| basic FUNCTION
| catalyzing protein folding and thiol-disulfide interchange reactions |
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catalyzing disulfide bond formation in the endoplasmic reticulum of eukaryotes |
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involved in DNA-nuclear matrix anchoring |
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may be playing a role with HSPA5 in insulin biosynthesis, although an excess of PDIA2 disrupts normal proinsulin processing (Zhang 2009) |
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involved in insulin disulfide bond formation and an excess of this protein impedes normal insulin folding and probably exit from the ER (Zhang 2009) |
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likely a dynamic equilibrium between ERO1- and glutathione disulphide-mediated oxidation of PDIA2 constitutes an important element of ER redox homeostasis  |
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involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson disease |
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cell surface PDIA2 expression and function regulate the capacity of natriuretic peptides to generate cGMP through interaction with their receptors |
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ER-stress protein that controls tissue factor (TF) -procoagulant activity |
