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P35704

- PRDX2_RAT

UniProt

P35704 - PRDX2_RAT

Protein

Peroxiredoxin-2

Gene

Prdx2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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. negative regulation of neuron apoptotic process Source: RGD
    2. removal of superoxide radicals Source: Ensembl
    3. response to oxidative stress Source: RGD

    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

    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
    Disulfide bondi172 – 172Interchain (with C-51); in linked formBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond

    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. 2 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.
    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

    Experimental Info

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

    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...
    MobiDBi 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-2DPAGE 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

    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: October 1, 2014
    This is version 121 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