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P49290

- PERE_MOUSE

UniProt

P49290 - PERE_MOUSE

Protein

Eosinophil peroxidase

Gene

Epx

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils.By similarity

    Catalytic activityi

    2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.

    Cofactori

    Binds 1 calcium ion per heterodimer.PROSITE-ProRule annotation
    Binds 1 heme B (iron-protoporphyrin IX) group covalently per heterodimer.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei233 – 2331Heme (covalent; via 2 links)By similarity
    Active sitei234 – 2341Proton acceptorPROSITE-ProRule annotation
    Metal bindingi235 – 2351CalciumPROSITE-ProRule annotation
    Metal bindingi307 – 3071CalciumPROSITE-ProRule annotation
    Metal bindingi309 – 3091Calcium; via carbonyl oxygenPROSITE-ProRule annotation
    Metal bindingi311 – 3111CalciumPROSITE-ProRule annotation
    Metal bindingi313 – 3131CalciumPROSITE-ProRule annotation
    Sitei378 – 3781Transition state stabilizerPROSITE-ProRule annotation
    Binding sitei381 – 3811Heme (covalent; via 2 links)By similarity
    Metal bindingi475 – 4751Iron (heme axial ligand)PROSITE-ProRule annotation

    GO - Molecular functioni

    1. heme binding Source: InterPro
    2. metal ion binding Source: UniProtKB-KW
    3. peroxidase activity Source: MGI

    GO - Biological processi

    1. defense response to nematode Source: MGI
    2. eosinophil migration Source: MGI
    3. hydrogen peroxide catabolic process Source: UniProtKB-KW
    4. negative regulation of interleukin-10 production Source: MGI
    5. negative regulation of interleukin-5 production Source: MGI
    6. positive regulation of interleukin-4 production Source: MGI

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Calcium, Heme, Iron, Metal-binding

    Protein family/group databases

    PeroxiBasei3346. MmEPO.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eosinophil peroxidase (EC:1.11.1.7)
    Short name:
    EPO
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Epx
    Synonyms:Eper
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:107569. Epx.

    Subcellular locationi

    Cytoplasmic granule
    Note: Cytoplasmic granules of eosinophils.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Propeptidei19 – 140122Sequence AnalysisPRO_0000023642Add
    BLAST
    Chaini141 – 251111Eosinophil peroxidase light chainPRO_0000023643Add
    BLAST
    Chaini252 – 716465Eosinophil peroxidase heavy chainPRO_0000023644Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi142 ↔ 153PROSITE-ProRule annotation
    Disulfide bondi254 ↔ 264PROSITE-ProRule annotation
    Disulfide bondi258 ↔ 282PROSITE-ProRule annotation
    Glycosylationi328 – 3281N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi360 ↔ 371PROSITE-ProRule annotation
    Glycosylationi364 – 3641N-linked (GlcNAc...)Sequence Analysis
    Modified residuei489 – 4891Nitrated tyrosineBy similarity
    Disulfide bondi579 ↔ 636PROSITE-ProRule annotation
    Disulfide bondi677 ↔ 702PROSITE-ProRule annotation
    Glycosylationi709 – 7091N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Nitration

    Proteomic databases

    PaxDbiP49290.
    PRIDEiP49290.

    PTM databases

    PhosphoSiteiP49290.

    Expressioni

    Gene expression databases

    BgeeiP49290.
    CleanExiMM_EPX.
    GenevestigatoriP49290.

    Interactioni

    Subunit structurei

    Tetramer of two light chains and two heavy chains.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP49290.
    SMRiP49290. Positions 144-716.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peroxidase family. XPO subfamily.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG262194.
    GeneTreeiENSGT00550000074325.
    HOGENOMiHOG000016084.
    HOVERGENiHBG000071.
    InParanoidiQ5SW51.
    KOiK10788.
    OMAiMHVALGL.
    OrthoDBiEOG7M0NQW.
    TreeFamiTF314316.

