PDIA3 Antibody – Mouse Monoclonal

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. [provided by RefSeq, Jul 2008]

GRP58: a protein disulfide isomerase found in the endoplasmic reticulum lumen. Catalyzes the rearrangement of both intrachain and interchain disulfide bonds in proteins to form the native structures. An essential component of the peptide-loading complex of the major histocompatibility complex class I pathway.

Protein type: EC 5.3.4.1; Endoplasmic reticulum; Apoptosis; Isomerase; Protease; Chaperone; Phospholipase

Chromosomal Location of Human Ortholog: 15q15

Cellular Component: cell surface; smooth endoplasmic reticulum; focal adhesion; endoplasmic reticulum; endoplasmic reticulum lumen; melanosome; nucleus

Molecular Function: disulfide oxidoreductase activity; protein binding; cysteine-type endopeptidase activity; protein disulfide isomerase activity; phospholipase C activity

Biological Process: antigen processing and presentation of peptide antigen via MHC class I; cellular protein metabolic process; protein folding; cell redox homeostasis; protein import into nucleus; antigen processing and presentation of exogenous peptide antigen via MHC class I; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; protein amino acid N-linked glycosylation via asparagine; post-translational protein modification; proteolysis; signal transduction; protein retention in ER