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Protein

Peroxiredoxin-6

Gene

Prdx6

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.3 Publications

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.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=0.25 mM for dipalmitoyl phosphatidylcholine1 Publication
  1. Vmax=1.89 nmol/h/mg enzyme for dipalmitoyl phosphatidylcholine1 Publication

pH dependencei

Optimum pH is 4 (for phospholipase activity).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei32Important for phospholipase activity1 Publication1
Active sitei47Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activity1 Publication1
Active sitei140For phospholipase activity1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BRENDAi1.11.1.15. 5301.
ReactomeiR-RNO-3299685. Detoxification of Reactive Oxygen Species.
R-RNO-6798695. Neutrophil degranulation.

Protein family/group databases

PeroxiBasei4427. Rno1CysPrx.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-6 (EC:1.11.1.151 Publication)
Alternative name(s):
1-Cys peroxiredoxin
Short name:
1-Cys PRX
Acidic calcium-independent phospholipase A2 (EC:3.1.1.41 Publication)
Short name:
aiPLA2
Antioxidant protein 2
Non-selenium glutathione peroxidase
Short name:
NSGPx
Thiol-specific antioxidant protein
Gene namesi
Name:Prdx6
Synonyms:Aipla2, Aop2, Tsa
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi71005. 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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi26H → A: Abolishes lipid binding. 1 Publication1
Mutagenesisi32S → A: Abolishes lipid binding. 1 Publication1
Mutagenesisi140D → A: Abolishes phospholipase activity, but does not impair lipid binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001351042 – 224Peroxiredoxin-6Add BLAST223

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei44PhosphothreonineBy similarity1
Modified residuei63N6-acetyllysineBy similarity1
Modified residuei89PhosphotyrosineBy similarity1
Modified residuei177Phosphothreonine; by MAPK1 Publication1
Modified residuei209N6-acetyllysine; alternateBy similarity1
Modified residuei209N6-succinyllysine; alternateBy similarity1

Post-translational modificationi

Phosphorylation at Thr-177 by MAP kinases increases the phospholipase activity of the enzyme.1 Publication
Irreversibly inactivated by overoxidation of Cys-47 to sulfinic acid (Cys-SO2H) and sulfonic acid (Cys-SO3H) forms upon oxidative stress.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiO35244.
PRIDEiO35244.

2D gel databases

World-2DPAGEi0004:O35244.

PTM databases

iPTMnetiO35244.
PhosphoSitePlusiO35244.
SwissPalmiO35244.

Expressioni

Gene expression databases

BgeeiENSRNOG00000002896.
GenevisibleiO35244. RN.

Interactioni

Subunit structurei

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

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi250165. 2 interactors.
IntActiO35244. 4 interactors.
STRINGi10116.ENSRNOP00000030323.

Structurei

3D structure databases

ProteinModelPortaliO35244.
SMRiO35244.
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 bodies1 Publication10

Sequence similaritiesi

Belongs to the peroxiredoxin family. Prx6 subfamily.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0854. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00550000074794.
HOGENOMiHOG000022346.
HOVERGENiHBG105234.
InParanoidiO35244.
KOiK11188.
OMAiYPIIADD.
OrthoDBiEOG091G0IWK.
PhylomeDBiO35244.
TreeFamiTF105183.

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.

O35244-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGGLLLGDE APNFEANTTI GHIRFHDFLG DSWGILFSHP RDFTPVCTTE
60 70 80 90 100
LGRAAKLAPE FAKRNVKLIA LSIDSVEDHF AWSKDINAYN GAAPTEKLPF
110 120 130 140 150
PIIDDKDRDL AILLGMLDPA EKDEKGMPVT ARVVFIFGPD KKLKLSILYP
160 170 180 190 200
ATTGRNFDEI LRVVDSLQLT ASNPVATPVD WKKGESVMVL PTLPEEEAKQ
210 220
LFPKGVFTKE LPSGKKYLRY TPQP
Length:224
Mass (Da):24,819
Last modified:January 23, 2007 - v3
Checksum:iEE41D9079A708FD9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF014009 mRNA. Translation: AAB66341.1.
Y17295 mRNA. Translation: CAA76732.1.
RefSeqiNP_446028.1. NM_053576.2.
UniGeneiRn.42.

Genome annotation databases

EnsembliENSRNOT00000034583; ENSRNOP00000030323; ENSRNOG00000002896.
GeneIDi94167.
KEGGirno:94167.
UCSCiRGD:71005. rat.

Similar proteinsi

Entry informationi

Entry nameiPRDX6_RAT
AccessioniPrimary (citable) accession number: O35244
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 149 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, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families