encodes a cytosolic thioredoxin that reduces disulfide bridges of target proteins by the reversible formation of a disulfide bridge between two neighboring Cys residues present in the active site. Thioredoxins have been found to regulate a variety of biological reactions in prokaryotic and eukaryotic cells. The mRNA is cell-to-cell mobile.
Thiol-disulfide oxidoreductase that possesses disulfide reductase and insulin disulfide bonds reducing activities. Heat shock causes oligomerization and formation of high molecular weight (HMW) complexes with concomitant functional switching from a disulfide reductase to chaperone.