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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.
Protein class

Enzymes, Metabolic proteins, Plasma proteins

Predicted location

Intracellular

Single cell type specificity

Cell type enhanced (Syncytiotrophoblasts)

Immune cell specificity

Low immune cell specificity

Cell line specificity

Low cell line specificity

Interaction

Subunit of the TAP complex, also known as the peptide loading complex (PLC). Can form disulfide-linked heterodimers with TAPBP. Interacts with ERP27 and CANX. Interacts with SERPINA2 and with the S and Z variants of SERPINA1. Interacts with ATP2A2.

Molecular function

Isomerase

More Types Infomation

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For Research Use Only. Not For Clinical Use.

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