IFI30

Lysosomal thiol reductase that catalyzes protein disulfide bonds reduction. Plays an important role in antigen processing and presentation, of namely both major histocompatibility complex (MHC) class I- and class II-restricted antigen by reducing the disulfide bonds of endocytosed proteins and facilitating their unfolding and optimal degradation. Shares with thioredoxin a reduction mechanism in which the N-terminal cysteine thiol group in the CXXC active site motif initiates a nucleophilic attack on the substrate disulfide bond,resulting in the formation of a mixed disulfide-linked enzyme-substrate intermediate (Probable). Subsequent intramolecular attack by the second cysteine thiol group enables the release of the reduced substrate and oxidized enzyme (Probable). Lysosomal cysteine is a physiological reducing agent that is capable of reducing IFI30, so that it can catalyzes the next reaction. Dithiothreitol, cysteine, and cysteinyl glycine, but not glutathione, are capable of regenerating active precursor and mature IFI30 in vitro..

Function from UniProtKB (P13284), read 2026-09-23. CC BY 4.0.