Protein Domain : Protein disulfide-isomerase A4, TRX-like domain b IPR041866

Type	Domain
Description	This entry represents the first redox inactive TRX-like domain b found in protein disulfide-isomerase A4 (also known as ERp72). ERp72 exhibits both disulfide oxidase and reductase functions like PDI, by catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER and acting as isomerases to correct any non-native disulfide bonds [ , ]. It also displays chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins []. ERp72 contains three redox-active TRX (a) domains and two redox inactive TRX-like (b) domains. Its molecular structure is a'abb'a', compared to the abb'a' structure of PDI. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. Similar to PDI, the b domain of ERp72 is likely involved in binding to substrates.
Short Name	PDIA4_PDI_b