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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

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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei32 – 321For phospholipase activityBy similarity
Active sitei47 – 471Cysteine sulfenic acid (-SOH) intermediateBy similarity

GO - Molecular functioni

  • glutathione peroxidase activity Source: RGD
  • peroxiredoxin activity Source: UniProtKB-EC
  • phospholipase A2 activity Source: Ensembl

GO - Biological processi

  • cellular oxidant detoxification Source: GOC
  • hydrogen peroxide catabolic process Source: RGD
  • phospholipid catabolic process Source: Ensembl
  • response to oxidative stress Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Hydrolase, Oxidoreductase, Peroxidase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi1.11.1.15. 5301.
ReactomeiR-RNO-3299685. Detoxification of Reactive Oxygen Species.

Protein family/group databases

PeroxiBasei4427. Rno1CysPrx.

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.-)
Short name:
aiPLA2
Antioxidant protein 2
Non-selenium glutathione peroxidase (EC:1.11.1.9)
Short name:
NSGPx
Thiol-specific antioxidant protein
Gene namesi
Name:Prdx6
Synonyms:Aipla2, Aop2, Tsa
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi71005. Prdx6.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 224223Peroxiredoxin-6PRO_0000135104Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441PhosphothreonineBy similarity
Disulfide bondi47 – 47Interchain; in linked formBy similarity
Modified residuei63 – 631N6-acetyllysineBy similarity
Modified residuei89 – 891PhosphotyrosineBy similarity
Modified residuei209 – 2091N6-acetyllysine; alternateBy similarity
Modified residuei209 – 2091N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiO35244.
PRIDEiO35244.

2D gel databases

World-2DPAGE0004:O35244.

PTM databases

iPTMnetiO35244.
PhosphoSiteiO35244.
SwissPalmiO35244.

Expressioni

Gene expression databases

GenevisibleiO35244. RN.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
YWHAEP622582EBI-915490,EBI-356498From a different organism.
YwhaeP622592EBI-915490,EBI-356480From a different organism.

Protein-protein interaction databases

IntActiO35244. 4 interactions.
STRINGi10116.ENSRNOP00000030323.

Structurei

3D structure databases

ProteinModelPortaliO35244.
SMRiO35244. Positions 5-224.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 169165ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family. Rehydrin subfamily.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0854. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00550000074794.
HOGENOMiHOG000022346.
HOVERGENiHBG105234.
InParanoidiO35244.
KOiK11188.
OMAiIRFHDYL.
OrthoDBiEOG7CNZGP.
PhylomeDBiO35244.
TreeFamiTF105183.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliO35244.
SMRiO35244. Positions 5-224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO35244. 4 interactions.
STRINGi10116.ENSRNOP00000030323.

Protein family/group databases

PeroxiBasei4427. Rno1CysPrx.

PTM databases

iPTMnetiO35244.
PhosphoSiteiO35244.
SwissPalmiO35244.

2D gel databases

World-2DPAGE0004:O35244.

Proteomic databases

PaxDbiO35244.
PRIDEiO35244.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9588.
RGDi71005. Prdx6.

Phylogenomic databases

eggNOGiKOG0854. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00550000074794.
HOGENOMiHOG000022346.
HOVERGENiHBG105234.
InParanoidiO35244.
KOiK11188.
OMAiIRFHDYL.
OrthoDBiEOG7CNZGP.
PhylomeDBiO35244.
TreeFamiTF105183.

Enzyme and pathway databases

BRENDAi1.11.1.15. 5301.
ReactomeiR-RNO-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

NextBioi617808.
PROiO35244.

Gene expression databases

GenevisibleiO35244. RN.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Kim T.-S., Feinstein S.I., Dodia C., Hennigan B.B., Fisher A.B.
    Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Lung.
  2. Andreeva S.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Olfactory epithelium.
  3. Lubec G., Afjehi-Sadat L., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-41; 57-84; 98-118; 133-142; 156-162 AND 183-199, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Spinal cord.
  4. "Identification of a human cDNA clone for lysosomal type Ca2+-independent phospholipase A2 and properties of the expressed protein."
    Kim T.-S., Sundaresh C.S., Feinstein S.I., Dodia C., Skach W.R., Jain M.K., Nagase T., Seki N., Ishikawa K., Nomura N., Fisher A.B.
    J. Biol. Chem. 272:2542-2550(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-42 AND 146-163.
  5. "Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST."
    Manevich Y., Feinstein S.I., Fisher A.B.
    Proc. Natl. Acad. Sci. U.S.A. 101:3780-3785(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVATION BY GLUTATHIONE.

Entry informationi

Entry nameiPRDX6_RAT
AccessioniPrimary (citable) accession number: O35244
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.