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P11678

- PERE_HUMAN

UniProt

P11678 - PERE_HUMAN

Protein

Eosinophil peroxidase

Gene

EPX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils. Shows significant inhibitory activity towards Mycobacterium tuberculosis H37Rv by inducing bacterial fragmentation and lysis.2 Publications

    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) covalently through ester linkages to hydroxylated methyl groups formed auto-catalytically with hydrogen peroxide at the heme C-1 and C-5 positions. The ester linkage to Asp-232 was observed in 30% of the chains.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei232 – 2321Heme (covalent; via 2 links); partial
    Active sitei233 – 2331Proton acceptorPROSITE-ProRule annotation
    Metal bindingi234 – 2341CalciumPROSITE-ProRule annotation
    Metal bindingi306 – 3061CalciumPROSITE-ProRule annotation
    Metal bindingi308 – 3081Calcium; via carbonyl oxygenPROSITE-ProRule annotation
    Metal bindingi310 – 3101CalciumPROSITE-ProRule annotation
    Metal bindingi312 – 3121CalciumPROSITE-ProRule annotation
    Sitei377 – 3771Transition state stabilizerPROSITE-ProRule annotation
    Binding sitei380 – 3801Heme (covalent; via 2 links)
    Metal bindingi474 – 4741Iron (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: ProtInc

    GO - Biological processi

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

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Calcium, Heme, Iron, Metal-binding

    Protein family/group databases

    PeroxiBasei3317. HsEPO.

    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, EPO, EPP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:3423. EPX.

    Subcellular locationi

    Cytoplasmic granule
    Note: Cytoplasmic granules of eosinophils.

    Pathology & Biotechi

    Involvement in diseasei

    Eosinophil peroxidase deficiency (EPXD) [MIM:261500]: A rare abnormality without clinical symptoms characterized by decreased or absent peroxidase activity and decreased volume of the granule matrix in eosinophils.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti286 – 2861R → H in EPXD. 1 Publication
    Corresponds to variant rs121434566 [ dbSNP | Ensembl ].
    VAR_015376

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi261500. phenotype.
    PharmGKBiPA27841.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Propeptidei18 – 1391221 PublicationPRO_0000023639Add
    BLAST
    Chaini140 – 250111Eosinophil peroxidase light chainPRO_0000023640Add
    BLAST
    Chaini251 – 715465Eosinophil peroxidase heavy chainPRO_0000023641Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi52 – 521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi141 ↔ 152PROSITE-ProRule annotation
    Disulfide bondi253 ↔ 263PROSITE-ProRule annotation
    Disulfide bondi257 ↔ 281PROSITE-ProRule annotation
    Glycosylationi327 – 3271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi359 ↔ 370PROSITE-ProRule annotation
    Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis
    Modified residuei488 – 4881Nitrated tyrosine1 Publication
    Disulfide bondi578 ↔ 635PROSITE-ProRule annotation
    Disulfide bondi676 ↔ 701PROSITE-ProRule annotation
    Glycosylationi700 – 7001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi708 – 7081N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Nitration

    Proteomic databases

    PaxDbiP11678.
    PRIDEiP11678.

    PTM databases

    PhosphoSiteiP11678.

    Expressioni

    Gene expression databases

    BgeeiP11678.
    CleanExiHS_EPO.
    HS_EPX.
    GenevestigatoriP11678.

    Organism-specific databases

    HPAiHPA050507.

    Interactioni

    Subunit structurei

    Tetramer of two light chains and two heavy chains.

    Protein-protein interaction databases

    IntActiP11678. 3 interactions.
    STRINGi9606.ENSP00000225371.

    Structurei

    3D structure databases

    ProteinModelPortaliP11678.
    SMRiP11678. Positions 143-713.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG262194.
    HOGENOMiHOG000016084.
    HOVERGENiHBG000071.
    InParanoidiP11678.
    KOiK10788.
    OMAiMHVALGL.
    OrthoDBiEOG7M0NQW.
    PhylomeDBiP11678.
    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.

