PRDX1

This gene encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein may play an antioxidant protective role in cells, and may contribute to the antiviral activity of CD8(+) T-cells. This protein may have a proliferative effect and play a role in cancer development or progression. Three transcript variants encoding the same protein have been identified for this gene. [provided by RefSeq]

PRDX1

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2 (PubMed:9497357).
Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).

Cell population proliferationManual Assertion Based On ExperimentTAS:ProtInc
Cell redox homeostasisManual Assertion Based On ExperimentIBA:GO_Central
Erythrocyte homeostasisIEA:Ensembl
Hydrogen peroxide catabolic processManual Assertion Based On ExperimentIDA:BHF-UCL
Leukocyte activationManual Assertion Based On ExperimentIBA:GO_Central
Natural killer cell activationManual Assertion Based On ExperimentIDA:UniProtKB
Natural killer cell mediated cytotoxicityIEA:Ensembl
Regulation of NIK/NF-kappaB signalingIEA:Ensembl
Regulation of stress-activated MAPK cascadeIEA:Ensembl
Removal of superoxide radicalsManual Assertion Based On ExperimentIBA:GO_Central
Retina homeostasisManual Assertion Based On ExperimentHEP:UniProtKB
Skeletal system developmentManual Assertion Based On ExperimentTAS:ProtInc

Cytoplasm
Melanosome
Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity.
The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner.