| 释义 |
- Function
- References
- Further reading
{{Infobox_gene}}Protein disulfide isomerase family A member 2 is a protein that in humans is encoded by the PDIA2 gene. [1]FunctionThis 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]. References 1. ^{{cite web| title = Entrez Gene: Protein disulfide isomerase family A member 2| url = https://www.ncbi.nlm.nih.gov/gene/64714| accessdate = 2017-12-20}}
Further reading {{refbegin | 2}}- {{cite journal |vauthors=VanderWaal RP, Spitz DR, Griffith CL, Higashikubo R, Roti Roti JL |title=Evidence that protein disulfide isomerase (PDI) is involved in DNA-nuclear matrix anchoring |journal=J. Cell. Biochem. |volume=85 |issue=4 |pages=689–702 |year=2002 |pmid=11968009 |doi=10.1002/jcb.10169 |url=}}
- {{cite journal |vauthors=Ko HS, Uehara T, Nomura Y |title=Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death |journal=J. Biol. Chem. |volume=277 |issue=38 |pages=35386–92 |year=2002 |pmid=12095988 |doi=10.1074/jbc.M203412200 |url=}}
- {{cite journal |vauthors=Lumb RA, Bulleid NJ |title=Is protein disulfide isomerase a redox-dependent molecular chaperone? |journal=EMBO J. |volume=21 |issue=24 |pages=6763–70 |year=2002 |pmid=12485997 |pmc=139105 |doi= |url=}}
- {{cite journal |vauthors=Clissold PM, Bicknell R |title=The thioredoxin-like fold: hidden domains in protein disulfide isomerases and other chaperone proteins |journal=BioEssays |volume=25 |issue=6 |pages=603–11 |year=2003 |pmid=12766950 |doi=10.1002/bies.10287 |url=}}
- {{cite journal |vauthors=Pirneskoski A, Klappa P, Lobell M, Williamson RA, Byrne L, Alanen HI, Salo KE, Kivirikko KI, Freedman RB, Ruddock LW |title=Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase |journal=J. Biol. Chem. |volume=279 |issue=11 |pages=10374–81 |year=2004 |pmid=14684740 |doi=10.1074/jbc.M312193200 |url=}}
- {{cite journal |vauthors=Spooner RA, Watson PD, Marsden CJ, Smith DC, Moore KA, Cook JP, Lord JM, Roberts LM |title=Protein disulphide-isomerase reduces ricin to its A and B chains in the endoplasmic reticulum |journal=Biochem. J. |volume=383 |issue=Pt 2 |pages=285–93 |year=2004 |pmid=15225124 |pmc=1134069 |doi=10.1042/BJ20040742 |url=}}
- {{cite journal |vauthors=Li SJ, Hong XG, Shi YY, Li H, Wang CC |title=Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: a small angle X-ray scattering study in solution |journal=J. Biol. Chem. |volume=281 |issue=10 |pages=6581–8 |year=2006 |pmid=16407203 |doi=10.1074/jbc.M508422200 |url=}}
- {{cite journal |vauthors=Otsu M, Bertoli G, Fagioli C, Guerini-Rocco E, Nerini-Molteni S, Ruffato E, Sitia R |title=Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44 |journal=Antioxid. Redox Signal. |volume=8 |issue=3-4 |pages=274–82 |year=2006 |pmid=16677073 |doi=10.1089/ars.2006.8.274 |url=}}
- {{cite journal |vauthors=Park B, Lee S, Kim E, Cho K, Riddell SR, Cho S, Ahn K |title=Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing |journal=Cell |volume=127 |issue=2 |pages=369–82 |year=2006 |pmid=17055437 |doi=10.1016/j.cell.2006.08.041 |url=}}
{{refend}}{{NLM content}}{{gene-16-stub}} 1 : Endoplasmic reticulum resident proteins |