    P11678-1 [UniParc]FASTAAdd to Basket

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    MHLLPALAGV LATLVLAQPC EGTDPASPGA VETSVLRDCI AEAKLLVDAA    50
    YNWTQKSIKQ RLRSGSASPM DLLSYFKQPV AATRTVVRAA DYMHVALGLL 100
    EEKLQPQRSG PFNVTDVLTE PQLRLLSQAS GCALRDQAER CSDKYRTITG 150
    RCNNKRRPLL GASNQALARW LPAEYEDGLS LPFGWTPSRR RNGFLLPLVR 200
    AVSNQIVRFP NERLTSDRGR ALMFMQWGQF IDHDLDFSPE SPARVAFTAG 250
    VDCERTCAQL PPCFPIKIPP NDPRIKNQRD CIPFFRSAPS CPQNKNRVRN 300
    QINALTSFVD ASMVYGSEVS LSLRLRNRTN YLGLLAINQR FQDNGRALLP 350
    FDNLHDDPCL LTNRSARIPC FLAGDTRSTE TPKLAAMHTL FMREHNRLAT 400
    ELRRLNPRWN GDKLYNEARK IMGAMVQIIT YRDFLPLVLG KARARRTLGH 450
    YRGYCSNVDP RVANVFTLAF RFGHTMLQPF MFRLDSQYRA SAPNSHVPLS 500
    SAFFASWRIV YEGGIDPILR GLMATPAKLN RQDAMLVDEL RDRLFRQVRR 550
    IGLDLAALNM QRSRDHGLPG YNAWRRFCGL SQPRNLAQLS RVLKNQDLAR 600
    KFLNLYGTPD NIDIWIGAIA EPLLPGARVG PLLACLFENQ FRRARDGDRF 650
    WWQKRGVFTK RQRKALSRIS LSRIICDNTG ITTVSRDIFR ANIYPRGFVN 700
    CSRIPRLNLS AWRGT 715
    Length:715
    Mass (Da):81,040
    Last modified:February 1, 1996 - v2
    Checksum:iCEB4E689A6C46374
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 186TLVLAQ → EFRGQD AA sequence (PubMed:2541222)Curated
    Sequence conflicti21 – 211E → Q AA sequence (PubMed:2541222)Curated
    Sequence conflicti113 – 1131N → I in CAA32530. (PubMed:2541222)Curated
    Sequence conflicti163 – 1631S → C AA sequence (PubMed:2541222)Curated
    Sequence conflicti645 – 66016RDGDR…GVFTK → ETETGSGGRTRCFHQ AA sequence (PubMed:2541222)CuratedAdd
    BLAST

    Polymorphismi

    Allelic variant in EPX is associated with Japanese cedar pollinosis which is a type I allergic disease with ocular and nasal symptoms that develop paroxysmally on contact with Japanese cedar pollen. These symptoms, which occur seasonally each year, are typical features of allergic rhinitis, such as sneezing, excessive nasal secretion, nasal congestion, and conjunctival itching.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti35 – 351V → I.
    Corresponds to variant rs34553736 [ dbSNP | Ensembl ].
    VAR_050485
    Natural varianti40 – 401I → M.1 Publication
    Corresponds to variant rs11079339 [ dbSNP | Ensembl ].
    VAR_025138
    Natural varianti122 – 1221Q → H.1 Publication
    Corresponds to variant rs11652709 [ dbSNP | Ensembl ].
    VAR_025139
    Natural varianti249 – 2491A → E.1 Publication
    Corresponds to variant rs35896669 [ dbSNP | Ensembl ].
    VAR_025140
    Natural varianti276 – 2761K → R.1 Publication
    Corresponds to variant rs35074452 [ dbSNP | Ensembl ].
    VAR_025141
    Natural varianti286 – 2861R → H in EPXD. 1 Publication
    Corresponds to variant rs121434566 [ dbSNP | Ensembl ].
    VAR_015376
    Natural varianti292 – 2921P → L.1 Publication
    Corresponds to variant rs33971258 [ dbSNP | Ensembl ].
    VAR_025142
    Natural varianti326 – 3261R → H.1 Publication
    Corresponds to variant rs35832094 [ dbSNP | Ensembl ].
    VAR_060197
    Natural varianti326 – 3261R → L.1 Publication
    VAR_060198
    Natural varianti326 – 3261R → P.1 Publication
    Corresponds to variant rs35832094 [ dbSNP | Ensembl ].
    VAR_025143
    Natural varianti358 – 3581P → L Associated with Japanese cedar pollinosis. 2 Publications
    Corresponds to variant rs35135976 [ dbSNP | Ensembl ].
    VAR_025144
    Natural varianti364 – 3641R → H.1 Publication
    Corresponds to variant rs35232062 [ dbSNP | Ensembl ].
    VAR_025145
    Natural varianti441 – 4411K → T.1 Publication
    Corresponds to variant rs35750729 [ dbSNP | Ensembl ].
    VAR_025146
    Natural varianti458 – 4581V → M.
    Corresponds to variant rs34817773 [ dbSNP | Ensembl ].
    VAR_050486
    Natural varianti496 – 4961H → Q.1 Publication
    Corresponds to variant rs33955150 [ dbSNP | Ensembl ].
    VAR_025147
    Natural varianti572 – 5721N → Y.1 Publication
    Corresponds to variant rs2302311 [ dbSNP | Ensembl ].
    VAR_020031

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29913
    , M29904, M29905, M29906, M29907, M29908, M29909, M29910, M29911, M29912 Genomic DNA. Translation: AAA58458.1.
    DQ054598 Genomic DNA. Translation: AAY43126.1.
    X14346 mRNA. Translation: CAA32530.1.
    CCDSiCCDS11602.1.
    PIRiA34408.
    RefSeqiNP_000493.1. NM_000502.4.
    XP_006722191.1. XM_006722128.1.
    UniGeneiHs.279259.

