Identification |
HMDB Protein ID
| HMDBP13907 |
Secondary Accession Numbers
| None |
Name
| Peroxiredoxin-6 |
Synonyms
|
- 1-Cys peroxiredoxin
- Acidic calcium-independent phospholipase A2
- Antioxidant protein 2
- Glutathione-dependent peroxiredoxin
- Lysophosphatidylcholine acyltransferase 5
- Non-selenium glutathione peroxidase
- Thiol-specific antioxidant protein
- 1-Cys PRX
- aiPLA2
- LPC acyltransferase 5
- LPCAT-5
- Lyso-PC acyltransferase 5
- 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). |
Pathways
|
|
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 |
cytosol |
cytoplasm |
mitochondrion |
perinuclear region of cytoplasm |
nucleus |
lysosome |
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
|
External Links |
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 |
References |
General References
| - 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 ]
- 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 ]
- 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 ]
- 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 ]
- 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 ]
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