PDIA2 explained

Protein disulfide isomerase family A member 2 is a protein that in humans is encoded by the PDIA2 gene.^[1]

Function

This gene encodes a member of the disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyze protein folding and thiol-disulfide interchange reactions. The encoded protein has an N-terminal ER-signal sequence, two catalytically active thioredoxin (TRX) domains, two TRX-like domains and a C-terminal ER-retention sequence. The protein plays a role in the folding of nascent proteins in the endoplasmic reticulum by forming disulfide bonds through its thiol isomerase, oxidase, and reductase activity. The encoded protein also possesses estradiol-binding activity and can modulate intracellular estradiol levels. [provided by RefSeq, Sep 2017].

Further reading

• VanderWaal RP, Spitz DR, Griffith CL, Higashikubo R, Roti Roti JL . Evidence that protein disulfide isomerase (PDI) is involved in DNA-nuclear matrix anchoring . J. Cell. Biochem. . 85 . 4 . 689–702 . 2002 . 11968009 . 10.1002/jcb.10169 . 20675717 .
• Ko HS, Uehara T, Nomura Y . Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death . J. Biol. Chem. . 277 . 38 . 35386–92 . 2002 . 12095988 . 10.1074/jbc.M203412200 . free .
• Lumb RA, Bulleid NJ . Is protein disulfide isomerase a redox-dependent molecular chaperone? . EMBO J. . 21 . 24 . 6763–70 . 2002 . 12485997 . 139105 . 10.1093/emboj/cdf685.
• Clissold PM, Bicknell R . The thioredoxin-like fold: hidden domains in protein disulfide isomerases and other chaperone proteins . BioEssays . 25 . 6 . 603–11 . 2003 . 12766950 . 10.1002/bies.10287 .
• Pirneskoski A, Klappa P, Lobell M, Williamson RA, Byrne L, Alanen HI, Salo KE, Kivirikko KI, Freedman RB, Ruddock LW . Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase . J. Biol. Chem. . 279 . 11 . 10374–81 . 2004 . 14684740 . 10.1074/jbc.M312193200 . free .
• Spooner RA, Watson PD, Marsden CJ, Smith DC, Moore KA, Cook JP, Lord JM, Roberts LM . Protein disulphide-isomerase reduces ricin to its A and B chains in the endoplasmic reticulum . Biochem. J. . 383 . Pt 2 . 285–93 . 2004 . 15225124 . 1134069 . 10.1042/BJ20040742 .
• Li SJ, Hong XG, Shi YY, Li H, Wang CC . Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: a small angle X-ray scattering study in solution . J. Biol. Chem. . 281 . 10 . 6581–8 . 2006 . 16407203 . 10.1074/jbc.M508422200 . free .
• Otsu M, Bertoli G, Fagioli C, Guerini-Rocco E, Nerini-Molteni S, Ruffato E, Sitia R . Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44 . Antioxid. Redox Signal. . 8 . 3–4 . 274–82 . 2006 . 16677073 . 10.1089/ars.2006.8.274 .
• Park B, Lee S, Kim E, Cho K, Riddell SR, Cho S, Ahn K . Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing . Cell . 127 . 2 . 369–82 . 2006 . 17055437 . 10.1016/j.cell.2006.08.041 . 2178004 . free .

Notes and References

1. Web site: Entrez Gene: Protein disulfide isomerase family A member 2. 2017-12-20.