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FLASH GENE
Symbol ERO1A contributors: mct/npt - updated : 11-05-2016
HGNC name endoplasmic reticulum oxidoreductase alpha
HGNC id 13280
Location 14q22.1      Physical location : -
Synonym name
  • endoplasmic reticulum oxidoreductin 1 (S.cerevisiae-like alpha)
  • endoplasmic oxidoreductin-1-like protein
  • Synonym symbol(s) ERO1LA, ERO1-alpha, ERO1L, ERO1-L, ERO1-L-alpha,
    EC.number 1.8.4.-
    DNA
    TYPE functioning gene
    STRUCTURE 56.02 kb     16 Exon(s)
    MAPPING cloned Y linked N status provisional
    RNA
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    16 - 5512 - 468 - 2014 24758166
    EXPRESSION
    Type widely
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    digestiveesophagus   highly
    Endocrineadrenal gland   highly
    Reproductivefemale systemuteruscervix highly
    Respiratoryrespiratory tracttrachea  highly
    Visualeye    
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    PROTEIN
    PHYSICAL PROPERTIES
    STRUCTURE
    motifs/domains
  • an EF-calcium binding motif
  • N-glycosylation sites
  • potential active site was predicted as the binding site of FAD (Chu 2009)
  • conjugated GlycoP
    HOMOLOGY
    interspecies ortholog to yeast S.cerevisiae ERO1 required for oxidative protein folding
    Homologene
    FAMILY
  • EROs family
  • CATEGORY chaperone/stress , regulatory
    SUBCELLULAR LOCALIZATION     plasma membrane
        intracellular
    intracellular,cytoplasm,organelle,mitochondria,matrix
    intracellular,cytoplasm,organelle,lumen
    intracellular,cytoplasm,organelle,membrane
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    text
  • type II integral membrane protein
  • ERO1alpha is almost exclusively found on the mitochondria-associated membrane (MAM), and the localization of ERO1A on the MAM is dependent on oxidizing conditions within the ER
  • basic FUNCTION
  • essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds
  • may be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress
  • combined activities of ERO1L and protein disulphide isomerase are necessary for formation of disulphide bonds within the mammalian endoplasmic reticulum (ER) (Baker 2008)
  • hypoxic induction of ERO1L is the key adaptive response in a previously unrecognized HIF-1-mediated pathway that operates to improve protein secretion under hypoxia and might be harnessed for inhibiting tumor growth via inhibiting VEGF-driven angiogenesis (May 2005)
  • catalyzes the formation of disulfide bond and hence plays an essential role in protein folding (Chu 2009)
  • key controller of oxidative folding and ER redox homeostasis, enriched in mitochondrial-associated ER membranes (MAM) and regulating Ca(2+) fluxes
  • levels, subcellular localization, and activity of ERO1A coordinately regulate Ca(2+) and redox homeostasis and signaling in the early secretory compartment
  • ERP44 together with ERO1A plays an important role in disulfide formation of SLC6A4, which may be a prerequisite step for the assembly of SLC6A4 molecules in oligomeric form
  • ERO1A hyperactivity affects cell viability when cellular glutathione levels are compromised
  • different binding properties of ERO1A and PRDX4 increase the robustness of ER redox homeostasis
  • oxidizing enzyme that exists in the endoplasmic reticulum and is induced under hypoxia
  • cancer-associated ERO1A regulates the expression of the MHC class I molecule via oxidative folding
  • CELLULAR PROCESS protein, post translation, folding
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule cofactor,
  • FAD
  • protein
  • interacts with the oxidoreductase PDILT, demonstrating that the N-terminal cysteine of the CXXC sequence is not required for binding of PDI family proteins to ER oxidoreductases
  • GPX7 and GPX8 may represent a novel route for the productive use of peroxide produced by ERO1A during disulfide bond formation
  • potential ability of ERP44 to inhibit ERO1A activity may suggest its physiological role in ER redox and protein homeostasis
  • ERP44 plays a critical role in the release of proteins from the ER via binding to ERO1A
  • TXNDC5 is involved in insulin production as well as in adiponectin signaling and interacts specifically with the redox-regulatory endoplasmic reticulum proteins ERO1A and PRDX4
  • PDIA2 binds preferentially ERO1A, whereas ERP44 equally retains ERO1A and PRDX4
  • ERO1A oxidizes PDIA2 to introduce disulfides into substrates, and PDIA2 can feedback-regulate ERO1A activity
  • ERO1A, a target of DDIT3, is an important oxidizing enzyme that regulates reactive oxygen species (ROS), which play a prominent role in hepatocellular death during acute liver failure (ALF)
  • cell & other
    REGULATION
    Other regulated by non-catalytic disulphides (Baker 2008)
    its activity is tightly regulated by a mechanism that requires the formation of regulatory disulfides (
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    SystemTypeDisorderPubmed
    digestiveliver 
    targeting DDIT3/ERO1A signalling could be a novel therapeutic approach during acute liver failure (ALF)
    ANIMAL & CELL MODELS