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Q61171

- PRDX2_MOUSE

UniProt

Q61171 - PRDX2_MOUSE

Protein

Peroxiredoxin-2

Gene

Prdx2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (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: MGI
    2. protein binding Source: MGI
    3. selenium binding Source: MGI
    4. thioredoxin peroxidase activity Source: MGI

    GO - Biological processi

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

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase, Peroxidase

    Enzyme and pathway databases

    ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.

    Protein family/group databases

    PeroxiBasei4474. Mm2CysPrx02.

    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, Tpx
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:109486. Prdx2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 198197Peroxiredoxin-2PRO_0000135081Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    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

    MaxQBiQ61171.
    PaxDbiQ61171.
    PRIDEiQ61171.

    2D gel databases

    REPRODUCTION-2DPAGEQ61171.
    SWISS-2DPAGEQ61171.
    UCD-2DPAGEQ61171.

    PTM databases

    PhosphoSiteiQ61171.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels in bone marrow. High levels also found in heart, brain, kidney and skeletal muscle. Lower levels in liver, lung and thymus.

    Gene expression databases

    ArrayExpressiQ61171.
    BgeeiQ61171.
    CleanExiMM_PRDX2.
    GenevestigatoriQ61171.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked, upon oxidation By similarity. Interacts with TIPIN.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi204094. 2 interactions.
    IntActiQ61171. 13 interactions.
    MINTiMINT-1862390.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61171.
    SMRiQ61171. 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.
    InParanoidiQ61171.
    KOiK03386.
    OMAiEGVIQHA.
    OrthoDBiEOG7T1RCD.
    PhylomeDBiQ61171.
    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.

    Q61171-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASGNAQIGK SAPDFTATAV 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):21,779
    Last modified:January 23, 2007 - v3
    Checksum:iFE216F5426F7174D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 381V → M in BAB27093. (PubMed:16141072)Curated
    Sequence conflicti39 – 391V → D in BAB23893. (PubMed:16141072)Curated
    Sequence conflicti69 – 691G → R in BAB23893. (PubMed:16141072)Curated
    Sequence conflicti97 – 971G → A in AAA69475. 1 PublicationCurated
    Sequence conflicti113 – 1131Q → H in BAB23893. (PubMed:16141072)Curated
    Sequence conflicti124 – 1241I → V in BAB23893. (PubMed:16141072)Curated
    Sequence conflicti135 – 1351K → S in BAB23893. (PubMed:16141072)Curated
    Sequence conflicti182 – 1821T → N1 PublicationCurated
    Sequence conflicti182 – 1821T → N(PubMed:9714804)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51679 mRNA. Translation: AAB01941.1.
    X82067 mRNA. Translation: CAA57566.1.
    U20611 mRNA. Translation: AAA69475.1.
    AF032722
    , AF032718, AF032719, AF032720, AF032721 Genomic DNA. Translation: AAC35744.1.
    AK005225 mRNA. Translation: BAB23893.1.
    AK008433 mRNA. Translation: BAB25666.1.
    AK010653 mRNA. Translation: BAB27093.1.
    AK088280 mRNA. Translation: BAC40255.1.
    BC002034 mRNA. Translation: AAH02034.1.
    BC081454 mRNA. Translation: AAH81454.1.
    CCDSiCCDS40416.1.
    RefSeqiNP_035693.3. NM_011563.5.
    XP_006530898.1. XM_006530835.1.
    UniGeneiMm.347009.
    Mm.393373.

