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Protein

Peroxiredoxin-6

Gene

PRDX6

Organism
Bos taurus (Bovine)
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.2 Publications
Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.1 Publication

Cofactori

Note: Does not need Ca2+ as cofactor.1 Publication

Kineticsi

  1. KM=25 µM for H2O21 Publication
  2. KM=180 µM for H2O21 Publication
  3. KM=22 µM for tert-butyl hydroperoxide1 Publication
  4. KM=142 µM for tert-butyl hydroperoxide1 Publication
  5. KM=170 µM for cumene hydroperoxide1 Publication
  6. KM=120 µM for cumene hydroperoxide1 Publication
  7. KM=12 µM for triphenylcarbinyl hydroperoxide1 Publication
  8. KM=34 µM for linoleic hydroperoxide1 Publication
  9. KM=141 µM for linolenoyl hydroperoxide1 Publication
  10. KM=135 µM for arachidonoyl hydroperoxide1 Publication
  11. KM=120 µM for PLCP hydroperoxide1 Publication
  12. KM=129 µM for PACP hydroperoxide1 Publication
  13. KM=22 µM for 5-phenyl-3-pentenyl hydroperoxide1 Publication
  14. KM=350 µM for dipalmitoyl phosphatidylcholine (at pH 4)1 Publication
  1. Vmax=5.07 µmol/min/mg enzyme for H2O21 Publication
  2. Vmax=1810 nmol/min/mg enzyme for H2O21 Publication
  3. Vmax=8.56 µmol/min/mg enzyme for tert-butyl hydroperoxide1 Publication
  4. Vmax=1270 nmol/min/mg enzyme for tert-butyl hydroperoxide1 Publication
  5. Vmax=9.18 µmol/min/mg enzyme for cumene hydroperoxide1 Publication
  6. Vmax=1120 nmol/min/mg enzyme for cumene hydroperoxide1 Publication
  7. Vmax=2.57 µmol/min/mg enzyme for triphenylcarbinyl hydroperoxide1 Publication
  8. Vmax=9.88 µmol/min/mg enzyme for linoleic hydroperoxide1 Publication
  9. Vmax=1390 nmol/min/mg enzyme for linolenoyl hydroperoxide1 Publication
  10. Vmax=7.34 µmol/min/mg enzyme for 5-phenyl-3-pentenyl hydroperoxide1 Publication
  11. Vmax=1380 nmol/min/mg enzyme for arachidonoyl hydroperoxide1 Publication
  12. Vmax=1500 nmol/min/mg enzyme for PLCP hydroperoxide1 Publication
  13. Vmax=1640 nmol/min/mg enzyme for PACP hydroperoxide1 Publication
  14. Vmax=4225 nmol/h/mg enzyme for dipalmitoyl phosphatidylcholine (at pH 4)1 Publication

pH dependencei

Optimum pH is 7-8.1 Publication

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

Keywordsi

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

Enzyme and pathway databases

BRENDAi1.11.1.15. 908.
ReactomeiR-BTA-3299685. Detoxification of Reactive Oxygen Species.
R-BTA-6798695. Neutrophil degranulation.

Protein family/group databases

PeroxiBasei4423. Bt1CysPrx.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-6 (EC:1.11.1.152 Publications)
Alternative name(s):
1-Cys peroxiredoxin
Short name:
1-Cys PRX
Acidic calcium-independent phospholipase A21 Publication (EC:3.1.1.41 Publication)
Short name:
aiPLA2
Antioxidant protein 2
Ciliary body glutathione peroxidase
Non-selenium glutathione peroxidase
Short name:
NSGPx
PHGPx
Gene namesi
Name:PRDX6
Synonyms:AOP2, GPX, PHGPX
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 16

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 methionineiRemovedBy similarity
ChainiPRO_00001351012 – 224Peroxiredoxin-6Add BLAST223

Amino acid modifications

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

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

PaxDbiO77834.
PeptideAtlasiO77834.
PRIDEiO77834.

Expressioni

Gene expression databases

BgeeiENSBTAG00000004855.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with GSTP1; mediates PRDX6 glutathionylation and regeneration (PubMed:15004285). Interacts with APEX1. Interacts with STH. May interact with FAM168B (By similarity). May interact with HTR2A (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000006383.

Structurei

3D structure databases

ProteinModelPortaliO77834.
SMRiO77834.
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.
GeneTreeiENSGT00550000074794.
HOGENOMiHOG000022346.
HOVERGENiHBG105234.
InParanoidiO77834.
KOiK11188.
OMAiYPIIADD.
OrthoDBiEOG091G0IWK.
TreeFamiTF105183.

Family and domain databases

InterProiView protein in InterPro
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
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.

O77834-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGGLLLGDE APNFEANTTI GRIRFHDYLG DSWGILFSHP RDFTPVCTTE
60 70 80 90 100
LGRAAKLAPE FAKRNVKMIA LSIDSVEDHL AWSKDINAYN GEEPTEKLPF
110 120 130 140 150
PIIDDKNRDL AIQLGMLDPA EKDEKGMPVT ARVVFIFGPD KKLKLSILYP
160 170 180 190 200
ATTGRNFDEI LRVIISLQLT AEKRVATPVD WKNGDSVMVL PTIPEEEAKK
210 220
LFPKGVFTKE LPSGKKYLRY TPQP
Length:224
Mass (Da):25,067
Last modified:January 23, 2007 - v3
Checksum:i4013D59C4D9FC05E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF080228 mRNA. Translation: AAC63016.1.
AF090194 mRNA. Translation: AAC84043.1.
AJ243848 mRNA. Translation: CAB64802.1.
BT020967 mRNA. Translation: AAX08984.1.
BC102172 mRNA. Translation: AAI02173.1.
RefSeqiNP_777068.1. NM_174643.1.
UniGeneiBt.49705.

Genome annotation databases

EnsembliENSBTAT00000006383; ENSBTAP00000006383; ENSBTAG00000004855.
GeneIDi282438.
KEGGibta:282438.

Similar proteinsi

Entry informationi

Entry nameiPRDX6_BOVIN
AccessioniPrimary (citable) accession number: O77834
Secondary accession number(s): Q5E9F3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: September 27, 2017
This is version 126 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