Description: Homo sapiens peroxiredoxin 2 (PRDX2), nuclear gene encoding mitochondrial protein, mRNA. RefSeq Summary (NM_005809): This gene encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein plays an antioxidant protective role in cells, and it may contribute to the antiviral activity of CD8(+) T-cells. The crystal structure of this protein has been resolved to 2.7 angstroms. This protein prevents hemolytic anemia from oxidative stress by stabilizing hemoglobin, thus making this gene a therapeutic target for patients with hemolytic anemia. This protein may have a proliferative effect and play a role in cancer development or progression. Related pseudogenes have been identified on chromosomes 5, 6, 10 and 13. [provided by RefSeq, Mar 2013]. Transcript (Including UTRs) Position: hg19 chr19:12,907,634-12,912,724 Size: 5,091 Total Exon Count: 6 Strand: - Coding Region Position: hg19 chr19:12,907,895-12,912,075 Size: 4,181 Coding Exon Count: 5
ID:PRDX2_HUMAN DESCRIPTION: RecName: Full=Peroxiredoxin-2; EC=1.11.1.15; AltName: Full=Natural killer cell-enhancing factor B; Short=NKEF-B; AltName: Full=PRP; AltName: Full=Thiol-specific antioxidant protein; Short=TSA; AltName: Full=Thioredoxin peroxidase 1; AltName: Full=Thioredoxin-dependent peroxide reductase 1; FUNCTION: Involved 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). CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. SUBUNIT: Homodimer; 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. SUBCELLULAR LOCATION: Cytoplasm. MISCELLANEOUS: The 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. MISCELLANEOUS: Inactivated 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. SIMILARITY: Belongs to the AhpC/TSA family. SIMILARITY: Contains 1 thioredoxin domain. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/prdx2/";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P32119
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0006979 response to oxidative stress GO:0019430 removal of superoxide radicals GO:0034599 cellular response to oxidative stress GO:0042744 hydrogen peroxide catabolic process GO:0042981 regulation of apoptotic process GO:0043066 negative regulation of apoptotic process GO:0045454 cell redox homeostasis GO:0055114 oxidation-reduction process
US Server
