Protein Disulfide-Isomerase A3 (PDIA3) Antibody – Rabbit Polyclonal

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

Chromosomal Location of Human Ortholog: 15q15

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

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

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