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P35700

- PRDX1_MOUSE

UniProt

P35700 - PRDX1_MOUSE

Protein

Peroxiredoxin-1

Gene

Prdx1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      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 but not 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. Regulates GDPD5 function by reducing an intramolecular disulfide bond By similarity. Cooperates with GDPD5 to drive postmitotic motor neuron differentiation.By similarity1 Publication

    Catalytic activityi

    2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei52 – 521Cysteine sulfenic acid (-SOH) intermediateBy similarity

    GO - Molecular functioni

    1. heme binding Source: Ensembl
    2. identical protein binding Source: IntAct
    3. protein binding Source: IntAct
    4. thioredoxin peroxidase activity Source: Ensembl

    GO - Biological processi

    1. cell proliferation Source: MGI
    2. erythrocyte homeostasis Source: MGI
    3. hydrogen peroxide catabolic process Source: Ensembl
    4. natural killer cell mediated cytotoxicity Source: MGI
    5. regulation of NF-kappaB import into nucleus Source: MGI
    6. regulation of stress-activated MAPK cascade Source: MGI
    7. removal of superoxide radicals Source: MGI
    8. response to oxidative stress Source: MGI
    9. response to reactive oxygen species Source: MGI

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase, Peroxidase

    Enzyme and pathway databases

    ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.

    Protein family/group databases

    PeroxiBasei4555. Mm2CysPrx01-1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxiredoxin-1 (EC:1.11.1.15)
    Alternative name(s):
    Macrophage 23 kDa stress protein
    Osteoblast-specific factor 3
    Short name:
    OSF-3
    Thioredoxin peroxidase 2
    Thioredoxin-dependent peroxide reductase 2
    Gene namesi
    Name:Prdx1
    Synonyms:Msp23, Paga, Tdpx2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:99523. Prdx1.

    Subcellular locationi

    Cytoplasm. Melanosome By similarity

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. melanosome Source: UniProtKB-SubCell
    3. mitochondrial matrix Source: Ensembl
    4. mitochondrion Source: MGI
    5. nuclear euchromatin Source: Ensembl
    6. nucleolus Source: Ensembl
    7. peroxisomal matrix Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Mice embryos loss approximately 50% of Islet1/Islet2+ and HB9+ motor neurons, whereas dorsal-ventral patterning events and the numbers of Olig2+ progenitors are normal. Toward the end of the cell death phase they have equivalent numbers of motor neurons as wild type embryos.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 199198Peroxiredoxin-1PRO_0000135077Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei7 – 71N6-acetyllysineBy similarity
    Modified residuei16 – 161N6-acetyllysineBy similarity
    Modified residuei27 – 271N6-acetyllysineBy similarity
    Modified residuei35 – 351N6-acetyllysine; alternateBy similarity
    Modified residuei35 – 351N6-succinyllysine; alternate1 Publication
    Disulfide bondi52 – 52Interchain (with C-173); in linked formBy similarity
    Modified residuei90 – 901PhosphothreonineBy similarity
    Modified residuei136 – 1361N6-acetyllysine1 Publication
    Disulfide bondi173 – 173Interchain (with C-52); in linked formBy similarity

    Post-translational modificationi

    Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity.By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiP35700.
    PaxDbiP35700.
    PRIDEiP35700.

    2D gel databases

    REPRODUCTION-2DPAGEP35700.
    SWISS-2DPAGEP35700.

    PTM databases

    PhosphoSiteiP35700.

    Expressioni

    Tissue specificityi

    Found in various tissues; high concentration in liver.

    Inductioni

    By oxidative and sulfhydryl-reactive agents.

    Gene expression databases

    ArrayExpressiP35700.
    BgeeiP35700.
    CleanExiMM_PRDX1.
    GenevestigatoriP35700.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked, upon oxidation By similarity. May form heterodimers with AOP2. Interacts with GDPD5; forms a mixed-disulfide with GDPD5 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-444948,EBI-444948
    STK4Q130433EBI-444948,EBI-367376From a different organism.

    Protein-protein interaction databases

    BioGridi202018. 5 interactions.
    IntActiP35700. 18 interactions.
    MINTiMINT-1863043.

    Structurei

    3D structure databases

    ProteinModelPortaliP35700.
    SMRiP35700. Positions 3-199.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 165160ThioredoxinPROSITE-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.
    InParanoidiP35700.
    KOiK13279.
    OMAiFKKINCE.
    OrthoDBiEOG7T1RCD.
    PhylomeDBiP35700.
    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.

    P35700-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSGNAKIGY PAPNFKATAV MPDGQFKDIS LSEYKGKYVV FFFYPLDFTF    50
    VCPTEIIAFS DRADEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM 100
    NIPLISDPKR TIAQDYGVLK ADEGISFRGL FIIDDKGILR QITINDLPVG 150
    RSVDEIIRLV QAFQFTDKHG EVCPAGWKPG SDTIKPDVNK SKEYFSKQK 199
    Length:199
    Mass (Da):22,176
    Last modified:June 1, 1994 - v1
    Checksum:iBEF5C995A86124D1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti196 – 1961S → F in BAB27120. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16142 mRNA. Translation: BAA03713.1.
    D21252 mRNA. Translation: BAA04796.1.
    AF157331, AF157329, AF157330 Genomic DNA. Translation: AAD45323.1.
    AB023564 Genomic DNA. Translation: BAA86992.1.
    AK002287 mRNA. Translation: BAB21990.1.
    AK008711 mRNA. Translation: BAB25847.1.
    AK010688 mRNA. Translation: BAB27120.1.
    AK083243 mRNA. Translation: BAC38827.1.
    AK145138 mRNA. Translation: BAE26255.1.
    AK150797 mRNA. Translation: BAE29860.1.
    AK151459 mRNA. Translation: BAE30417.1.
    AK167624 mRNA. Translation: BAE39676.1.
    AK169154 mRNA. Translation: BAE40933.1.
    BC083348 mRNA. Translation: AAH83348.1.
    BC086648 mRNA. Translation: AAH86648.1.
    CCDSiCCDS18515.1.
    PIRiA48513.
    RefSeqiNP_035164.1. NM_011034.4.
    UniGeneiMm.30929.

