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Reviewed, UniProtKB/Swiss-Prot P35704 (PRDX2_RAT)

Last modified November 25, 2008. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peroxiredoxin-2
    EC=1.11.1.15
Alternative name(s):
    Thioredoxin peroxidase 1
    Thioredoxin-dependent peroxide reductase 1
    Thiol-specific antioxidant protein
      Short name=TSA
Gene names
Name: Prdx2
Synonyms: Tdpx1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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 H(2)O(2).

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.

Subunit structure

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

Subcellular location

Cytoplasm.

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.

Inactivated upon oxidative stress by overoxidation of Cys-51 to Cys-SO(2)H and Cys-SO(3)H. Cys-SO(2)H is retroreduced to Cys-SOH after removal of H(2)O(2), while Cys-SO(3)H may be irreversibly oxidized By similarity.

Sequence similarities

Belongs to the ahpC/TSA family.

Contains 1 thioredoxin domain.

Ontologies

Keywords

   Cellular componentCytoplasm
   DomainRedox-active center
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   PTMAcetylation
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionperoxiredoxin activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 198197Peroxiredoxin-2
PRO_0000135083

Regions

Domain6 – 164159Thioredoxin

Sites

Active site511Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Disulfide bond51Interchain (with C-172); in linked form By similarity
Disulfide bond172Interchain (with C-51); in linked form By similarity

Experimental info

Sequence conflict171G → A in AAH58481. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P35704-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: FC6AD9B0E9C4447B

FASTA19821,784
        10         20         30         40         50         60 
MASGNAHIGK PAPDFTGTAV VDGAFKEIKL SDYRGKYVVL FFYPLDFTFV CPTEIIAFSD 

        70         80         90        100        110        120 
HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTKS LSQNYGVLKN 

       130        140        150        160        170        180 
DEGIAYRGLF IIDAKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS 

       190 
DTIKPNVDDS KEYFSKHN 

« Hide

References

« Hide 'large scale' references
[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(1994) [PubMed: 8041738] [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(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pituitary.
[3]Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 93-135 AND 140-157, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain, Hippocampus and Spinal cord.

Cross-references

Sequence databases

U06099 mRNA. Translation: AAA19959.1.
BC058481 mRNA. Translation: AAH58481.1.
PIRA57716.
RefSeqNP_058865.1.
UniGeneRn.2511

3D structure databases

HSSPHSSP built from PDB template 1QMV based on UniProtKB P32119.
SMRP35704. Positions 2-197, 3-198.
ModBaseSearch...

Protein family/group databases

PeroxiBase4477. Rno2CysPrx02.

PTM databases

PhosphoSiteP35704.

Genome annotation databases

EnsemblENSRNOG00000003520. Rattus norvegicus. [Contig view]
GeneID29338.
KEGGrno:29338.

Organism-specific databases

RGD3838. Prdx2.

Phylogenomic databases

HOVERGENP35704.

Gene expression databases

ArrayExpressP35704.
GermOnlineENSRNOG00000003520. Rattus norvegicus.

Family and domain databases

InterProIPR000866. AhpC-TSA.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF00578. AhpC-TSA. 1 hit.
[Graphical view]
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio608824.

Entry information

Entry namePRDX2_RAT
AccessionPrimary (citable) accession number: P35704
Secondary accession number(s): Q6PDV3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: November 25, 2008
This is version 76 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents