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P35704

- PRDX2_RAT

UniProt

P35704 - PRDX2_RAT

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Protein
Peroxiredoxin-2
Gene
Prdx2, Tdpx1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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) intermediate By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. negative regulation of neuron apoptotic process Source: RGD
  2. removal of superoxide radicals Source: Ensembl
  3. response to oxidative stress Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

ReactomeiREACT_213899. 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: Chromosome 19

Organism-specific databases

RGDi3838. Prdx2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Disulfide bondi51 – 51Interchain (with C-172); in linked form By similarity
Disulfide bondi172 – 172Interchain (with C-51); in linked form By similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiP35704.
PRIDEiP35704.

2D gel databases

World-2DPAGEi0004:P35704.

PTM databases

PhosphoSiteiP35704.

Expressioni

Gene expression databases

GenevestigatoriP35704.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP35704.
SMRiP35704. Positions 3-198.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 164159Thioredoxin
Add
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family.
Contains 1 thioredoxin domain.

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0450.
GeneTreeiENSGT00390000004653.
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

MASGNAHIGK PAPDFTGTAV VDGAFKEIKL SDYRGKYVVL FFYPLDFTFV    50
CPTEIIAFSD HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN 100
IPLLADVTKS LSQNYGVLKN DEGIAYRGLF IIDAKGVLRQ ITVNDLPVGR 150
SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS DTIKPNVDDS KEYFSKHN 198
Length:198
Mass (Da):21,784
Last modified:January 23, 2007 - v3
Checksum:iFC6AD9B0E9C4447B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171G → A in AAH58481. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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

EnsembliENSRNOT00000004799; ENSRNOP00000004799; ENSRNOG00000003520.
GeneIDi29338.
KEGGirno:29338.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U06099 mRNA. Translation: AAA19959.1 .
BC058481 mRNA. Translation: AAH58481.1 .
PIRi A57716.
RefSeqi NP_058865.1. NM_017169.1.
XP_006255306.1. XM_006255244.1.
UniGenei Rn.2511.

3D structure databases

ProteinModelPortali P35704.
SMRi P35704. Positions 3-198.
ModBasei Search...

Protein-protein interaction databases

BioGridi 247997. 2 interactions.
IntActi P35704. 2 interactions.
STRINGi 10116.ENSRNOP00000004799.

Protein family/group databases

PeroxiBasei 4477. Rno2CysPrx02.

PTM databases

PhosphoSitei P35704.

2D gel databases

World-2DPAGEi 0004:P35704.

Proteomic databases

PaxDbi P35704.
PRIDEi P35704.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000004799 ; ENSRNOP00000004799 ; ENSRNOG00000003520 .
GeneIDi 29338.
KEGGi rno:29338.

Organism-specific databases

CTDi 7001.
RGDi 3838. Prdx2.

Phylogenomic databases

eggNOGi COG0450.
GeneTreei ENSGT00390000004653.
HOGENOMi HOG000022343.
HOVERGENi HBG000286.
InParanoidi P35704.
KOi K03386.
OrthoDBi EOG7T1RCD.
PhylomeDBi P35704.
TreeFami TF105181.

Enzyme and pathway databases

Reactomei REACT_213899. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

NextBioi 608824.
PROi P35704.

Gene expression databases

Genevestigatori P35704.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view ]
PIRSFi PIRSF000239. AHPC. 1 hit.
SUPFAMi SSF52833. SSF52833. 1 hit.
PROSITEi PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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.

Entry informationi

Entry nameiPRDX2_RAT
AccessioniPrimary (citable) accession number: P35704
Secondary accession number(s): Q6PDV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 120 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.
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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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