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Protein

Peroxiredoxin-6

Gene

Prdx6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides. Also has phospholipase activity, and can therefore either reduce the oxidized sn-2 fatty acyl grup of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH. Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis.By similarity

Miscellaneous

The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this 1-Cys peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide with a cysteine from another protein or with a small thiol molecule. C(P) is reactivated by glutathionylation mediated by glutathione S-transferase Pi, followed by spontaneous reduction of the enzyme with glutathione.By similarity

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.By similarity
Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei32Important for phospholipase activityBy similarity1
Active sitei47Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activityBy similarity1
Active sitei140For phospholipase activityBy similarity1

GO - Molecular functioni

GO - Biological processi

  • bleb assembly Source: MGI
  • cell redox homeostasis Source: InterPro
  • cellular oxidant detoxification Source: MGI
  • glycerophospholipid catabolic process Source: MGI
  • positive regulation of mRNA splicing, via spliceosome Source: MGI
  • response to oxidative stress Source: MGI
  • response to reactive oxygen species Source: MGI

Keywordsi

Molecular functionAntioxidant, Hydrolase, Multifunctional enzyme, Oxidoreductase, Peroxidase
Biological processLipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi1.11.1.15 3474

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-6 (EC:1.11.1.15)
Alternative name(s):
1-Cys peroxiredoxin
Short name:
1-Cys PRX
Acidic calcium-independent phospholipase A2 (EC:3.1.1.4)
Short name:
aiPLA2
Antioxidant protein 2
Non-selenium glutathione peroxidase
Short name:
NSGPx
Gene namesi
Name:Prdx6
Synonyms:Aop2, Ltw4, Prdx5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:894320 Prdx6

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001351032 – 224Peroxiredoxin-6Add BLAST223

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei44PhosphothreonineBy similarity1
Modified residuei63N6-acetyllysineBy similarity1
Modified residuei89PhosphotyrosineCombined sources1
Modified residuei93PhosphothreonineCombined sources1
Modified residuei177Phosphothreonine; by MAPKBy similarity1
Modified residuei209N6-acetyllysine; alternateBy similarity1
Modified residuei209N6-succinyllysine; alternateCombined sources1

Post-translational modificationi

Irreversibly inactivated by overoxidation of Cys-47 to sulfinic acid (Cys-SO2H) and sulfonic acid (Cys-SO3H) forms upon oxidative stress.By similarity
Phosphorylation at Thr-177 by MAP kinases increases the phospholipase activity of the enzyme.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO08709
MaxQBiO08709
PaxDbiO08709
PeptideAtlasiO08709
PRIDEiO08709
TopDownProteomicsiO08709

2D gel databases

COMPLUYEAST-2DPAGEO08709
REPRODUCTION-2DPAGEO08709
SWISS-2DPAGEO08709
UCD-2DPAGEO08709

PTM databases

iPTMnetiO08709
PhosphoSitePlusiO08709
SwissPalmiO08709

Expressioni

Tissue specificityi

Highly expressed in heart, kidney and liver. Moderate expression in brain and stomach. Very low levels in intestine.

Gene expression databases

CleanExiMM_PRDX5
MM_PRDX6

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with GSTP1; mediates PRDX6 glutathionylation and regeneration (By similarity). Interacts with APEX1. Interacts with STH. May interact with FAM168B (By similarity). May interact with HTR2A (PubMed:14988405).By similarity1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198118, 4 interactors
IntActiO08709, 9 interactors
MINTiO08709
STRINGi10090.ENSMUSP00000071636

Structurei

3D structure databases

ProteinModelPortaliO08709
SMRiO08709
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 169ThioredoxinPROSITE-ProRule annotationAdd BLAST165

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni31 – 40Required and sufficient for targeting to lysosomes and lamellar bodiesBy similarity10

Sequence similaritiesi

Belongs to the peroxiredoxin family. Prx6 subfamily.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0854 Eukaryota
COG0450 LUCA
HOVERGENiHBG105234
InParanoidiO08709
KOiK11188

Family and domain databases

InterProiView protein in InterPro
IPR000866 AhpC/TSA
IPR024706 Peroxiredoxin_AhpC-typ
IPR019479 Peroxiredoxin_C
IPR036249 Thioredoxin-like_sf
IPR013766 Thioredoxin_domain
PfamiView protein in Pfam
PF10417 1-cysPrx_C, 1 hit
PF00578 AhpC-TSA, 1 hit
PIRSFiPIRSF000239 AHPC, 1 hit
SUPFAMiSSF52833 SSF52833, 1 hit
PROSITEiView protein in PROSITE
PS51352 THIOREDOXIN_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O08709-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGGLLLGDE APNFEANTTI GRIRFHDFLG DSWGILFSHP RDFTPVCTTE
60 70 80 90 100
LGRAAKLAPE FAKRNVKLIA LSIDSVEDHL AWSKDINAYN GETPTEKLPF
110 120 130 140 150
PIIDDKGRDL AILLGMLDPV EKDDNNMPVT ARVVFIFGPD KKLKLSILYP
160 170 180 190 200
ATTGRNFDEI LRVVDSLQLT GTKPVATPVD WKKGESVMVV PTLSEEEAKQ
210 220
CFPKGVFTKE LPSGKKYLRY TPQP
Length:224
Mass (Da):24,871
Last modified:January 23, 2007 - v3
Checksum:iAECDEDD332858B8F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti154G → S in AAC67553 (PubMed:10395907).Curated1
Sequence conflicti181W → R in AAD03716 (PubMed:10395907).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti124D → A in strain: C57BL/6, C57BL/6J and FVB/N. Combined sources1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004670 mRNA Translation: AAC53277.1
Y12883 mRNA Translation: CAA73383.1
AF093852 mRNA Translation: AAC63376.1
AF093853 Genomic DNA Translation: AAC67553.1
AF093857
, AF093854, AF093855, AF093856 Genomic DNA Translation: AAD03716.1
AK030413 mRNA Translation: BAC26952.1
BC013489 mRNA Translation: AAH13489.1
CCDSiCCDS15415.1
RefSeqiNP_031479.1, NM_007453.4
UniGeneiMm.186185

Genome annotation databases

GeneIDi11758
KEGGimmu:11758

Similar proteinsi

Entry informationi

Entry nameiPRDX6_MOUSE
AccessioniPrimary (citable) accession number: O08709
Secondary accession number(s): Q91WT2, Q9QWP4, Q9QWW0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 166 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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