PRDX6

The protein encoded by this gene is a member of the thiol-specific antioxidant protein family. This protein is a bifunctional enzyme with two distinct active sites. It is involved in redox regulation of the cell; it can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. It may play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. [provided by RefSeq]

peroxiredoxin 6

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (PubMed:9497358, PubMed:10893423).
Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides (PubMed:10893423).
Also has phospholipase activity, can therefore either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (PubMed:10893423, PubMed:26830860).
These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (PubMed:10893423).
Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (PubMed:10893423).
Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (PubMed:26830860).
Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (PubMed:26830860).

Cell redox homeostasisManual Assertion Based On ExperimentIBA:GO_Central
Cellular oxidant detoxificationManual Assertion Based On ExperimentIMP:CAFA
Glycerophospholipid catabolic processManual Assertion Based On ExperimentIMP:CAFA
Positive regulation of mRNA splicing, via spliceosomeManual Assertion Based On ExperimentIGI:UniProtKB
Response to oxidative stressManual Assertion Based On ExperimentIMP:CAFA

Cytoplasm
Lysosome
Also found in lung secretory organelles (lamellar bodies).

Irreversibly inactivated by overoxidation of Cys-47 to sulfinic acid (Cys-SO2H) and sulfonic acid (Cys-SO3H) forms upon oxidative stress.
Phosphorylation at Thr-177 by MAP kinases increases the phospholipase activity of the enzyme (By similarity).
The phosphorylated form exhibits a greater lysophosphatidylcholine acyltransferase activity compared to the non-phosphorylated form (PubMed:26830860).