PDIA5

PDIA5 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, three catalytically active thioredoxin (TRX) domains, a TRX-like domain, and a C-terminal ER-retention sequence. The N-terminal TRX-like domain is the primary binding site for the major ER chaperone calreticulin and possibly other proteins and substrates as well. Alternative splicing results in multiple protein-and non-protein-coding transcript variants.

protein disulfide isomerase family A, member 5

Electron transport chainManual Assertion Based On ExperimentTAS:UniProtKB
Protein foldingManual Assertion Based On ExperimentIDA:FlyBase

Endoplasmic reticulum lumen