PDIA3
PDIA3 (protein disulfide isomerase family A member 3, also known as ERp57, ERp61, ERp60, GRP57, GRP58 and P58) is an endoplasmic reticulum enzyme that catalyses disulfide bond formation and acts as a folding chaperone. It is a core component of the MHC class I peptide loading complex. Browse Assay Genie's current range of PDIA3 research reagents below, or read on for the biology behind the target.
PDIA3 is a protein disulfide isomerase that catalyses the formation, isomerisation, and reduction or oxidation of disulfide bonds in client proteins, and it also functions as a protein folding chaperone. It interacts with the lectin chaperones calreticulin and calnexin to modulate the folding of newly synthesised glycoproteins. Complexes of these lectins with PDIA3 are thought to promote disulfide bond formation in glycoprotein substrates. PDIA3 also acts as a molecular chaperone that prevents the formation of protein aggregates.
In adaptive immunity, PDIA3 is a core component of the major histocompatibility complex class I (MHC I) peptide loading complex. There it serves as an essential folding chaperone for TAPBP (tapasin). Through TAPBP, it assists the dynamic assembly of the MHC I complex with high-affinity antigens in the endoplasmic reticulum, and so plays a crucial role in presenting antigens to cytotoxic T cells.
The human PDIA3 gene belongs to the protein disulfide isomerase family and encodes a protein found in the endoplasmic reticulum, with a further annotated location in the melanosome. Its many aliases reflect its history: it was once thought to be a phospholipase, hence the alias PI-PLC, but has since been shown to have protein disulfide isomerase activity. Earlier names include glucose regulated protein, 58kDa (GRP58) and protein disulfide isomerase-associated 3. Orthologous Pdia3 genes are annotated in mouse and rat, which makes comparative work in rodent models straightforward.
PDIA3 works with calreticulin and calnexin to fold newly synthesised glycoproteins, making it a key subject in studies of ER chaperone systems.
As a folding chaperone for TAPBP in the MHC I peptide loading complex, PDIA3 supports antigen presentation to cytotoxic T cells.
PDIA3 catalyses formation, isomerisation, and reduction or oxidation of disulfide bonds, so it is used to study oxidative protein folding.
PDIA3 acts as a molecular chaperone that prevents protein aggregates from forming, which is relevant to work on protein misfolding.
PDIA3 is an endoplasmic reticulum protein disulfide isomerase. It catalyses formation, isomerisation, and reduction or oxidation of disulfide bonds, and acts as a chaperone for glycoprotein folding with calreticulin and calnexin. It is also a core component of the MHC class I peptide loading complex, where it supports TAPBP.
PDIA3 is also called ERp57, ERp61, ERp60, GRP57, GRP58, P58 and PI-PLC. The PI-PLC name dates from when the protein was thought to be a phospholipase, later shown to be incorrect. Earlier names include glucose regulated protein, 58kDa, and protein disulfide isomerase-associated 3.
Yes. Orthologous Pdia3 genes are annotated in both mouse and rat, so findings can be compared across human and rodent systems. Researchers should check the datasheet of any product for its validated reactivity before choosing a reagent for a given species.
Other members of the protein disulfide isomerase family that act in endoplasmic reticulum protein folding.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P30101; product specifications from Assay Genie datasheets.