thioredoxin reductase 2, mitochondrial; selenoprotein Z; selZ; TR-beta; thioredoxin reductase TR3 (TXNRD2, KIAA1652, TRXR2)
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Function
- maintains thioredoxin in a reduced state
- implicated in the defenses against oxidative stress
- may play a role in redox-regulated cell signaling
- the active site is a redox-active disulfide bond
- the selenocysteine residue is essential for enzymatic activity
thioredoxin + NADP+ = thioredoxin disulfide + NADPH
Structure
- homodimer
- belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family
Compartment
Alternative splicing
named isoforms=4
Expression
- highly expressed in the prostate, ovary, liver, testis, uterus, colon & small intestine
- moderately expressed in brain, skeletal muscle, heart & spleen
- low expression in placenta, pancreas, thymus & peripheral blood leukocytes
- high levels in kidney[2]; low levels in kidney[3]
More general terms
References
- ↑ UniProt http://www.uniprot.org/uniprot/Q9NNW7.html
- ↑ 2.0 2.1 Lescure A et al Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif. J Biol Chem. 1999 Dec 31;274(53):38147-54. PMID: https://www.ncbi.nlm.nih.gov/pubmed/10608886
- ↑ 3.0 3.1 Gasdaska PY Cloning, sequencing and functional expression of a novel human thioredoxin reductase FEBS Lett. 1999 Jan 8;442(1):105-11. PMID: https://www.ncbi.nlm.nih.gov/pubmed/9923614