Thioredoxin (mTXN) Mouse Active Protein

TXN: 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. Homodimer; disulfide-linked. Interacts with TXNIP through the redox-active site. Interacts with MAP3K5 and CASP3. In case of infection, interacts with S.typhimurium protein slrP. Interacts with APEX1; the interaction stimulates the FOS/JUN AP-1 DNA- binding activity in a redox-dependent manner. Up-regulated by ionizing radiation. Belongs to the thioredoxin family.

Protein type: Nuclear receptor co-regulator

Cellular Component: cell soma; mitochondrion; axon; cytoplasm; dendrite; extracellular region; nucleus; cytosol

Molecular Function: protein binding; enzyme binding; protein disulfide oxidoreductase activity; peptide disulfide oxidoreductase activity; oxidoreductase activity, acting on sulfur group of donors, disulfide as acceptor

Biological Process: sulfate assimilation; response to radiation; negative regulation of protein export from nucleus; transcription, DNA-dependent; protein folding; regulation of transcription, DNA-dependent; cell redox homeostasis; transport; regulation of protein import into nucleus, translocation; negative regulation of transcription from RNA polymerase II promoter; positive regulation of peptidyl-serine phosphorylation; glycerol ether metabolic process; positive regulation of DNA binding