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Identification
HMDB Protein ID HMDBP00281
Secondary Accession Numbers
  • 5513
Name Peroxiredoxin-6
Synonyms
  1. 1-Cys PRX
  2. 1-Cys peroxiredoxin
  3. 24 kDa protein
  4. Acidic calcium-independent phospholipase A2
  5. Antioxidant protein 2
  6. Liver 2D page spot 40
  7. NSGPx
  8. Non-selenium glutathione peroxidase
  9. Red blood cells page spot 12
  10. aiPLA2
Gene Name PRDX6
Protein Type Enzyme
Biological Properties
General Function Involved in antioxidant activity
Specific Function Involved in redox regulation of the cell. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. May play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.
Pathways
  • Phenylalanine metabolism
Reactions
R'-SH + ROOH → R'-S-S-R' + Water + ROH details
Glutathione + Hydrogen peroxide → Oxidized glutathione + Water details
Methanol + Hydrogen peroxide → Formaldehyde + Water details
L-Phenylalanine + Oxygen → 2-Phenylacetamide + Carbon dioxide details
Coniferyl alcohol → Guaiacyl lignin details
Sinapyl alcohol → Syringyl lignin details
4-Coumaryl alcohol → p-Hydroxyphenyl lignin details
5-Hydroxyconiferyl alcohol → 5-Hydroxy-guaiacyl lignin details
GO Classification
Biological Process
response to oxidative stress
phospholipid catabolic process
hydrogen peroxide catabolic process
Cellular Component
cytosol
lysosome
cytoplasmic membrane-bounded vesicle
Function
peroxiredoxin activity
catalytic activity
antioxidant activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
oxidoreductase activity
Molecular Function
glutathione peroxidase activity
phospholipase A2 activity
peroxiredoxin activity
antioxidant activity
Process
cellular process
cellular homeostasis
cell redox homeostasis
Cellular Location
  1. Cytoplasm
  2. Lysosome
  3. Cytoplasmic vesicle
Gene Properties
Chromosome Location 1
Locus 1q25.1
SNPs PRDX6
Gene Sequence
>675 bp
ATGCCCGGAGGTCTGCTTCTCGGGGACGTGGCTCCCAACTTTGAGGCCAATACCACCGTC
GGCCGCATCCGTTTCCACGACTTTCTGGGAGACTCATGGGGCATTCTCTTCTCCCACCCT
CGGGACTTTACCCCAGTGTGCACCACAGAGCTTGGCAGAGCTGCAAAGCTGGCACCAGAA
TTTGCCAAGAGGAATGTTAAGTTGATTGCCCTTTCAATAGACAGTGTTGAGGACCATCTT
GCCTGGAGCAAGGATATCAATGCTTACAATTGTGAAGAGCCCACAGAAAAGTTACCTTTT
CCCATCATCGATGATAGGAATCGGGAGCTTGCCATCCTGTTGGGCATGCTGGATCCAGCA
GAGAAGGATGAAAAGGGCATGCCTGTGACAGCTCGTGTGGTGTTTGTTTTTGGTCCTGAT
AAGAAGCTGAAGCTGTCTATCCTCTACCCAGCTACCACTGGCAGGAACTTTGATGAGATT
CTCAGGGTAGTCATCTCTCTCCAGCTGACAGCAGAAAAAAGGGTTGCCACCCCAGTTGAT
TGGAAGGATGGGGATAGTGTGATGGTCCTTCCAACCATCCCTGAAGAAGAAGCCAAAAAA
CTTTTCCCGAAAGGAGTCTTCACCAAAGAGCTCCCATCTGGCAAGAAATACCTCCGCTAC
ACACCCCAGCCTTAA
Protein Properties
Number of Residues 224
Molecular Weight 25034.715
Theoretical pI 6.378
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Peroxiredoxin-6
MPGGLLLGDVAPNFEANTTVGRIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPE
FAKRNVKLIALSIDSVEDHLAWSKDINAYNCEEPTEKLPFPIIDDRNRELAILLGMLDPA
EKDEKGMPVTARVVFVFGPDKKLKLSILYPATTGRNFDEILRVVISLQLTAEKRVATPVD
WKDGDSVMVLPTIPEEEAKKLFPKGVFTKELPSGKKYLRYTPQP
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P30041
UniProtKB/Swiss-Prot Entry Name PRDX6_HUMAN
PDB IDs
GenBank Gene ID D14662
GeneCard ID PRDX6
GenAtlas ID PRDX6
HGNC ID HGNC:16753
References
General References
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  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  8. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed:12665801 ]
  9. 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 ]
  10. Frank S, Munz B, Werner S: The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene. Oncogene. 1997 Feb 27;14(8):915-21. [PubMed:9050990 ]
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  13. Kang SW, Baines IC, Rhee SG: Characterization of a mammalian peroxiredoxin that contains one conserved cysteine. J Biol Chem. 1998 Mar 13;273(11):6303-11. [PubMed:9497358 ]
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  15. Wagner E, Luche S, Penna L, Chevallet M, Van Dorsselaer A, Leize-Wagner E, Rabilloud T: A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress. Biochem J. 2002 Sep 15;366(Pt 3):777-85. [PubMed:12059788 ]
  16. Gao L, Tse SW, Conrad C, Andreadis A: Saitohin, which is nested in the tau locus and confers allele-specific susceptibility to several neurodegenerative diseases, interacts with peroxiredoxin 6. J Biol Chem. 2005 Nov 25;280(47):39268-72. Epub 2005 Sep 26. [PubMed:16186110 ]
  17. Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE: Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution. Nat Struct Biol. 1998 May;5(5):400-6. [PubMed:9587003 ]