PDIA6

Protein disulfide isomerases (EC 5.3.4.1), such as PDIA6, are endoplasmic reticulum (ER) resident proteins that catalyze formation, reduction, and isomerization of disulfide bonds in proteins and are thought to play a role in folding of disulfide-bonded proteins (Hayano and Kikuchi, 1995 [PubMed 7590364]).[supplied by OMIM

protein disulfide isomerase family A, member 6

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).

Protein foldingManual Assertion Based On ExperimentTAS:ProtInc

Endoplasmic reticulum lumen
Cell membrane
Melanosome
Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:12643545).