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MGP005039

UniProt Annotations

Entry Information

Gene Name	ERO1-like (S. cerevisiae)
Protein Entry	ERO1A_HUMAN
UniProt ID	Q96HE7
Species	Human

Comments

Comment type	Description
Cofactor	Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269\|PubMed:18971943, ECO:0000269\|PubMed:20834232};
Enzyme Regulation	Enzyme activity is tightly regulated to prevent the accumulation of reactive oxygen species in the endoplasmic reticulum. Reversibly down-regulated by the formation of disulfide bonds between the active site Cys-94 and Cys-131, and between Cys- 99 and Cys-104. Glutathione may be required to regulate its activity in the endoplasmic reticulum. {ECO:0000269\|PubMed:15161913, ECO:0000269\|PubMed:18833192, ECO:0000269\|PubMed:18971943}.
Function	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. {ECO:0000269\|PubMed:10671517, ECO:0000269\|PubMed:10970843, ECO:0000269\|PubMed:11707400, ECO:0000269\|PubMed:12403808, ECO:0000269\|PubMed:18833192, ECO:0000269\|PubMed:18971943, ECO:0000269\|PubMed:23027870}.
Induction	Stimulated by hypoxia; suggesting that it is regulated via the HIF-pathway. {ECO:0000269\|PubMed:12752442}.
Interaction	P07237:P4HB; NbExp=2; IntAct=EBI-2564539, EBI-395883; P30101:PDIA3; NbExp=3; IntAct=EBI-2564539, EBI-979862;
Ptm	N-glycosylated. {ECO:0000269\|PubMed:10671517, ECO:0000269\|PubMed:10970843, ECO:0000269\|PubMed:19159218}.
Ptm	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). {ECO:0000250, ECO:0000269\|PubMed:23027870}.
Similarity	Belongs to the EROs family. {ECO:0000305}.
Subcellular Location	Endoplasmic reticulum membrane {ECO:0000269\|PubMed:10671517, ECO:0000269\|PubMed:14517240}; Peripheral membrane protein {ECO:0000269\|PubMed:10671517, ECO:0000269\|PubMed:14517240}; Lumenal side {ECO:0000269\|PubMed:10671517, ECO:0000269\|PubMed:14517240}. Note=The association with ERP44 is essential for its retention in the endoplasmic reticulum.
Subunit	Predominantly monomer. May function both as a monomer and a homodimer. Interacts with PDILT. {ECO:0000269\|PubMed:11847130, ECO:0000269\|PubMed:15475357, ECO:0000269\|PubMed:18971943}.
Tissue Specificity	Widely expressed at low level. Expressed at high level in upper digestive tract. Highly expressed in esophagus. Weakly expressed in stomach and duodenum. {ECO:0000269\|PubMed:10818100}.