Protein disulfide isomerase that catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds in client proteins and functions as a protein folding chaperone (PubMed:11825568, PubMed:16193070, PubMed:27897272, PubMed:36104323, PubMed:7487104). Core component of the major histocompatibility complex class I (MHC I) peptide loading complex where it functions as an essential folding chaperone for TAPBP. Through TAPBP, assists the dynamic assembly of the MHC I complex with high affinity antigens in the endoplasmic reticulum.
Therefore, plays a crucial role in the presentation of antigens to cytotoxic T cells in adaptive immunity (PubMed:35948544, PubMed:36104323)
Part of the major histocompatibility complex class I (MHC I) peptide loading complex composed of TAP1, TAP2, B2M, MHC heavy chain, TAPBP, PDIA3, and CALR (PubMed:19119025, PubMed:35948544, PubMed:36104323). Interacts with ERP27 and CANX (PubMed:16905107, PubMed:16940051). Interacts with SERPINA2 and with the S and Z variants of SERPINA1 (PubMed:23826168).
Interacts with ATP2A2 (By similarity)
Detected in the flagellum and head region of spermatozoa (at protein level) (PubMed:20400973). Expressed in liver, stomach and colon (at protein level). Expressed in gastric parietal cells and chief cells (at protein level) (PubMed:24188822)
No mutation information available.
Genes with an experimentally identified or computationally predicted synthetic-lethal relationship to PDIA3, aggregated across our SSL data sources. Click any partner node to view that gene’s page.
Nodes and edges are coloured by the SSL data source. Partners appearing in more than one source are shown in grey.
No clinical trials information available.