S000004599; FungiDB:YML130C; VEuPathDB:YML130C
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Enables thiol oxidase activity. Involved in protein folding in endoplasmic reticulum. Located in endoplasmic reticulum. Orthologous to human ERO1A (endoplasmic reticulum oxidoreductase 1 alpha) and ERO1B (endoplasmic reticulum oxidoreductase 1 beta). [provided by Alliance of Genome Resources, Jul 2025]
Orthologs
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See ERO1 in Genome Data Viewer
Location:
chromosome: XIII
Exon count:
1
Sequence:
Chromosome: XIII; NC_001145.3 (11483..13174, complement)

Chromosome XIII - NC_001145.3Genomic Context describing neighboring genes Neighboring gene Cos3p Neighboring gene uncharacterized protein Neighboring gene Cox14p Neighboring gene double-strand break repair enhancer MSC1

Genomic Sequence:
NC_001145.3

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
Products Interactant Other Gene Complex Source Pubs Description

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables FAD binding IEA
Inferred from Electronic Annotation
more info
 
enables flavin-dependent sulfhydryl oxidase activity IEA
Inferred from Electronic Annotation
more info
 
enables protein-disulfide reductase activity IBA
Inferred from Biological aspect of Ancestor
more info
 
enables protein-disulfide reductase activity IEA
Inferred from Electronic Annotation
more info
 
enables thiol oxidase activity IDA
Inferred from Direct Assay
more info
PubMed 
enables thiol oxidase activity IEA
Inferred from Electronic Annotation
more info
 
Process Evidence Code Pubs
involved_in protein folding in endoplasmic reticulum IBA
Inferred from Biological aspect of Ancestor
more info
 
involved_in protein folding in endoplasmic reticulum IEA
Inferred from Electronic Annotation
more info
 
involved_in protein folding in endoplasmic reticulum IMP
Inferred from Mutant Phenotype
more info
PubMed 
Component Evidence Code Pubs
located_in endoplasmic reticulum HDA PubMed 
located_in endoplasmic reticulum IDA
Inferred from Direct Assay
more info
PubMed 
located_in endoplasmic reticulum IEA
Inferred from Electronic Annotation
more info
 
is_active_in endoplasmic reticulum membrane IBA
Inferred from Biological aspect of Ancestor
more info
 
located_in endoplasmic reticulum membrane IEA
Inferred from Electronic Annotation
more info
 
Preferred Names
ER oxidoreductin
NP_013576.1
  • Thiol oxidase required for oxidative protein folding in the ER; essential for maintaining ER redox balance; feedback regulated via reduction and oxidation of regulatory bonds; reduced Pdi1p activates Ero1p by direct reduction of Ero1p regulatory bonds; depletion of thiol substrates and accumulation of oxidized Pdi1p results in inactivation of Ero1p by both Pdi1p-mediated oxidation and autonomous oxidation of Ero1p regulatory bonds; ero1-1 mutation complemented by human ERO1L

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001145.3 Reference assembly

    Range
    11483..13174 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001182493.1NP_013576.1  ER oxidoreductin

    See identical proteins and their annotated locations for NP_013576.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6W0F5, E9P913, Q03103
    UniProtKB/TrEMBL
    A6ZLT5, B3LLD0, C7GVB1, C8ZE72, G2WJS7, N1P098
    Conserved Domains (1) summary
    COG5061
    Location:8526
    ERO1; Oxidoreductin, endoplasmic reticulum membrane-associated protein involved in disulfide bond formation [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion]