PDIA3

This gene encodes a protein of the endoplasmic reticulum that interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. The protein was once thought to be a phospholipase; however, it has been demonstrated that the protein actually has protein disulfide isomerase activity. It is thought that complexes of lectins and this protein mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates. This protein also functions as a molecular chaperone that prevents the formation of protein aggregates. [provided by RefSeq, Dec 2016]

Protein Disulfide Isomerase Family A Member 3

Disulfide isomerase which catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds (PubMed:7487104, PubMed:27897272).
Associates with calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells (PubMed:27897272).
Association with calcitriol does not affect its enzymatic activity (PubMed:27897272).

Cellular response to interleukin-7IEA:Ensembl
Peptide antigen assembly with MHC class I protein complexManual Assertion Based On ExperimentIDA:ComplexPortal
Positive regulation of extrinsic apoptotic signaling pathwayIEA:Ensembl
Protein foldingManual Assertion Based On ExperimentIBA:GO_Central
Protein folding in endoplasmic reticulumManual Assertion Based On ExperimentTAS:ParkinsonsUK-UCL
Response to endoplasmic reticulum stressManual Assertion Based On ExperimentIBA:GO_Central

Endoplasmic reticulum
Endoplasmic reticulum lumen
Melanosome
Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:12643545).