This gene encodes a member of the thioredoxin superfamily. Members of this family are characterized by a conserved active motif called the thioredoxin fold that catalyzes disulfide bond formation and isomerization. This protein localizes to the endoplasmic reticulum and has a single atypical active motif. The encoded protein is mainly involved in catalyzing native disulfide bond formation and displays activity similar to protein-disulfide isomerases. This protein may play a role in defense against endoplasmic reticulum stress. Alternate splicing results in both coding and non-coding variants. [provided by RefSeq, Mar 2012],
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Function:
Catalytic activity:2 glutathione + protein-disulfide = glutathione disulfide + protein-dithiol.,cofactor:FAD.,Function:Possesses significant protein thiol-disulfide oxidase activity.,Function:Probable oxidoreductase that acts as a caspase-independent mitochondrial effector of apoptotic cell death. Extramitochondrial AIF induces nuclear chromatin condensation and large scale DNA fragmentation (in vitro). Binds to DNA in a sequence-independent manner.,similarity:Belongs to the FAD-dependent oxidoreductase family.,similarity:Contains 1 thioredoxin domain.,subcellular location:Translocated to the nucleus upon induction of apoptosis.,subunit:Interacts with XIAP.,tissue specificity:Widely expressed.,