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Protein

Peroxiredoxin-6

Gene

PRDX6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in redox regulation of the cell. Can reduce H2O2 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.

Miscellaneous

The active site is the redox-active Cys-47 oxidized to Cys-SOH. Unlike 2-Cys peroxiredoxins, PRDX6 conserves only this peroxidatic cysteine. To regenerate and activate the enzyme, the oxidized form is directly reduced to cysteine by glutathione and not thioredoxin.
Irreversibly inactivated by overoxidation of Cys-47 (to Cys-SO3H) upon oxidative stress.

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei32For phospholipase activity1
Active sitei47Cysteine sulfenic acid (-SOH) intermediate1

GO - Molecular functioni

  • cadherin binding Source: BHF-UCL
  • calcium-independent phospholipase A2 activity Source: CAFA
  • glutathione peroxidase activity Source: CAFA
  • peroxiredoxin activity Source: UniProtKB-EC
  • protein homodimerization activity Source: CAFA
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • cellular oxidant detoxification Source: CAFA
  • cellular response to oxidative stress Source: Reactome
  • glycerophospholipid catabolic process Source: CAFA
  • hydrogen peroxide catabolic process Source: Ensembl
  • neutrophil degranulation Source: Reactome
  • response to oxidative stress Source: CAFA

Keywordsi

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

Enzyme and pathway databases

BRENDAi1.11.1.15. 2681.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.
R-HSA-6798695. Neutrophil degranulation.
SIGNORiP30041.

Protein family/group databases

PeroxiBasei4426. Hs1CysPrx01.

Chemistry databases

SwissLipidsiSLP:000001691.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-6 (EC:1.11.1.15)
Alternative name(s):
1-Cys peroxiredoxin
Short name:
1-Cys PRX
24 kDa protein
Acidic calcium-independent phospholipase A2 (EC:3.1.1.-)
Short name:
aiPLA2
Antioxidant protein 2
Liver 2D page spot 40
Non-selenium glutathione peroxidase (EC:1.11.1.9)
Short name:
NSGPx
Red blood cells page spot 12
Gene namesi
Name:PRDX6
Synonyms:AOP2, KIAA0106
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:16753. PRDX6.

Subcellular locationi

GO - Cellular componenti

  • azurophil granule lumen Source: Reactome
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • membrane Source: UniProtKB

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Lysosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi32S → A: Loss of AIPLA2 activity, but no effect on NSGPX activity. 1
Mutagenesisi47C → S: Loss of NSGPX activity, but no effect on AIPLA2 activity. 1

Organism-specific databases

DisGeNETi9588.
OpenTargetsiENSG00000117592.
PharmGKBiPA134992760.

Chemistry databases

DrugBankiDB03814. 2-(N-Morpholino)-Ethanesulfonic Acid.
DB02325. Isopropyl Alcohol.

Polymorphism and mutation databases

BioMutaiPRDX6.
DMDMi1718024.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources4 Publications
ChainiPRO_00001351022 – 224Peroxiredoxin-6Add BLAST223

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei44PhosphothreonineCombined sources1
Disulfide bondi47Interchain; in linked formBy similarity
Modified residuei63N6-acetyllysineCombined sources1
Modified residuei89PhosphotyrosineCombined sources1
Modified residuei209N6-acetyllysine; alternateCombined sources1
Modified residuei209N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiP30041.
PaxDbiP30041.
PeptideAtlasiP30041.
PRIDEiP30041.
TopDownProteomicsiP30041.

2D gel databases

DOSAC-COBS-2DPAGEiP30041.
OGPiP30041.
REPRODUCTION-2DPAGEiIPI00220301.
P30041.
SWISS-2DPAGEiP30041.

PTM databases

iPTMnetiP30041.
PhosphoSitePlusiP30041.
SwissPalmiP30041.

Expressioni

Gene expression databases

BgeeiENSG00000117592.
CleanExiHS_PRDX6.
ExpressionAtlasiP30041. baseline and differential.
GenevisibleiP30041. HS.

