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Proteins/UNIPROT:Q96HE7
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. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. 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..
Function from UniProtKB (Q96HE7), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 0
279 statements
279 statements · 3 reference databases · Subject: ERO1A · Sources: Hetionet, Reactome, UniProt
2 reactions
2CHEBI:16520+dioxygenCHEBI:17412+hydrogen peroxide
Catalysed by QSOX1 or GFER or QSOX2 or ERO1B or ERO1A
Reaction pageLeft to rightBalance undeterminable
Rhea RHEA:17357CC BY 4.0Reference data
[protein]-dithiol+dioxygen[protein]-disulfide+hydrogen peroxide
Catalysed by GFER or
6 names
Resolves to: ERO1A
Reaction pageLeft to rightBalance undeterminable
Rhea RHEA:59116CC BY 4.0Reference data