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Protein

Peroxiredoxin-2

Gene

Prdx2

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. Reduces peroxides with reducing equivalents provided through the thioredoxin system. It is not able to receive electrons from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei51 – 511Cysteine sulfenic acid (-SOH) intermediateBy similarity

GO - Molecular functioni

  1. peroxidase activity Source: UniProtKB-KW
  2. peroxiredoxin activity Source: UniProtKB-EC

GO - Biological processi

  1. activation of MAPK activity Source: Ensembl
  2. homeostasis of number of cells Source: Ensembl
  3. hydrogen peroxide catabolic process Source: Ensembl
  4. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  5. negative regulation of lipopolysaccharide-mediated signaling pathway Source: Ensembl
  6. negative regulation of neuron apoptotic process Source: RGD
  7. negative regulation of NF-kappaB transcription factor activity Source: Ensembl
  8. negative regulation of reactive oxygen species metabolic process Source: Ensembl
  9. negative regulation of T cell differentiation Source: Ensembl
  10. positive regulation of blood coagulation Source: Ensembl
  11. regulation of hydrogen peroxide metabolic process Source: Ensembl
  12. removal of superoxide radicals Source: Ensembl
  13. respiratory burst involved in inflammatory response Source: Ensembl
  14. response to lipopolysaccharide Source: Ensembl
  15. response to oxidative stress Source: RGD
  16. T cell proliferation Source: Ensembl
  17. thymus development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BRENDAi1.11.1.15. 5301.
ReactomeiREACT_317923. Detoxification of Reactive Oxygen Species.

Protein family/group databases

PeroxiBasei4477. Rno2CysPrx02.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-2 (EC:1.11.1.15)
Alternative name(s):
Thiol-specific antioxidant protein
Short name:
TSA
Thioredoxin peroxidase 1
Thioredoxin-dependent peroxide reductase 1
Gene namesi
Name:Prdx2
Synonyms:Tdpx1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi3838. Prdx2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RGD
  2. extracellular vesicular exosome Source: Ensembl
  3. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 198197Peroxiredoxin-2PRO_0000135083Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Disulfide bondi51 – 51Interchain (with C-172); in linked formBy similarity
Modified residuei112 – 1121PhosphoserineBy similarity
Disulfide bondi172 – 172Interchain (with C-51); in linked formBy similarity
Modified residuei182 – 1821PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP35704.
PRIDEiP35704.

2D gel databases

World-2DPAGE0004:P35704.

PTM databases

PhosphoSiteiP35704.

Expressioni

Gene expression databases

GenevestigatoriP35704.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation. Interacts with TIPIN (By similarity).By similarity

Protein-protein interaction databases

BioGridi247997. 3 interactions.
IntActiP35704. 2 interactions.
STRINGi10116.ENSRNOP00000004799.

Structurei

3D structure databases

ProteinModelPortaliP35704.
SMRiP35704. Positions 3-198.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 164159ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0450.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiP35704.
KOiK03386.
OrthoDBiEOG7T1RCD.
PhylomeDBiP35704.
TreeFamiTF105181.

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.

P35704-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGNAHIGK PAPDFTGTAV VDGAFKEIKL SDYRGKYVVL FFYPLDFTFV
60 70 80 90 100
CPTEIIAFSD HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN
110 120 130 140 150
IPLLADVTKS LSQNYGVLKN DEGIAYRGLF IIDAKGVLRQ ITVNDLPVGR
160 170 180 190
SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS DTIKPNVDDS KEYFSKHN
Length:198
Mass (Da):21,784
Last modified:January 22, 2007 - v3
Checksum:iFC6AD9B0E9C4447B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171G → A in AAH58481 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06099 mRNA. Translation: AAA19959.1.
BC058481 mRNA. Translation: AAH58481.1.
PIRiA57716.
RefSeqiNP_058865.1. NM_017169.1.
XP_006255306.1. XM_006255244.1.
UniGeneiRn.2511.

Genome annotation databases

GeneIDi29338.
KEGGirno:29338.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U06099 mRNA. Translation: AAA19959.1.
BC058481 mRNA. Translation: AAH58481.1.
PIRiA57716.
RefSeqiNP_058865.1. NM_017169.1.
XP_006255306.1. XM_006255244.1.
UniGeneiRn.2511.

3D structure databases

ProteinModelPortaliP35704.
SMRiP35704. Positions 3-198.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247997. 3 interactions.
IntActiP35704. 2 interactions.
STRINGi10116.ENSRNOP00000004799.

Protein family/group databases

PeroxiBasei4477. Rno2CysPrx02.

PTM databases

PhosphoSiteiP35704.

2D gel databases

World-2DPAGE0004:P35704.

Proteomic databases

PaxDbiP35704.
PRIDEiP35704.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29338.
KEGGirno:29338.

Organism-specific databases

CTDi7001.
RGDi3838. Prdx2.

Phylogenomic databases

eggNOGiCOG0450.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiP35704.
KOiK03386.
OrthoDBiEOG7T1RCD.
PhylomeDBiP35704.
TreeFamiTF105181.

Enzyme and pathway databases

BRENDAi1.11.1.15. 5301.
ReactomeiREACT_317923. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

NextBioi608824.
PROiP35704.

Gene expression databases

GenevestigatoriP35704.

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

« Hide 'large scale' publications
  1. "Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes."
    Chae H.Z., Robison K., Poole L.B., Church G., Storz G., Rhee S.G.
    Proc. Natl. Acad. Sci. U.S.A. 91:7017-7021(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary.
  3. Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.
    Submitted (JUN-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 93-135 AND 140-157, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.

Entry informationi

Entry nameiPRDX2_RAT
AccessioniPrimary (citable) accession number: P35704
Secondary accession number(s): Q6PDV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 1994
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 125 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-51 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-172-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin (By similarity).By similarity
Inactivated upon oxidative stress by overoxidation of Cys-51 to Cys-SO2H and Cys-SO3H. Cys-SO2H is retroreduced to Cys-SOH after removal of H2O2, while Cys-SO3H may be irreversibly oxidized (By similarity).By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.