protein disulfide-isomerase A6; endoplasmic reticulum protein 5; ER protein 5; ERp5; protein disulfide isomerase P5; thioredoxin domain-containing protein 7 (PDIA6, ERP5, P5, TXNDC7)
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Function
- may function as a chaperone that inhibits aggregation of misfolded proteins
- role in platelet aggregation & activation by agonists such as convulxin, collagen & thrombin
- catalyzes the rearrangement of -S-S- bonds in proteins
- part a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 & very small amounts of ERP29, & perhaps 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
Structure
- belongs to the protein disulfide isomerase family
- contains 2 thioredoxin domains
Compartment
- endoplasmic reticulum lumen (putative)
- cell membrane, melanosome
- identified by mass spectrometry in melanosome fractions from stage 1 to stage 4
Alternative splicing
named isoforms=2
Expression
expressed in platelets (at protein level)