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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.
Gene Name: | prolyl 4-hydroxylase, beta polypeptide |
Synonyms: | P4HB, ERBA2L, DSI, GIT, p4HB, p4Hbeta, PDIA1, PHDB, PO4DB, PROHB, Protocollagen hydroxylase, Protein disulfide-isomerase, PO4HB, PDI |
Target Sequences: | NM_000918 NP_000909.2 P07237 |
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