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P35704 (PRDX2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Prdx2
Synonyms:Tdpx1
OrganismRattus norvegicus (Rat) [Reference proteome]
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 H2O2.

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H2O + 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-SO2H and Cys-SO3H. Cys-SO2H is retroreduced to Cys-SOH after removal of H2O2, while Cys-SO3H may be irreversibly oxidized By similarity.

Sequence similarities

Belongs to the AhpC/TSA family.

Contains 1 thioredoxin domain.

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 [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] [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(2004) [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 (JUL-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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U06099 mRNA. Translation: AAA19959.1.
BC058481 mRNA. Translation: AAH58481.1.
PIRA57716.
RefSeqNP_058865.1. NM_017169.1.
XP_006255306.1. XM_006255244.1.
UniGeneRn.2511.

3D structure databases

ProteinModelPortalP35704.
SMRP35704. Positions 3-198.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247997. 2 interactions.
IntActP35704. 2 interactions.
STRING10116.ENSRNOP00000004799.

Protein family/group databases

PeroxiBase4477. Rno2CysPrx02.

PTM databases

PhosphoSiteP35704.

2D gel databases

World-2DPAGE0004:P35704.

Proteomic databases

PaxDbP35704.
PRIDEP35704.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000004799; ENSRNOP00000004799; ENSRNOG00000003520.
GeneID29338.
KEGGrno:29338.

Organism-specific databases

CTD7001.
RGD3838. Prdx2.

Phylogenomic databases

eggNOGCOG0450.
GeneTreeENSGT00390000004653.
HOGENOMHOG000022343.
HOVERGENHBG000286.
InParanoidP35704.
KOK03386.
OrthoDBEOG7T1RCD.
PhylomeDBP35704.
TreeFamTF105181.

Gene expression databases

GenevestigatorP35704.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFPIRSF000239. AHPC. 1 hit.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio608824.
PROP35704.

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: May 14, 2014
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families