ERO1 ER oxidoreductin [Saccharomyces cerevisiae S288C] - Gene

Summary

Go to the top of the page Help

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, Dec 2024]
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help

See ERO1 in Genome Data Viewer

Location:: chromosome: XIII

Exon count:: 1

Sequence:: Chromosome: XIII; NC_001145.3 (11483..13174, complement)

Chromosome XIII - NC_001145.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_001145.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

It has been concluded that soluble eukaryotic fumarate reductases can maintain an oxidizing environment under anaerobic conditions, either by oxidizing cellular flavin cofactors or by a direct interaction with flavoenzymes such as Ero1.
Title: Molecular basis of maintaining an oxidizing environment under anaerobiosis by soluble fumarate reductase.
Increased endoplasmic reticulum glutathione import triggers H2O2-dependent Bip oxidation through Ero1 reductive activation, which inhibits glutathione import in a negative regulatory loop.
Title: Endoplasmic Reticulum Transport of Glutathione by Sec61 Is Regulated by Ero1 and Bip.
ERO1 is enzymatically active even with its regulatory disulfides intact, and further activation of ERO1 by reduction of the regulatory disulfides requires the reduction of non-catalytic Cys(90)-Cys(97)disulfide in PDI1.
Title: Novel Roles of the Non-catalytic Elements of Yeast Protein-disulfide Isomerase in Its Interplay with Endoplasmic Reticulum Oxidoreductin 1.
Coexpression of Kar2p, Pdi1p and Ero1p gave a synergistic effect on CPY expression
Title: Effects of signal sequences and folding accessory proteins on extracellular expression of carboxypeptidase Y in recombinant Saccharomyces cerevisiae.
Balanced Ero1 activation and inactivation establishes ER redox homeostasis.
Title: Balanced Ero1 activation and inactivation establishes ER redox homeostasis.
the intramolecular electron transfer from the a domain to the a' domain within PDI during its oxidation by ERO1alpha.
Title: Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway.
Data of the crystal structure revealed local changes compared to the wild-type enzyme around the sites of mutation, but no conformational transitions within 25 A of the active site were observed.
Title: Steps in reductive activation of the disulfide-generating enzyme Ero1p.
analysis of the oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum
Title: Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum.
The ero1-1 leu2 strain does not grow in standard synthetic complete medium at 30 degrees C, a defect that can be remedied by increasing the L-leucine concentration in the medium or by transforming the ero1-1 leu2 strain with the LEU2 wild-type allele.
Title: Genetic interaction between the ero1-1 and leu2 mutations in Saccharomyces cerevisiae.
PDI has a role in native disulfide bond formation in a reaction driven by Ero1p
Title: Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.

Submit: New GeneRIF Correction See all GeneRIFs (13)

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables FAD binding	IEA Inferred from Electronic Annotation more info
enables oxidoreductase 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 more info	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
located_in membrane	IEA Inferred from Electronic Annotation more info

General protein information

Go to the top of the page Help

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

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

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

Reference assembly

Genomic

NC_001145.3 Reference assembly

Range

11483..13174 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001182493.1 → NP_013576.1 TPA: ER oxidoreductin [Saccharomyces cerevisiae S288C]

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:8 → 526

ERO1; Oxidoreductin, endoplasmic reticulum membrane-associated protein involved in disulfide bond formation [Posttranslational modification, protein turnover, chaperones / Intracellular trafficking and secretion]