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MGP003099

UniProt Annotations

Entry Information
Gene Nameperoxiredoxin 2
Protein EntryPRDX2_HUMAN
UniProt IDP32119
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=P32119-1; Sequence=Displayed; Name=2; IsoId=P32119-2; Sequence=VSP_042924; Note=No experimental confirmation available. Due to intron retention. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Catalytic Activity2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. {ECO:0000269|PubMed:8554614}.
FunctionInvolved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons 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).
MiscellaneousInactivated upon oxidative stress by overoxidation of Cys-51 to Cys-SO(2)H and Cys-SO(3)H. Cys-SO(2)H is retroreduced to Cys-SOH after removal of H(2)O(2), while Cys-SO(3)H may be irreversibly oxidized.
MiscellaneousThe active site is the redox-active Cys-51 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-172-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.
SimilarityBelongs to the AhpC/TSA family. {ECO:0000305}.
SimilarityContains 1 thioredoxin domain. {ECO:0000255|PROSITE- ProRule:PRU00691}.
Subcellular LocationCytoplasm.
SubunitHomodimer; disulfide-linked, upon oxidation. May be found as a toroid-shaped decamer composed of 5 dimers, depending on pH and calcium concentration. Interacts with TIPIN. {ECO:0000269|PubMed:17141802}.
Web ResourceName=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/prdx2/";
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