    Family and domain databases

    Gene3Di1.10.640.10. 1 hit.
    InterProiIPR029599. EPX/EPO.
    IPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    [Graphical view]
    PANTHERiPTHR11475:SF49. PTHR11475:SF49. 1 hit.
    PfamiPF03098. An_peroxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00457. ANPEROXIDASE.
    SUPFAMiSSF48113. SSF48113. 1 hit.
    PROSITEiPS00435. PEROXIDASE_1. 1 hit.
    PS50292. PEROXIDASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P49290-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMQQLLALVG ALATLILTQH AEGTAPASPS PVEISVLRDC IAEAKLLVDT    50
    AYNHTQKSIM QRLRSGSASP MDLLAYFKQP VAATRRVVQA ADYMHVALGL 100
    LEERLQPRGS RPFNATDVLT EPQLRLLSQA SGCALQDQAE RCSNKYRTIT 150
    GRCNNKKHPW LGASNQALAR WLPAEYEDHR SLPFGWTPGK RRNGFLLPLV 200
    RDVSNQIVRF PSKKLTSDRG RALMFMQWGQ FIDHDLDFSP ESPARVAFSM 250
    GVDCEKTCAQ LPPCFPIKIP RNDPRIKNQR DCIPFFRSAP ACPQNRNKVR 300
    NQINALTSFV DASMVYGSEV TLALRLRNRT NFLGLLATNQ RFQDNGRALL 350
    PFDNLHEDPC LLTNRSARIP CFLAGDTRSS ETPKLTALHT LFVREHNRLA 400
    AELRRLNPHW SGDKLYNEAR KIVGAMVQII TYRDFLPLVL GRARIRRTLG 450
    PYRGYCSNVD PRVANVFTLA FRFGHTMLQP FMFRLDSQYR ASAPNSHVPL 500
    SSVFFASWRI IHEGGIDPIL RGLMATPAKL NRQDSMLVDE LRDKLFQQVR 550
    RIGLDLAALN MQRSRDHGLP GYNAWRRFCG LSQPRNLAQL SRVLKNQDLA 600
    RKFLRLYKTP DNIDIWVGAI AEPLLPGARV GPLLACLFEN QFRRARDGDR 650
    FWWQKWGVFT KRQRKALRRI SLSRIVCDNT GITTVSRDIF RANIYPQGFV 700
    SCSRIPKLNL SAWRGK 716
    Length:716
    Mass (Da):81,380
    Last modified:July 27, 2011 - v2
    Checksum:i9D1D1A88E6E259A1
    GO

    Sequence cautioni

    The sequence AAB40403.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti167 – 1671A → P in AAB40403. (PubMed:8773591)Curated
    Sequence conflicti400 – 4001A → P in AAB40403. (PubMed:8773591)Curated
    Sequence conflicti524 – 5241M → K in BAA11370. 1 PublicationCurated
    Sequence conflicti531 – 5311N → Y in BAA11370. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78353 mRNA. Translation: BAA11370.1.
    L77979 mRNA. Translation: AAB40403.1. Different initiation.
    AL606805 Genomic DNA. Translation: CAI25724.1.
    CCDSiCCDS25220.1.
    RefSeqiNP_031972.2. NM_007946.2.
    UniGeneiMm.1315.

    Genome annotation databases

    EnsembliENSMUST00000049768; ENSMUSP00000050497; ENSMUSG00000052234.
    GeneIDi13861.
    KEGGimmu:13861.
    UCSCiuc007kuw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78353 mRNA. Translation: BAA11370.1 .
    L77979 mRNA. Translation: AAB40403.1 . Different initiation.
    AL606805 Genomic DNA. Translation: CAI25724.1 .
    CCDSi CCDS25220.1.
    RefSeqi NP_031972.2. NM_007946.2.
    UniGenei Mm.1315.

    3D structure databases

    ProteinModelPortali P49290.
    SMRi P49290. Positions 144-716.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    PeroxiBasei 3346. MmEPO.

    PTM databases

    PhosphoSitei P49290.

    Proteomic databases

    PaxDbi P49290.
    PRIDEi P49290.

    Protocols and materials databases

    DNASUi 13861.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000049768 ; ENSMUSP00000050497 ; ENSMUSG00000052234 .
    GeneIDi 13861.
    KEGGi mmu:13861.
    UCSCi uc007kuw.1. mouse.

    Organism-specific databases

    CTDi 8288.
    MGIi MGI:107569. Epx.

    Phylogenomic databases

    eggNOGi NOG262194.
    GeneTreei ENSGT00550000074325.
    HOGENOMi HOG000016084.
    HOVERGENi HBG000071.
    InParanoidi Q5SW51.
    KOi K10788.
    OMAi MHVALGL.
    OrthoDBi EOG7M0NQW.
    TreeFami TF314316.

    Miscellaneous databases

    NextBioi 284746.
    PROi P49290.
    SOURCEi Search...

    Gene expression databases

    Bgeei P49290.
    CleanExi MM_EPX.
    Genevestigatori P49290.

    Family and domain databases

    Gene3Di 1.10.640.10. 1 hit.
    InterProi IPR029599. EPX/EPO.
    IPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    [Graphical view ]
    PANTHERi PTHR11475:SF49. PTHR11475:SF49. 1 hit.
    Pfami PF03098. An_peroxidase. 1 hit.
    [Graphical view ]
    PRINTSi PR00457. ANPEROXIDASE.
    SUPFAMi SSF48113. SSF48113. 1 hit.
    PROSITEi PS00435. PEROXIDASE_1. 1 hit.
    PS50292. PEROXIDASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Ohmori J., Itoh H., Tomita M., Nawa Y.
      Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
    2. "Cloning of the murine eosinophil peroxidase gene (mEPO): characterization of a conserved subgroup of mammalian hematopoietic peroxidases."
      Horton M.A., Larson K.A., Lee J.J., Lee N.A.
      J. Leukoc. Biol. 60:285-294(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Cited for: FUNCTION, NITRATION.

    Entry informationi

    Entry nameiPERE_MOUSE
    AccessioniPrimary (citable) accession number: P49290
    Secondary accession number(s): Q5SW51, Q61798
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 119 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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