Protein Domain : Protein disulfide-isomerase A5, TRX (a) domain IPR046374

Type	Domain
Description	This entry represents the three redox active TRX (a) domains found in protein disulfide-isomerase A5 (PDIA5, also known as PDIR). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved in oxidative protein folding in the endoplasmic reticulum (ER) through its isomerase and chaperone activities. These activities are lower compared to PDI, probably due to PDIR acting only on a subset of proteins. PDIR is preferentially expressed in cells actively secreting proteins and its expression is induced by stress [ ]. Similar to PDI, the isomerase and chaperone activities of PDIR are independent; CXXC mutants lacking isomerase activity retain chaperone activity. The TRX-like b domain of PDIR is critical for its chaperone activity [].
Short Name	PDI_a_PDIR