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Protein

Eosinophil peroxidase

Gene

Epx

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Protein has several cofactor binding sites:
  • Ca2+PROSITE-ProRule annotationNote: Binds 1 Ca2+ ion per heterodimer.PROSITE-ProRule annotation
  • heme bPROSITE-ProRule annotationNote: Binds 1 heme b (iron(II)-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
  7. response to oxidative stress Source: InterPro
Complete GO annotation...

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 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:107569. Epx.

Subcellular locationi

  1. Cytoplasmic granule

  2. Note: Cytoplasmic granules of eosinophils.

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
Complete GO annotation...

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

MaxQBiP49290.
PaxDbiP49290.
PRIDEiP49290.

PTM databases

PhosphoSiteiP49290.

Expressioni

Gene expression databases

BgeeiP49290.
CleanExiMM_EPX.
ExpressionAtlasiP49290. baseline and differential.
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.
InParanoidiP49290.
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

        10         20         30         40         50
MMQQLLALVG ALATLILTQH AEGTAPASPS PVEISVLRDC IAEAKLLVDT
60 70 80 90 100
AYNHTQKSIM QRLRSGSASP MDLLAYFKQP VAATRRVVQA ADYMHVALGL
110 120 130 140 150
LEERLQPRGS RPFNATDVLT EPQLRLLSQA SGCALQDQAE RCSNKYRTIT
160 170 180 190 200
GRCNNKKHPW LGASNQALAR WLPAEYEDHR SLPFGWTPGK RRNGFLLPLV
210 220 230 240 250
RDVSNQIVRF PSKKLTSDRG RALMFMQWGQ FIDHDLDFSP ESPARVAFSM
260 270 280 290 300
GVDCEKTCAQ LPPCFPIKIP RNDPRIKNQR DCIPFFRSAP ACPQNRNKVR
310 320 330 340 350
NQINALTSFV DASMVYGSEV TLALRLRNRT NFLGLLATNQ RFQDNGRALL
360 370 380 390 400
PFDNLHEDPC LLTNRSARIP CFLAGDTRSS ETPKLTALHT LFVREHNRLA
410 420 430 440 450
AELRRLNPHW SGDKLYNEAR KIVGAMVQII TYRDFLPLVL GRARIRRTLG
460 470 480 490 500
PYRGYCSNVD PRVANVFTLA FRFGHTMLQP FMFRLDSQYR ASAPNSHVPL
510 520 530 540 550
SSVFFASWRI IHEGGIDPIL RGLMATPAKL NRQDSMLVDE LRDKLFQQVR
560 570 580 590 600
RIGLDLAALN MQRSRDHGLP GYNAWRRFCG LSQPRNLAQL SRVLKNQDLA
610 620 630 640 650
RKFLRLYKTP DNIDIWVGAI AEPLLPGARV GPLLACLFEN QFRRARDGDR
660 670 680 690 700
FWWQKWGVFT KRQRKALRRI SLSRIVCDNT GITTVSRDIF RANIYPQGFV
710
SCSRIPKLNL SAWRGK
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. Curated

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 (Ref. 1) Curated
Sequence conflicti531 – 5311N → Y in BAA11370 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein family/group databases

PeroxiBasei3346. MmEPO.

PTM databases

PhosphoSiteiP49290.

Proteomic databases

MaxQBiP49290.
PaxDbiP49290.
PRIDEiP49290.

Protocols and materials databases

DNASUi13861.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8288.
MGIiMGI:107569. Epx.

Phylogenomic databases

eggNOGiNOG262194.
GeneTreeiENSGT00550000074325.
HOGENOMiHOG000016084.
HOVERGENiHBG000071.
InParanoidiP49290.
KOiK10788.
OMAiMHVALGL.
OrthoDBiEOG7M0NQW.
TreeFamiTF314316.

Miscellaneous databases

NextBioi284746.
PROiP49290.
SOURCEiSearch...

Gene expression databases

BgeeiP49290.
CleanExiMM_EPX.
ExpressionAtlasiP49290. baseline and differential.
GenevestigatoriP49290.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: March 4, 2015
This is version 124 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.