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; OMA:PDIA2 - orthologs
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16p13.3 Start 283,164 bp[1] End 287,215 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17|17 A3.3 Start 26,414,973 bp[2] End 26,418,061 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas right hemisphere of cerebellum right frontal lobe C1 segment anterior cingulate cortex paraflocculus of cerebellum Brodmann area 9 testicle body of stomach Amygdala Top expressed in epithelium of stomach islet of Langerhans duodenum embryo embryo morula human fetus sexually immature organism bone marrow blastocyst More reference expression data BioGPS n/a
Gene ontology Molecular function disulfide oxidoreductase activity steroid binding protein binding peptidyl-proline 4-dioxygenase activity isomerase activity lipid binding protein disulfide isomerase 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 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: 26.41 – 26.42 Mb PubMed search [3] [4]
Wikidata
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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].