Protein disulfide isomerases (EC 5.3.4.1), such as PDIP, are endoplasmic reticulum (ER) resident proteins that catalyze protein folding and thiol-disulfide interchange reactions
A synthesized peptide derived from human PDIA3, corresponding to a region within the internal amino acids.
PDIA4(Protein disulfide-isomerase A4) is also named as ERP70,ERP72 and belongs to the protein disulfide isomerase family. It catalyzes the rearrangement of -S-S- bonds in proteins. ERp72 is a soluble protein localized in the ER lumen and contains the COOH-terminal retention signal,KEEL. There are 6 cysteine residues in the amino acid sequences of mouse and human ERp72. All of the cysteine residues occur in the internal thioredoxin motif,CGHC. The full length protein has a signal peptide with 20 amino acid.
Participates in the apoptotic response to DNA damage. Isoforms containing the transactivation domain are pro-apoptotic, isoforms lacking the domain are anti-apoptotic and block the function of p53 and transactivating p73 isoforms.
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