Protein Function: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.
Background: Thioredoxin is a class of small redox proteins known to be present in all organisms. It is mapped to 9q31.3. Thioredoxins are proteins that act as antioxidants by facilitating the reduction of other proteins by cysteine thiol-disulfide exchange. They can also act as electron donors to peroxidases and ribonucleotide reductase. Thioredoxin is a 12-kD oxidoreductase enzyme containing a dithiol-disulfide active site. It plays a role in many important biological processes, including redox signaling. This gene also plays a central role in humans and is increasingly linked to medicine through their response to reactive oxygen species (ROS). VDUP1 is a key stress-responsive inhibitor of Thioredoxin activity in cardiomyocytes.
Synonyms: Thioredoxin,Trx,ATL-derived factor,ADF,Surface-associated sulphydryl protein,SASP,TXN,TRDX, TRX, TRX1,
Full Gene Name: ThioredoxinCellular Localisation: Nucleus. Cytoplasm. Secreted. Secreted by a leaderless secretory pathway. Predominantly in the cytoplasm in non irradiated cells. Radiation induces translocation of TRX from the cytoplasm to the nucleus.