TXNRD1
Domain
Isoform 1
The N-terminal glutaredoxin domain 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.
Function
Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form (PubMed:8577704). Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catalysis (Probable). Also has reductase activity on hydrogen peroxide (H2O2) (PubMed:10849437).
Isoform 1
Induces actin and tubulin polymerization, leading to formation of cell membrane protrusions.
Isoform 4
Enhances the transcriptional activity of estrogen receptors ESR1 and ESR2.
Isoform 5
Enhances the transcriptional activity of the estrogen receptor ESR2 only (PubMed:15199063). Mediates cell death induced by a combination of interferon-beta and retinoic acid (PubMed:9774665).
Post-translational modifications
Isoform 5
The N-terminus is blocked.
ISGylated.
Sequence Similarities
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Tissue Specificity
Isoform 1
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
Widely expressed with highest levels in kidney, testis, uterus, ovary, prostate, placenta and fetal liver.
Cellular localization
- Isoform 1
- Cytoplasm
- Isoform 4
- Cytoplasm
- Nucleus
- Isoform 5
- Cytoplasm
Alternative names
GRIM12, KDRF, TXNRD1, TR, Gene associated with retinoic and interferon-induced mortality 12 protein, KM-102-derived reductase-like factor, Peroxidase TXNRD1, Thioredoxin reductase TR1, GRIM-12, Gene associated with retinoic and IFN-induced mortality 12 protein