Ero1a endoplasmic reticulum oxidoreductase 1 alpha [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Ero1aprovided by MGI
Official Full Name: endoplasmic reticulum oxidoreductase 1 alphaprovided by MGI
Primary source: MGI:MGI:1354385
See related: Ensembl:ENSMUSG00000021831 AllianceGenome:MGI:1354385
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Ero1l; ERO1-L
Summary: This gene encodes a member of the endoplasmic reticulum oxidoreductin family. The encoded protein is localized to the endoplasmic reticulum and promotes the formation of disulfide bonds by oxidizing protein disulfide isomerase. This gene may play a role in endoplasmic reticulum stress-induced apoptosis and the cellular response to hypoxia. [provided by RefSeq, Feb 2011]
Expression: Ubiquitous expression in placenta adult (RPKM 26.9), liver E18 (RPKM 11.5) and 26 other tissues See more
Orthologs: human all
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Genomic context

Location:: 14 C1; 14 22.86 cM

Exon count:: 16

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	14	NC_000080.7 (45520544..45556029, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	14	NC_000080.6 (45283087..45318572, complement)

Chromosome 14 - NC_000080.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

SEPN1-related myopathy depends on the oxidoreductase ERO1A and is druggable with the chemical chaperone TUDCA.
Title: SEPN1-related myopathy depends on the oxidoreductase ERO1A and is druggable with the chemical chaperone TUDCA.
A Critical Role for ERO1alpha in Arterial Thrombosis and Ischemic Stroke.
Title: A Critical Role for ERO1α in Arterial Thrombosis and Ischemic Stroke.
Homocysteine facilitates endoplasmic reticulum stress and apoptosis of hepatocytes by suppressing ERO1alpha expression via cooperation between DNMT1 and G9a.
Title: Homocysteine facilitates endoplasmic reticulum stress and apoptosis of hepatocytes by suppressing ERO1α expression via cooperation between DNMT1 and G9a.
Endophilin A2-mediated alleviation of endoplasmic reticulum stress-induced cardiac injury involves the suppression of ERO1alpha/IP3R signaling pathway.
Title: Endophilin A2-mediated alleviation of endoplasmic reticulum stress-induced cardiac injury involves the suppression of ERO1α/IP(3)R signaling pathway.
ERO1alpha inhibits cell apoptosis and regulates steroidogenesis in mouse granulosa cells.
Title: ERO1α inhibits cell apoptosis and regulates steroidogenesis in mouse granulosa cells.
ERO1alpha promotes testosterone secretion in hCG-stimulated mouse Leydig cells via activation of the PI3K/AKT/mTOR signaling pathway.
Title: ERO1α promotes testosterone secretion in hCG-stimulated mouse Leydig cells via activation of the PI3K/AKT/mTOR signaling pathway.
this study shows that the hypoxia-inducible ER-resident oxidase ERO1-alpha plays an important role in the hypoxia-induced augmentation of MHC class I-peptide complex expression
Title: Hypoxia augments MHC class I antigen presentation via facilitation of ERO1-α-mediated oxidative folding in murine tumor cells.
Data (including data from knockout mice) suggest that up-regulation of expression of ERO1alpha (oxidoreductin-1-L-alpha) and CHOP (c/EBP-homologous protein) is involved in liver apoptosis/necrosis exhibited in acute liver failure.
Title: C/EBP homologous protein (CHOP) contributes to hepatocyte death via the promotion of ERO1α signalling in acute liver failure.
These results suggest that overexpression of ERO1-alpha in the tumor inhibits the T cell response by recruiting polymorphonuclear myeloid-derived suppressor cells
Title: Cancer-associated oxidoreductase ERO1-α drives the production of tumor-promoting myeloid-derived suppressor cells via oxidative protein folding.
ER stress induced by misfolded proinsulin was limited by increased expression of Ero1alpha, suggesting that enhancing the oxidative folding of proinsulin may be a viable therapeutic strategy in the treatment of type 2 diabetes.
Title: Endoplasmic reticulum oxidoreductin-1α (Ero1α) improves folding and secretion of mutant proinsulin and limits mutant proinsulin-induced endoplasmic reticulum stress.

Submit: New GeneRIF Correction See all GeneRIFs (18)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (3)
Gene trapped (1)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables FAD binding	IEA Inferred from Electronic Annotation more info
enables oxidoreductase activity	IDA Inferred from Direct Assay more info	PubMed
enables oxidoreductase activity	ISO Inferred from Sequence Orthology more info
enables protein-disulfide reductase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein-disulfide reductase activity	IDA Inferred from Direct Assay more info	PubMed
enables thiol oxidase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
acts_upstream_of_or_within L-ascorbic acid metabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within brown fat cell differentiation	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within cell redox homeostasis	IGI Inferred from Genetic Interaction more info	PubMed
involved_in cell redox homeostasis	ISO Inferred from Sequence Orthology more info
involved_in cell redox homeostasis	ISS Inferred from Sequence or Structural Similarity more info
involved_in cellular response to hypoxia	IEA Inferred from Electronic Annotation more info
involved_in chaperone cofactor-dependent protein refolding	IEA Inferred from Electronic Annotation more info
involved_in chaperone cofactor-dependent protein refolding	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within collagen fibril organization	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within endoplasmic reticulum unfolded protein response	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within extracellular matrix organization	IGI Inferred from Genetic Interaction more info	PubMed
involved_in intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within peptidyl-proline hydroxylation to 4-hydroxy-L-proline	IGI Inferred from Genetic Interaction more info	PubMed
acts_upstream_of_or_within protein folding	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within protein folding	ISO Inferred from Sequence Orthology more info	PubMed
involved_in protein folding	ISO Inferred from Sequence Orthology more info
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
acts_upstream_of_or_within protein maturation by protein folding	IGI Inferred from Genetic Interaction more info	PubMed
involved_in release of sequestered calcium ion into cytosol	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in response to endoplasmic reticulum stress	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within response to oxidative stress	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within skeletal muscle tissue development	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within transforming growth factor beta receptor signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in Golgi lumen	ISO Inferred from Sequence Orthology more info
located_in Golgi lumen	ISS Inferred from Sequence or Structural Similarity more info
located_in dendrite	IEA Inferred from Electronic Annotation more info
located_in dendrite	ISO Inferred from Sequence Orthology more info
is_active_in endoplasmic reticulum	IMP Inferred from Mutant Phenotype more info	PubMed
located_in endoplasmic reticulum	ISO Inferred from Sequence Orthology more info
located_in endoplasmic reticulum	ISS Inferred from Sequence or Structural Similarity more info
is_active_in endoplasmic reticulum membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in endoplasmic reticulum membrane	ISO Inferred from Sequence Orthology more info	PubMed
located_in extracellular space	ISO Inferred from Sequence Orthology more info
located_in extracellular space	ISS Inferred from Sequence or Structural Similarity more info

General protein information

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Preferred Names: ERO1-like protein alpha

Names: ERO1-L-alpha; ERO1-like; endoplasmic oxidoreductin-1-like protein; endoplasmic reticulum oxidation 1; endoplasmic reticulum oxidoreductase alpha; endoplasmic reticulum oxidoreductin-1-like protein; oxidoreductin-1-L-alpha

NP_056589.1

EC 1.8.4.-

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.