ERO1A

ERO1A (Endoplasmic Reticulum Oxidoreductase 1 Alpha) is a Protein Coding gene. Diseases associated with ERO1A include Cholera. Among its related pathways are Peptide hormone metabolism and Detoxification of Reactive Oxygen Species. An important paralog of this gene is ERO1B.

Endoplasmic Reticulum Oxidoreductase 1 Alpha

Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1.

Animal organ senescence Source: Ensembl
Brown fat cell differentiation Source: Ensembl
Cell redox homeostasis Source: Ensembl
Cellular protein modification process Source: ProtInc
Cellular response to hypoxia Source: Ensembl
Chaperone cofactor-dependent protein refolding Source: UniProtKB
Endoplasmic reticulum unfolded protein response Source: Ensembl
Extracellular matrix organization Source: Ensembl
Intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
Peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: Ensembl
Protein folding Source: ProtInc
Protein folding in endoplasmic reticulum Source: GO_Central
Protein maturation by protein folding Source: Ensembl
Release of sequestered calcium ion into cytosol Source: UniProtKB
Response to endoplasmic reticulum stress Source: UniProtKB
Response to oxidative stress Source: Ensembl
Response to temperature stimulus Source: ProtInc

Endoplasmic reticulum membrane. The association with ERP44 is essential for its retention in the endoplasmic reticulum.

N-glycosylated.
The Cys-94/Cys-99 and Cys-394/Cys-397 disulfide bonds constitute the redox-active center. The Cys-94/Cys-99 disulfide bond may accept electron from P4HB and funnel them to the active site disulfide Cys-394/Cys-397 (By similarity). The regulatory Cys-99/Cys-104 disulfide bond stabilizes the other regulatory bond Cys-94/Cys-131 (PubMed:23027870).