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HMDB Protein ID HMDBP13907
Secondary Accession Numbers None
Name Peroxiredoxin-6
  1. 1-Cys peroxiredoxin
  2. Acidic calcium-independent phospholipase A2
  3. Antioxidant protein 2
  4. Glutathione-dependent peroxiredoxin
  5. Lysophosphatidylcholine acyltransferase 5
  6. Non-selenium glutathione peroxidase
  7. Thiol-specific antioxidant protein
  8. 1-Cys PRX
  9. aiPLA2
  10. LPC acyltransferase 5
  11. LPCAT-5
  12. Lyso-PC acyltransferase 5
  13. NSGPx
Gene Name PRDX6
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (PubMed:15004285). Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (By similarity). 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:8999971, PubMed:15004285, PubMed:17652308). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (By similarity). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (By similarity). 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 (By similarity).
  • Glutathione metabolism
Reactions Not Available
GO Classification
Biological Process
cell redox homeostasis
response to oxidative stress
response to reactive oxygen species
cellular oxidant detoxification
bleb assembly
hydrogen peroxide catabolic process
glycerophospholipid catabolic process
positive regulation of mRNA splicing, via spliceosome
Cellular Component
perinuclear region of cytoplasm
Molecular Function
glutathione peroxidase activity
phospholipase A2 activity
peroxiredoxin activity
ubiquitin protein ligase binding
calcium-independent phospholipase A2 activity
1-acylglycerophosphocholine O-acyltransferase activity
peroxidase activity
identical protein binding
phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine)
phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine)
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 224
Molecular Weight 24818.325
Theoretical pI 5.938
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID O35244
UniProtKB/Swiss-Prot Entry Name PRDX6_RAT
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
General References
  1. Kim TS, Sundaresh CS, Feinstein SI, Dodia C, Skach WR, Jain MK, Nagase T, Seki N, Ishikawa K, Nomura N, Fisher AB: Identification of a human cDNA clone for lysosomal type Ca2+-independent phospholipase A2 and properties of the expressed protein. J Biol Chem. 1997 Jan 24;272(4):2542-50. [PubMed:8999971 ]
  2. Manevich Y, Feinstein SI, Fisher AB: Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST. Proc Natl Acad Sci U S A. 2004 Mar 16;101(11):3780-5. doi: 10.1073/pnas.0400181101. Epub 2004 Mar 2. [PubMed:15004285 ]
  3. Manevich Y, Reddy KS, Shuvaeva T, Feinstein SI, Fisher AB: Structure and phospholipase function of peroxiredoxin 6: identification of the catalytic triad and its role in phospholipid substrate binding. J Lipid Res. 2007 Oct;48(10):2306-18. doi: 10.1194/jlr.M700299-JLR200. Epub 2007 Jul 24. [PubMed:17652308 ]
  4. Sorokina EM, Feinstein SI, Milovanova TN, Fisher AB: Identification of the amino acid sequence that targets peroxiredoxin 6 to lysosome-like structures of lung epithelial cells. Am J Physiol Lung Cell Mol Physiol. 2009 Nov;297(5):L871-80. doi: 10.1152/ajplung.00052.2009. Epub 2009 Aug 21. [PubMed:19700648 ]
  5. Fisher AB, Dodia C, Sorokina EM, Li H, Zhou S, Raabe T, Feinstein SI: A novel lysophosphatidylcholine acyl transferase activity is expressed by peroxiredoxin 6. J Lipid Res. 2016 Apr;57(4):587-96. doi: 10.1194/jlr.M064758. Epub 2016 Feb 1. [PubMed:26830860 ]