FEATURES

FAMILY

DESCRIPTION

Also known as PDIA6_HUMAN, PDIA6, ERP5, P5, TXNDC7. May function as a chaperone that inhibits aggregation of misfolded proteins (PubMed:12204115). Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling (PubMed:24508390). May also regulate the UPR via the EIF2AK3 UPR sensor (PubMed:24508390). Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin (PubMed:15466936). Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX (PubMed:12475965). Interacts with MICA on the surface of tumor cells, leading to MICA disulfide bond reduction which is required for its release from tumor cells (PubMed:17495932). Interacts with ITGB3 following platelet stimulation (PubMed:15466936). Interacts with ERN1; the interaction is direct (PubMed:24508390). Interacts with EIF2AK3 (PubMed:24508390).

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EXTERNAL LINKS

PDIA6

Protein disulfide-isomerase A6

ligandability Mutations

PDIA6

Molecular Synopsis