ID:PDIA6_HUMAN DESCRIPTION: RecName: Full=Protein disulfide-isomerase A6; EC=5.3.4.1; AltName: Full=Endoplasmic reticulum protein 5; Short=ER protein 5; Short=ERp5; AltName: Full=Protein disulfide isomerase P5; AltName: Full=Thioredoxin domain-containing protein 7; Flags: Precursor; FUNCTION: May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin. CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in proteins. SUBUNIT: Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Interacts with MICA on the surface of tumor cells, leading to MICA disulfide bond reduction which is required for its release from tumor cells. Interacts with ITGB3 following platelet stimulation. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity). Cell membrane. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. TISSUE SPECIFICITY: Expressed in platelets (at protein level). SIMILARITY: Belongs to the protein disulfide isomerase family. SIMILARITY: Contains 2 thioredoxin domains.
Protein Domain and Structure Information
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Other Names for This Gene
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Methods, Credits, and Use Restrictions
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