| Modification Notes |
Oxidoreductase-protein disulfide isomerase (PDI) is a homodimer that catalyzes thiol-disulfide exchange, mediates folding of newly synthesized proteins and functions as a molecular chaperone. PDIR (Protein disulfide isomerase-related protein), also known as PDIA5 (Protein disulfide-isomerase A5), is a 519 amino acid protein that catalyzes the rearrangement of sulfur-sulfur bonds in various proteins. Localized to the lumen of the endoplasmic reticulum (ER), PDIR has an oxidative refolding activity that is specific for å1-antitrypsin (AAT) and aids in the formation of disulfide bonds in the ER lumen. PDIR contains one ER retention signal at its C-terminus and three thioredoxin (CXXC) motifs which mediate the substrate-specific isomerase, chaperone and redox activity of PDIR. |