|FUNCTION: Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2).
* SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By similarity). May form heterodimers with AOP2.
* SUBCELLULAR LOCATION: Cytoplasmic.
* INDUCTION: Constitutively expressed in most human cells; is induced to higher levels upon serum stimulation in untransformed and transformed cells.
* MISCELLANEOUS: The active site is the redox-active Cys-52 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin.
* MISCELLANEOUS: Irreversibly inactived by overoxidation of Cys-52 (to Cys-SO2H and Cys-SO3H) upon oxidative stress.
* SIMILARITY: BELONGS TO THE AHPC/TSA FAMILY.
* DATABASE: NAME=Atlas Genet. Cytogenet. Oncol. Haematol.; WWW="http://www.infobiogen.fr/services/chromcancer/Genes/PAGID266.html".
Last Update 13-Mar-03