Description
Product Characteristics:
This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9, the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307).
Subcellular location: Cytoplasm
Synonyms: Protein Disulfide lsomerase, Cellular thyroid hormone-binding protein, PDI, Prolyl 4-hydroxylase subunit beta, p55, P4HB, ERBA2L, P4HB, ERBA2L, PDIA1, PO4DB, PDIA1_HUMAN.
Target Information: 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 (Desilva et al., 1996 [PubMed 8561901]).[supplied by OMIM, Mar 2008]