PDIA2

Protein disulfide isomerase family A member 2 is a protein that in humans is encoded by the PDIA2 gene. [5]

PDIA2
Identifiers
Aliases	PDIA2, PDA2, PDI, PDIP, PDIR, protein disulfide isomerase family A member 2
External IDs	OMIM: 608012 MGI: 1916441 HomoloGene: 55994 GeneCards: PDIA2
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16p13.3 Start 283,152 bp[1] End 287,215 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17|17 A3.3 Start 26,195,999 bp[2] End 26,199,087 bp[2]
Gene ontology Molecular function • disulfide oxidoreductase activity • steroid binding • GO:0001948 protein binding • peptidyl-proline 4-dioxygenase activity • isomerase activity • lipid binding • protein disulfide isomerase activity • peptide disulfide oxidoreductase activity Cellular component • endoplasmic reticulum lumen • endoplasmic reticulum Biological process • protein retention in ER lumen • protein folding in endoplasmic reticulum • protein folding • regulation of oxidative stress-induced intrinsic apoptotic signaling pathway • cell redox homeostasis • response to endoplasmic reticulum stress • oxidation-reduction process • peptidyl-proline hydroxylation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	64714	69191
Ensembl	ENSG00000185615	ENSMUSG00000024184
UniProt	Q13087	D3Z6P0
RefSeq (mRNA)	NM_006849	NM_001081070
RefSeq (protein)	NP_006840	NP_001074539
Location (UCSC)	Chr 16: 0.28 – 0.29 Mb	Chr 17: 26.2 – 26.2 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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].

References

1. GRCh38: Ensembl release 89: ENSG00000185615 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000024184 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: Protein disulfide isomerase family A member 2". Retrieved 2017-12-20.

Further reading

• VanderWaal RP, Spitz DR, Griffith CL, Higashikubo R, Roti Roti JL (2002). "Evidence that protein disulfide isomerase (PDI) is involved in DNA-nuclear matrix anchoring". J. Cell. Biochem. 85 (4): 689–702. doi:10.1002/jcb.10169. PMID 11968009. S2CID 20675717.
• Ko HS, Uehara T, Nomura Y (2002). "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. doi:10.1074/jbc.M203412200. PMID 12095988.
• Lumb RA, Bulleid NJ (2002). "Is protein disulfide isomerase a redox-dependent molecular chaperone?". EMBO J. 21 (24): 6763–70. doi:10.1093/emboj/cdf685. PMC 139105. PMID 12485997.
• Clissold PM, Bicknell R (2003). "The thioredoxin-like fold: hidden domains in protein disulfide isomerases and other chaperone proteins". BioEssays. 25 (6): 603–11. doi:10.1002/bies.10287. PMID 12766950.
• Pirneskoski A, Klappa P, Lobell M, Williamson RA, Byrne L, Alanen HI, Salo KE, Kivirikko KI, Freedman RB, Ruddock LW (2004). "Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase". J. Biol. Chem. 279 (11): 10374–81. doi:10.1074/jbc.M312193200. PMID 14684740.
• Spooner RA, Watson PD, Marsden CJ, Smith DC, Moore KA, Cook JP, Lord JM, Roberts LM (2004). "Protein disulphide-isomerase reduces ricin to its A and B chains in the endoplasmic reticulum". Biochem. J. 383 (Pt 2): 285–93. doi:10.1042/BJ20040742. PMC 1134069. PMID 15225124.
• Li SJ, Hong XG, Shi YY, Li H, Wang CC (2006). "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. doi:10.1074/jbc.M508422200. PMID 16407203.
• Otsu M, Bertoli G, Fagioli C, Guerini-Rocco E, Nerini-Molteni S, Ruffato E, Sitia R (2006). "Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44". Antioxid. Redox Signal. 8 (3–4): 274–82. doi:10.1089/ars.2006.8.274. PMID 16677073.
• Park B, Lee S, Kim E, Cho K, Riddell SR, Cho S, Ahn K (2006). "Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing". Cell. 127 (2): 369–82. doi:10.1016/j.cell.2006.08.041. PMID 17055437. S2CID 2178004.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.