TXNRD1 Antibody – Rabbit Polyclonal

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]

Function: Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid. Ref.3 Ref.12 Ref.14 Ref.17

Catalytic activity: Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactor: Binds 1 FAD per subunit.

Subunit structure: Homodimer. Isoform 4 interacts with ESR1 and ESR2. Interacts with HERC5. Ref.12 Ref.14 Ref.16

Subcellular location: Cytoplasm

By similarity Ref.14. Isoform 4: Cytoplasm Ref.14. Nucleus Ref.14. Isoform 5: Cytoplasm Ref.14.

Tissue specificity: Isoform 1 is expressed predominantly in Leydig cells (at protein level). Also expressed in ovary, spleen, heart, liver, kidney and pancreas and in a number of cancer cell lines. Isoform 4 is widely expressed with highest levels in kidney, testis, uterus, ovary, prostate, placenta and fetal liver. Ref.2 Ref.14 Ref.17

Induction: Isoform 5 is induced by a combination of interferon-beta and retinoic acid (at protein level). Isoform 1 is induced by estradiol or testosterone in HeLa cells. Ref.3 Ref.17

Domain: The N-terminal glutaredoxin domain found in isoform 1 does not contain the C-P-Y-C redox-active motif normally found in glutaredoxins and has been found to be inactive in classical glutaredoxin assays. Ref.13

Post-translational modification: The N-terminus of isoform 5 is blocked.ISGylated

Probable. Ref.16

Miscellaneous: The thioredoxin reductase active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity.

Sequence similarities: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.Contains 1 glutaredoxin domain.

Sequence caution: The sequence AAB35418.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.The sequence AAC69621.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.The sequence AAF15900.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.The sequence AAV38446.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.The sequence AAZ67916.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.The sequence BAA13674.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.The sequence CAA04503.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.The sequence CAA62629.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.The sequence CAG38744.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.