    Genome annotation databases

    EnsembliENSMUST00000005292; ENSMUSP00000005292; ENSMUSG00000005161.
    ENSMUST00000109733; ENSMUSP00000105355; ENSMUSG00000005161.
    ENSMUST00000109734; ENSMUSP00000105356; ENSMUSG00000005161.
    ENSMUST00000164807; ENSMUSP00000126451; ENSMUSG00000005161.
    GeneIDi21672.
    KEGGimmu:21672.
    UCSCiuc009mom.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51679 mRNA. Translation: AAB01941.1 .
    X82067 mRNA. Translation: CAA57566.1 .
    U20611 mRNA. Translation: AAA69475.1 .
    AF032722
    , AF032718 , AF032719 , AF032720 , AF032721 Genomic DNA. Translation: AAC35744.1 .
    AK005225 mRNA. Translation: BAB23893.1 .
    AK008433 mRNA. Translation: BAB25666.1 .
    AK010653 mRNA. Translation: BAB27093.1 .
    AK088280 mRNA. Translation: BAC40255.1 .
    BC002034 mRNA. Translation: AAH02034.1 .
    BC081454 mRNA. Translation: AAH81454.1 .
    CCDSi CCDS40416.1.
    RefSeqi NP_035693.3. NM_011563.5.
    XP_006530898.1. XM_006530835.1.
    UniGenei Mm.347009.
    Mm.393373.

    3D structure databases

    ProteinModelPortali Q61171.
    SMRi Q61171. Positions 3-198.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204094. 2 interactions.
    IntActi Q61171. 13 interactions.
    MINTi MINT-1862390.

    Protein family/group databases

    PeroxiBasei 4474. Mm2CysPrx02.

    PTM databases

    PhosphoSitei Q61171.

    2D gel databases

    REPRODUCTION-2DPAGE Q61171.
    SWISS-2DPAGE Q61171.
    UCD-2DPAGE Q61171.

    Proteomic databases

    MaxQBi Q61171.
    PaxDbi Q61171.
    PRIDEi Q61171.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000005292 ; ENSMUSP00000005292 ; ENSMUSG00000005161 .
    ENSMUST00000109733 ; ENSMUSP00000105355 ; ENSMUSG00000005161 .
    ENSMUST00000109734 ; ENSMUSP00000105356 ; ENSMUSG00000005161 .
    ENSMUST00000164807 ; ENSMUSP00000126451 ; ENSMUSG00000005161 .
    GeneIDi 21672.
    KEGGi mmu:21672.
    UCSCi uc009mom.1. mouse.

    Organism-specific databases

    CTDi 7001.
    MGIi MGI:109486. Prdx2.

    Phylogenomic databases

    eggNOGi COG0450.
    GeneTreei ENSGT00390000004653.
    HOGENOMi HOG000022343.
    HOVERGENi HBG000286.
    InParanoidi Q61171.
    KOi K03386.
    OMAi EGVIQHA.
    OrthoDBi EOG7T1RCD.
    PhylomeDBi Q61171.
    TreeFami TF105181.

    Enzyme and pathway databases

    Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    ChiTaRSi PRDX2. mouse.
    NextBioi 300952.
    PROi Q61171.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61171.
    Bgeei Q61171.
    CleanExi MM_PRDX2.
    Genevestigatori Q61171.

    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. "Murine thioredoxin peroxidase delays neuronal apoptosis and is expressed in areas of the brain most susceptible to hypoxic and ischemic injury."
      Ichimiya S., Davis J.G., O'Rourke D.M., Katsumata M., Greene M.I.
      DNA Cell Biol. 16:311-321(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Brain.
    2. Oberbaeumer I.
      Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 129.
    3. Chae H.Z., Kim H., Rhee S.
      Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
    4. "The type II peroxiredoxin gene family of the mouse: molecular structure, expression and evolution."
      Lim M.J., Chae H.Z., Rhee S.G., Yu D.-Y., Lee K.-K., Yeom Y.I.
      Gene 216:197-205(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: 129/SvJ.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: NOD.
      Tissue: Cerebellum, Small intestine and Thymus.
    6. "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].
      Strain: C57BL/6J.
      Tissue: Brain and Mammary gland.
    7. Bienvenut W.V.
      Submitted (JUL-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-10 AND 120-135, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Liver.
    8. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 11-26; 92-109; 120-127 AND 140-150, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    9. "Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors."
      Gotter A.L., Suppa C., Emanuel B.S.
      J. Mol. Biol. 366:36-52(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIPIN.

    Entry informationi

    Entry nameiPRDX2_MOUSE
    AccessioniPrimary (citable) accession number: Q61171
    Secondary accession number(s): O88376
    , Q60796, Q9CWJ4, Q9DB49
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 147 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3