Organism-specific databases

HPAiCAB008663.
HPA006983.

Interactioni

Subunit structurei

Homotetramer. Interacts with GSTP1; mediates PRDX6 glutathionylation and regeneration. May interact with HTR2A (By similarity). Interacts with APEX1 and STH. May interact with FAM168B.By similarity3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • cadherin binding Source: BHF-UCL
  • protein homodimerization activity Source: CAFA
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi114956. 81 interactors.
IntActiP30041. 25 interactors.
MINTiMINT-4999165.
STRINGi9606.ENSP00000342026.

Structurei

Secondary structure

1224
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 18Combined sources4
Beta strandi21 – 24Combined sources4
Helixi25 – 29Combined sources5
Beta strandi32 – 40Combined sources9
Helixi45 – 62Combined sources18
Turni63 – 65Combined sources3
Beta strandi66 – 74Combined sources9
Helixi76 – 89Combined sources14
Beta strandi102 – 104Combined sources3
Helixi109 – 113Combined sources5
Beta strandi117 – 122Combined sources6
Beta strandi124 – 126Combined sources3
Beta strandi128 – 130Combined sources3
Beta strandi133 – 137Combined sources5
Beta strandi141 – 148Combined sources8
Beta strandi151 – 153Combined sources3
Helixi157 – 173Combined sources17
Beta strandi175 – 177Combined sources3
Beta strandi187 – 189Combined sources3
Helixi195 – 201Combined sources7
Beta strandi219 – 221Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PRXX-ray2.00A/B1-224[»]
5B6MX-ray2.50A/B/C/D/E/F1-224[»]
5B6NX-ray2.90A/B/C/D/E/F1-224[»]
ProteinModelPortaliP30041.
SMRiP30041.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30041.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the AhpC/TSA family. Rehydrin subfamily.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0854. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00550000074794.
HOGENOMiHOG000022346.
HOVERGENiHBG105234.
InParanoidiP30041.
KOiK11188.
OMAiYPIIADD.
OrthoDBiEOG091G0IWK.
PhylomeDBiP30041.
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.

P30041-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGGLLLGDV APNFEANTTV GRIRFHDFLG DSWGILFSHP RDFTPVCTTE
60 70 80 90 100
LGRAAKLAPE FAKRNVKLIA LSIDSVEDHL AWSKDINAYN CEEPTEKLPF
110 120 130 140 150
PIIDDRNREL AILLGMLDPA EKDEKGMPVT ARVVFVFGPD KKLKLSILYP
160 170 180 190 200
ATTGRNFDEI LRVVISLQLT AEKRVATPVD WKDGDSVMVL PTIPEEEAKK
210 220
LFPKGVFTKE LPSGKKYLRY TPQP
Length:224
Mass (Da):25,035
Last modified:January 23, 2007 - v3
Checksum:i017D955F0FEEDFBC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14662 mRNA. Translation: BAA03496.1.
DQ230990 Genomic DNA. Translation: ABB02185.1.
AL139142 Genomic DNA. No translation available.
AK289352 mRNA. Translation: BAF82041.1.
CH471067 Genomic DNA. Translation: EAW90944.1.
BC035857 mRNA. Translation: AAH35857.1.
BC053550 mRNA. Translation: AAH53550.1.
AJ844621 mRNA. Translation: CAH59743.1.
CCDSiCCDS1307.1.
RefSeqiNP_004896.1. NM_004905.2.
UniGeneiHs.120.
Hs.731505.

Genome annotation databases

EnsembliENST00000340385; ENSP00000342026; ENSG00000117592.
GeneIDi9588.
KEGGihsa:9588.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiPRDX6_HUMAN
AccessioniPrimary (citable) accession number: P30041
Secondary accession number(s): A8JZY7
, P32077, Q5TAH4, Q5ZEZ8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: July 5, 2017
This is version 189 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families