    Genome annotation databases

    EnsembliENSMUST00000106470; ENSMUSP00000102078; ENSMUSG00000028691.
    ENSMUST00000135573; ENSMUSP00000114159; ENSMUSG00000028691.
    GeneIDi18477.
    KEGGimmu:18477.
    UCSCiuc008uhd.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16142 mRNA. Translation: BAA03713.1 .
    D21252 mRNA. Translation: BAA04796.1 .
    AF157331 , AF157329 , AF157330 Genomic DNA. Translation: AAD45323.1 .
    AB023564 Genomic DNA. Translation: BAA86992.1 .
    AK002287 mRNA. Translation: BAB21990.1 .
    AK008711 mRNA. Translation: BAB25847.1 .
    AK010688 mRNA. Translation: BAB27120.1 .
    AK083243 mRNA. Translation: BAC38827.1 .
    AK145138 mRNA. Translation: BAE26255.1 .
    AK150797 mRNA. Translation: BAE29860.1 .
    AK151459 mRNA. Translation: BAE30417.1 .
    AK167624 mRNA. Translation: BAE39676.1 .
    AK169154 mRNA. Translation: BAE40933.1 .
    BC083348 mRNA. Translation: AAH83348.1 .
    BC086648 mRNA. Translation: AAH86648.1 .
    CCDSi CCDS18515.1.
    PIRi A48513.
    RefSeqi NP_035164.1. NM_011034.4.
    UniGenei Mm.30929.

    3D structure databases

    ProteinModelPortali P35700.
    SMRi P35700. Positions 3-199.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202018. 5 interactions.
    IntActi P35700. 18 interactions.
    MINTi MINT-1863043.

    Protein family/group databases

    PeroxiBasei 4555. Mm2CysPrx01-1.

    PTM databases

    PhosphoSitei P35700.

    2D gel databases

    REPRODUCTION-2DPAGE P35700.
    SWISS-2DPAGE P35700.

    Proteomic databases

    MaxQBi P35700.
    PaxDbi P35700.
    PRIDEi P35700.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000106470 ; ENSMUSP00000102078 ; ENSMUSG00000028691 .
    ENSMUST00000135573 ; ENSMUSP00000114159 ; ENSMUSG00000028691 .
    GeneIDi 18477.
    KEGGi mmu:18477.
    UCSCi uc008uhd.1. mouse.

    Organism-specific databases

    CTDi 5052.
    MGIi MGI:99523. Prdx1.

    Phylogenomic databases

    eggNOGi COG0450.
    GeneTreei ENSGT00390000004653.
    HOGENOMi HOG000022343.
    HOVERGENi HBG000286.
    InParanoidi P35700.
    KOi K13279.
    OMAi FKKINCE.
    OrthoDBi EOG7T1RCD.
    PhylomeDBi P35700.
    TreeFami TF105181.

    Enzyme and pathway databases

    Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    NextBioi 294178.
    PROi P35700.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35700.
    Bgeei P35700.
    CleanExi MM_PRDX1.
    Genevestigatori P35700.

    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 characterization of a 23-kDa stress-induced mouse peritoneal macrophage protein."
      Ishii T., Yamada M., Sato H., Matsue M., Taketani S., Nakayama K., Sugita Y., Bannai S.
      J. Biol. Chem. 268:18633-18636(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Peritoneal macrophage.
    2. "Cloning and characterization of OSF-3, a new member of the MER5 family, expressed in mouse osteoblastic cells."
      Kawai S., Takeshita S., Okazaki M., Kikuno R., Kudo A., Amann E.
      J. Biochem. 115:641-643(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Osteoblast.
    3. "Characterization of mouse peroxiredoxin I genomic DNA and its expression."
      Lee T.-H., Yu S.-L., Kim S.-U., Lee K.-K., Rhee S.G., Yu D.-Y.
      Gene 239:243-250(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: 129/SvJ.
    4. "Characterization of mouse type I peroxiredoxin gene and pseudogenes."
      Hino K., Sato H., Bannai S.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/SvJ.
      Tissue: Liver.
    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: C57BL/6J.
      Tissue: Bone marrow, Hippocampus, Kidney, Liver, Mammary gland and Stomach.
    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/6.
      Tissue: Brain.
    7. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 17-27; 94-109; 111-120; 141-151; 159-168 AND 173-190, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    8. "The antioxidant enzyme Prdx1 controls neuronal differentiation by thiol-redox-dependent activation of GDE2."
      Yan Y., Sabharwal P., Rao M., Sockanathan S.
      Cell 138:1209-1221(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-136, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.

    Entry informationi

    Entry nameiPRDX1_MOUSE
    AccessioniPrimary (citable) accession number: P35700
    Secondary accession number(s): Q3UBV4, Q9CWI2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 149 of the entry and version 1 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-52 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-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-52 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