Thioredoxin Reductase 1 (TXNRD1) Human Active Protein

This gene encodes a member of the family of pyridine nucleotide oxidoreductases. This protein reduces thioredoxins as well as other substrates, and plays a role in selenium metabolism and protection against oxidative stress. The functional enzyme is thought to be a homodimer which uses FAD as a cofactor. Each subunit contains a selenocysteine (Sec) residue which is required for catalytic activity. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenocysteine-containing genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Alternative splicing results in several transcript variants encoding the same or different isoforms. [provided by RefSeq, Jul 2008]

TRXR1: a cytoplasmic pyridine nucleotide oxidoreductases. This protein reduces thioredoxins as well as other substrates, and plays a role in selenium metabolism and protection against oxidative stress. The functional enzyme is thought to be a homodimer which uses FAD as a cofactor. Each subunit contains a selenocysteine residue which is required for the catalytic activity.

Protein type: Nucleotide Metabolism - pyrimidine; EC 1.8.1.9; Nuclear receptor co-regulator; Oxidoreductase

Chromosomal Location of Human Ortholog: 12q23-q24.1

Cellular Component: nucleoplasm; nucleolus; cytosol

Molecular Function: protein binding; thioredoxin-disulfide reductase activity; electron carrier activity; FAD binding; protein disulfide oxidoreductase activity

Biological Process: response to reactive oxygen species; nucleobase, nucleoside and nucleotide metabolic process; cell redox homeostasis; nucleobase, nucleoside and nucleotide interconversion; cellular lipid metabolic process; signal transduction