    Genome annotation databases

    EnsembliENST00000225371; ENSP00000225371; ENSG00000121053.
    GeneIDi8288.
    KEGGihsa:8288.
    UCSCiuc002ivq.3. human.

    Polymorphism databases

    DMDMi1352738.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29913
    , M29904 , M29905 , M29906 , M29907 , M29908 , M29909 , M29910 , M29911 , M29912 Genomic DNA. Translation: AAA58458.1 .
    DQ054598 Genomic DNA. Translation: AAY43126.1 .
    X14346 mRNA. Translation: CAA32530.1 .
    CCDSi CCDS11602.1.
    PIRi A34408.
    RefSeqi NP_000493.1. NM_000502.4.
    XP_006722191.1. XM_006722128.1.
    UniGenei Hs.279259.

    3D structure databases

    ProteinModelPortali P11678.
    SMRi P11678. Positions 143-713.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P11678. 3 interactions.
    STRINGi 9606.ENSP00000225371.

    Chemistry

    ChEMBLi CHEMBL2438.

    Protein family/group databases

    PeroxiBasei 3317. HsEPO.

    PTM databases

    PhosphoSitei P11678.

    Polymorphism databases

    DMDMi 1352738.

    Proteomic databases

    PaxDbi P11678.
    PRIDEi P11678.

    Protocols and materials databases

    DNASUi 8288.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000225371 ; ENSP00000225371 ; ENSG00000121053 .
    GeneIDi 8288.
    KEGGi hsa:8288.
    UCSCi uc002ivq.3. human.

    Organism-specific databases

    CTDi 8288.
    GeneCardsi GC17P056270.
    H-InvDB HIX0202542.
    HGNCi HGNC:3423. EPX.
    HPAi HPA050507.
    MIMi 131399. gene.
    261500. phenotype.
    neXtProti NX_P11678.
    PharmGKBi PA27841.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG262194.
    HOGENOMi HOG000016084.
    HOVERGENi HBG000071.
    InParanoidi P11678.
    KOi K10788.
    OMAi MHVALGL.
    OrthoDBi EOG7M0NQW.
    PhylomeDBi P11678.
    TreeFami TF314316.

    Miscellaneous databases

    GeneWikii Eosinophil_peroxidase.
    GenomeRNAii 8288.
    NextBioi 31057.
    PROi P11678.
    SOURCEi Search...

    Gene expression databases

    Bgeei P11678.
    CleanExi HS_EPO.
    HS_EPX.
    Genevestigatori P11678.

    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. "Molecular cloning and characterization of a chromosomal gene for human eosinophil peroxidase."
      Sakamaki K., Tomonaga M., Tsukui K., Nagata S.
      J. Biol. Chem. 264:16828-16836(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    2. NIEHS SNPs program
      Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-40; HIS-122; GLU-249; ARG-276; LEU-292; PRO-326; LEU-358; HIS-364; THR-441; GLN-496 AND TYR-572.
    3. "Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family."
      Ten R.M., Pease L.R., McKean D.J., Bell M.P., Gleich G.J.
      J. Exp. Med. 169:1757-1769(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-715, PROTEIN SEQUENCE OF 140-187 AND 251-288.
      Tissue: Blood.
    4. "Biochemical evidence for heme linkage through esters with Asp-93 and Glu-241 in human eosinophil peroxidase. The ester with Asp-93 is only partially formed in vivo."
      Oxvig C., Thomsen A.R., Overgaard M.T., Sorensen E.S., Hoejrup P., Bjerrum M.J., Gleich G.J., Sottrup-Jensen L.
      J. Biol. Chem. 274:16953-16958(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: COVALENT HEME ATTACHMENT, PARTIAL PROTEIN SEQUENCE.
      Tissue: Blood.
    5. "Human eosinophil peroxidase induces surface alteration, killing, and lysis of Mycobacterium tuberculosis."
      Borelli V., Vita F., Shankar S., Soranzo M.R., Banfi E., Scialino G., Brochetta C., Zabucchi G.
      Infect. Immun. 71:605-613(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. Cited for: FUNCTION, NITRATION AT TYR-488.
    7. "Hereditary eosinophil peroxidase deficiency: immunochemical and spectroscopic studies and evidence for a compound heterozygosity of the defect."
      Romano M., Patriarca P., Melo C., Baralle F.E., Dri P.
      Proc. Natl. Acad. Sci. U.S.A. 91:12496-12500(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EPXD HIS-286.
    8. "High contribution contrast between the genes of eosinophil peroxidase and IL-4 receptor alpha-chain in Japanese cedar pollinosis."
      Nakamura H., Miyagawa K., Ogino K., Endo T., Imai T., Ozasa K., Motohashi Y., Matsuzaki I., Sasahara S., Hatta K., Eboshida A.
      J. Allergy Clin. Immunol. 112:1127-1131(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HIS-326; LEU-326 AND LEU-358, POLYMORPHISM.

    Entry informationi

    Entry nameiPERE_HUMAN
    AccessioniPrimary (citable) accession number: P11678
    Secondary accession number(s): Q4TVP3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3