thioredoxin reductase 3 (thioredoxin reductase TR2, thioredoxin & glutathione reductase, TXNRD3, TGR, TRXR3)

Function: - displays thioredoxin reductase, glutaredoxin & glutathione reductase activities - catalyzes disulfide bond isomerization - promotes disulfide bond formation between GPX4 & various sperm proteins & may play a role in sperm maturation by promoting formation of sperm structural components thioredoxin + NADP⁺ thioredoxin disulfide + NADPH Cofactor: binds 1 FAD per subunit (putative) Structure: - homodimer (putative) - N-terminal glutaredoxin domain does not contain the C-X-X-C redox-active motif normally found in glutaredoxins but activity may be mediated through a single Cys - C-terminal Cys-sec motif of one subunit of the homodimer may transfer electrons from the thiol-disulfide center to the glutaredoxin domain of the other subunit (putative) - belongs to the class-1 pyridine nucleotide-disulfide oxidoreductase family - contains 1 glutaredoxin domain - thioredoxin reductase active site is a redox-active disulfide bond - selenocysteine residue is also essential for catalytic activity (putative) Compartment: - cytoplasm, nucleus, microsome (putative) - detected in cytoplasm & nucleus in late spermatids (putative)

Properties

SIZE: entity length = 754 aa MW = 82 kD COMPARTMENT: cytoplasm cell nucleus MOTIF: Glutaredoxin {167-267} cofactor-binding site [269-298] COFACTOR-BOUND: flavin adenine dinucleotide cysteine residue {C314} MODIFICATION: cysteine residue {C319} cysteine residue {C319} MODIFICATION: cysteine residue {C314} histidine residue {H727}

Database Correlations

OMIM 606235 UniProt Q86VQ6 PFAM correlations Kegg hsa:1141 ENZYME 1.8.1.9

References

UniProt :accession Q86VQ6