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thioredoxin reductase 2, mitochondrial; selenoprotein Z; selZ; TR-beta; thioredoxin reductase TR3 (TXNRD2, KIAA1652, TRXR2)
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
Cofactor: FAD (putative)
Structure:
- homodimer
- belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family
Compartment: mitochondria
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]
General
flavoprotein
mitochondrial protein
oxidoreductase
selenoprotein
Properties
SIZE: entity length = 524 aa
MW = 57 kD
COMPARTMENT: mitochondria
MOTIF: cofactor-binding site [41-70]
COFACTOR-BOUND: flavin adenine dinucleotide
cysteine residue {C86}
MODIFICATION: cysteine residue {C91}
cysteine residue {C91}
MODIFICATION: cysteine residue {C86}
histidine residue {H497}
selenocysteine residue {C523}
Database Correlations
OMIM 606448
UniProt Q9NNW7
PFAM correlations
Entrez Gene 10587
Kegg hsa:10587
ENZYME 1.8.1.9
References
- UniProt :accession Q9NNW7
- 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: 10608886
- Gasdaska PY
Cloning, sequencing and functional expression of a novel human
thioredoxin reductase
FEBS Lett. 1999 Jan 8;442(1):105-11.
PMID: 9923614