PDIA2

PDIA2 is a member of the disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyze protein folding and thiol-disulfide interchange reactions. The encoded protein has an N-terminal ER-signal sequence, two catalytically active thioredoxin (TRX) domains, two TRX-like domains and a C-terminal ER-retention sequence. The protein plays a role in the folding of nascent proteins in the endoplasmic reticulum by forming disulfide bonds through its thiol isomerase, oxidase, and reductase activity. The encoded protein also possesses estradiol-binding activity and can modulate intracellular estradiol levels.

Protein Disulfide Isomerase Family A Member 2

Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins.

Protein foldingManual Assertion Based On ExperimentIBA:GO_Central
Protein folding in endoplasmic reticulumManual Assertion Based On ExperimentTAS:ParkinsonsUK-UCL
Protein retention in ER lumenManual Assertion Based On ExperimentTAS:ProtInc
Response to endoplasmic reticulum stressManual Assertion Based On ExperimentIBA:GO_Central

Endoplasmic reticulum lumen

The disulfide-linked homodimer exhibits an enhanced chaperone activity.
Glycosylated.