Peroxiredoxin-5, mitochondrial

Details

Name
Peroxiredoxin-5, mitochondrial
Synonyms
  • 1.11.1.15
  • ACR1
  • Alu corepressor 1
  • Antioxidant enzyme B166
  • AOEB166
  • Liver tissue 2D-page spot 71B
  • Peroxiredoxin V
  • Peroxisomal antioxidant enzyme
  • PLP
  • Prx-V
  • Thioredoxin peroxidase PMP20
  • Thioredoxin reductase
  • TPx type VI
Gene Name
PRDX5
Organism
Humans
Amino acid sequence
>lcl|BSEQ0037099|Peroxiredoxin-5, mitochondrial
MGLAGVCALRRSAGYILVGGAGGQSAAAAARRYSEGEWASGGVRSFSRAAAAMAPIKVGD
AIPAVEVFEGEPGNKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAEALKAKGV
QVVACLSVNDAFVTGEWGRAHKAEGKVRLLADPTGAFGKETDLLLDDSLVSIFGNRRLKR
FSMVVQDGIVKALNVEPDGTGLTCSLAPNIISQL
Number of residues
214
Molecular Weight
22086.245
Theoretical pI
8.77
GO Classification
Functions
antioxidant activity / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / peroxidase activity / peroxiredoxin activity / peroxynitrite reductase activity / protein dimerization activity / receptor binding / RNA polymerase III regulatory region DNA binding
Processes
apoptotic process / cellular response to reactive oxygen species / gene expression / hydrogen peroxide catabolic process / inflammatory response / NADPH oxidation / negative regulation of apoptotic process / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / negative regulation of oxidoreductase activity / negative regulation of transcription from RNA polymerase III promoter / positive regulation of collagen biosynthetic process / reactive nitrogen species metabolic process / regulation of apoptosis involved in tissue homeostasis / response to oxidative stress / response to reactive oxygen species / transcription initiation from RNA polymerase II promoter
Components
cytoplasm / cytoplasmic vesicle / cytosol / extracellular exosome / extracellular space / intracellular membrane-bounded organelle / mitochondrial matrix / mitochondrion / nucleus / perinuclear region of cytoplasm / peroxisomal matrix / peroxisome
General Function
Rna polymerase iii regulatory region dna binding
Specific Function
Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Mitochondrion
Gene sequence
>lcl|BSEQ0016248|Peroxiredoxin-5, mitochondrial (PRDX5)
ATGGGACTAGCTGGCGTGTGCGCCCTGAGACGCTCAGCGGGCTATATACTCGTCGGTGGG
GCCGGCGGTCAGTCTGCGGCAGCGGCAGCAAGACGGTGCAGTGAAGGAGAGTGGGCGTCT
GGCGGGGTCCGCAGTTTCAGCAGAGCCGCTGCAGCCATGGCCCCAATCAAGGTGGGAGAT
GCCATCCCAGCAGTGGAGGTGTTTGAAGGGGAGCCAGGGAACAAGGTGAACCTGGCAGAG
CTGTTCAAGGGCAAGAAGGGTGTGCTGTTTGGAGTTCCTGGGGCCTTCACCCCTGGATGT
TCCAAGACACACCTGCCAGGGTTTGTGGAGCAGGCTGAGGCTCTGAAGGCCAAGGGAGTC
CAGGTGGTGGCCTGTCTGAGTGTTAATGATGCCTTTGTGACTGGCGAGTGGGGCCGAGCC
CACAAGGCGGAAGGCAAGGTTCGGCTCCTGGCTGATCCCACTGGGGCCTTTGGGAAGGAG
ACAGACTTATTACTAGATGATTCGCTGGTGTCCATCTTTGGGAATCGACGTCTCAAGAGG
TTCTCCATGGTGGTACAGGATGGCATAGTGAAGGCCCTGAATGTGGAACCAGATGGCACA
GGCCTCACCTGCAGCCTGGCACCCAATATCATCTCACAGCTCTGA
Chromosome Location
11
Locus
11q13
External Identifiers
ResourceLink
UniProtKB IDP30044
UniProtKB Entry NamePRDX5_HUMAN
GenBank Protein ID6523289
GenBank Gene IDAJ249483
GenAtlas IDPRDX5
HGNC IDHGNC:9355
General References
  1. Kropotov A, Sedova V, Ivanov V, Sazeeva N, Tomilin A, Krutilina R, Oei SL, Griesenbeck J, Buchlow G, Tomilin N: A novel human DNA-binding protein with sequence similarity to a subfamily of redox proteins which is able to repress RNA-polymerase-III-driven transcription of the Alu-family retroposons in vitro. Eur J Biochem. 1999 Mar;260(2):336-46. [Article]
  2. Yamashita H, Avraham S, Jiang S, London R, Van Veldhoven PP, Subramani S, Rogers RA, Avraham H: Characterization of human and murine PMP20 peroxisomal proteins that exhibit antioxidant activity in vitro. J Biol Chem. 1999 Oct 15;274(42):29897-904. [Article]
  3. Knoops B, Clippe A, Bogard C, Arsalane K, Wattiez R, Hermans C, Duconseille E, Falmagne P, Bernard A: Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family. J Biol Chem. 1999 Oct 22;274(43):30451-8. [Article]
  4. Zhou Y, Kok KH, Chun AC, Wong CM, Wu HW, Lin MC, Fung PC, Kung H, Jin DY: Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis. Biochem Biophys Res Commun. 2000 Feb 24;268(3):921-7. [Article]
  5. Seo MS, Kang SW, Kim K, Baines IC, Lee TH, Rhee SG: Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate. J Biol Chem. 2000 Jul 7;275(27):20346-54. [Article]
  6. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [Article]
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  9. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [Article]
  10. 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. [Article]
  11. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  12. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  13. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]
  14. Declercq JP, Evrard C, Clippe A, Stricht DV, Bernard A, Knoops B: Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution. J Mol Biol. 2001 Aug 24;311(4):751-9. [Article]
  15. Smeets A, Marchand C, Linard D, Knoops B, Declercq JP: The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins. Arch Biochem Biophys. 2008 Sep 1;477(1):98-104. doi: 10.1016/j.abb.2008.04.036. Epub 2008 May 4. [Article]
  16. Hall A, Parsonage D, Poole LB, Karplus PA: Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization. J Mol Biol. 2010 Sep 10;402(1):194-209. doi: 10.1016/j.jmb.2010.07.022. Epub 2010 Jul 17. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00995Auranofinapproved, investigationalyesinhibitorDetails
DB03608DiminazeneexperimentalunknownDetails
DB09221PolaprezincexperimentalunknowninducerDetails