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Protein

Eosinophil peroxidase

Gene

EPX

Organism
Homo sapiens (Human)
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. 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

Protein has several cofactor binding sites:
  • Ca2+PROSITE-ProRule annotationNote: Binds 1 Ca2+ ion per heterodimer.PROSITE-ProRule annotation
  • heme bNote: Binds 1 heme b (iron(II)-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)DescriptionActionsGraphical viewLength
Binding sitei232Heme (covalent; via 2 links); partial1
Active sitei233Proton acceptorPROSITE-ProRule annotation1
Metal bindingi234CalciumPROSITE-ProRule annotation1
Metal bindingi306CalciumPROSITE-ProRule annotation1
Metal bindingi308Calcium; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi310CalciumPROSITE-ProRule annotation1
Metal bindingi312CalciumPROSITE-ProRule annotation1
Sitei377Transition state stabilizerPROSITE-ProRule annotation1
Binding sitei380Heme (covalent; via 2 links)1
Metal bindingi474Iron (heme axial ligand)PROSITE-ProRule annotation1

GO - Molecular functioni

  • heme binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • peroxidase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS04462-MONOMER.
ReactomeiR-HSA-6798695. Neutrophil degranulation.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:3423. EPX.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular space Source: GO_Central
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Eosinophil peroxidase deficiency (EPXD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare abnormality without clinical symptoms characterized by decreased or absent peroxidase activity and decreased volume of the granule matrix in eosinophils.
See also OMIM:261500
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015376286R → H in EPXD. 1 PublicationCorresponds to variant rs121434566dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi8288.
MalaCardsiEPX.
MIMi261500. phenotype.
OpenTargetsiENSG00000121053.
PharmGKBiPA27841.

Chemistry databases

ChEMBLiCHEMBL2438.
DrugBankiDB01065. Melatonin.

Polymorphism and mutation databases

BioMutaiEPX.
DMDMi1352738.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
PropeptideiPRO_000002363918 – 1391 PublicationAdd BLAST122
ChainiPRO_0000023640140 – 250Eosinophil peroxidase light chainAdd BLAST111
ChainiPRO_0000023641251 – 715Eosinophil peroxidase heavy chainAdd BLAST465

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi52N-linked (GlcNAc...)Sequence analysis1
Glycosylationi113N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi141 ↔ 152PROSITE-ProRule annotation
Disulfide bondi253 ↔ 263PROSITE-ProRule annotation
Disulfide bondi257 ↔ 281PROSITE-ProRule annotation
Glycosylationi327N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi359 ↔ 370PROSITE-ProRule annotation
Glycosylationi363N-linked (GlcNAc...)Sequence analysis1
Modified residuei488Nitrated tyrosine1 Publication1
Disulfide bondi578 ↔ 635PROSITE-ProRule annotation
Disulfide bondi676 ↔ 701PROSITE-ProRule annotation
Glycosylationi700N-linked (GlcNAc...)Sequence analysis1
Glycosylationi708N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration

Proteomic databases

EPDiP11678.
PaxDbiP11678.
PeptideAtlasiP11678.
PRIDEiP11678.
TopDownProteomicsiP11678.

PTM databases

iPTMnetiP11678.
PhosphoSitePlusiP11678.

Expressioni

Gene expression databases

BgeeiENSG00000121053.
CleanExiHS_EPO.
HS_EPX.
GenevisibleiP11678. HS.

Organism-specific databases

HPAiHPA050507.

Interactioni

Subunit structurei

Tetramer of two light chains and two heavy chains.

Protein-protein interaction databases

BioGridi113893. 2 interactors.
IntActiP11678. 3 interactors.
STRINGi9606.ENSP00000225371.

Structurei

3D structure databases

ProteinModelPortaliP11678.
SMRiP11678.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2408. Eukaryota.
ENOG410XPZ3. LUCA.
GeneTreeiENSGT00550000074325.
HOGENOMiHOG000016084.
HOVERGENiHBG000071.
InParanoidiP11678.
KOiK10788.
OMAiMHVALGL.
OrthoDBiEOG091G02JC.
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:SF63. PTHR11475:SF63. 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

« Hide

        10         20         30         40         50
MHLLPALAGV LATLVLAQPC EGTDPASPGA VETSVLRDCI AEAKLLVDAA
60 70 80 90 100
YNWTQKSIKQ RLRSGSASPM DLLSYFKQPV AATRTVVRAA DYMHVALGLL
110 120 130 140 150
EEKLQPQRSG PFNVTDVLTE PQLRLLSQAS GCALRDQAER CSDKYRTITG
160 170 180 190 200
RCNNKRRPLL GASNQALARW LPAEYEDGLS LPFGWTPSRR RNGFLLPLVR
210 220 230 240 250
AVSNQIVRFP NERLTSDRGR ALMFMQWGQF IDHDLDFSPE SPARVAFTAG
260 270 280 290 300
VDCERTCAQL PPCFPIKIPP NDPRIKNQRD CIPFFRSAPS CPQNKNRVRN
310 320 330 340 350
QINALTSFVD ASMVYGSEVS LSLRLRNRTN YLGLLAINQR FQDNGRALLP
360 370 380 390 400
FDNLHDDPCL LTNRSARIPC FLAGDTRSTE TPKLAAMHTL FMREHNRLAT
410 420 430 440 450
ELRRLNPRWN GDKLYNEARK IMGAMVQIIT YRDFLPLVLG KARARRTLGH
460 470 480 490 500
YRGYCSNVDP RVANVFTLAF RFGHTMLQPF MFRLDSQYRA SAPNSHVPLS
510 520 530 540 550
SAFFASWRIV YEGGIDPILR GLMATPAKLN RQDAMLVDEL RDRLFRQVRR
560 570 580 590 600
IGLDLAALNM QRSRDHGLPG YNAWRRFCGL SQPRNLAQLS RVLKNQDLAR
610 620 630 640 650
KFLNLYGTPD NIDIWIGAIA EPLLPGARVG PLLACLFENQ FRRARDGDRF
660 670 680 690 700
WWQKRGVFTK RQRKALSRIS LSRIICDNTG ITTVSRDIFR ANIYPRGFVN
710
CSRIPRLNLS AWRGT
Length:715
Mass (Da):81,040
Last modified:February 1, 1996 - v2
Checksum:iCEB4E689A6C46374
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti13 – 18TLVLAQ → EFRGQD AA sequence (PubMed:2541222).Curated6
Sequence conflicti21E → Q AA sequence (PubMed:2541222).Curated1
Sequence conflicti113N → I in CAA32530 (PubMed:2541222).Curated1
Sequence conflicti163S → C AA sequence (PubMed:2541222).Curated1
Sequence conflicti645 – 660RDGDR…GVFTK → ETETGSGGRTRCFHQ AA sequence (PubMed:2541222).CuratedAdd BLAST16

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_05048535V → I.Corresponds to variant rs34553736dbSNPEnsembl.1
Natural variantiVAR_02513840I → M.1 PublicationCorresponds to variant rs11079339dbSNPEnsembl.1
Natural variantiVAR_025139122Q → H.1 PublicationCorresponds to variant rs11652709dbSNPEnsembl.1
Natural variantiVAR_025140249A → E.1 PublicationCorresponds to variant rs35896669dbSNPEnsembl.1
Natural variantiVAR_025141276K → R.1 PublicationCorresponds to variant rs35074452dbSNPEnsembl.1
Natural variantiVAR_015376286R → H in EPXD. 1 PublicationCorresponds to variant rs121434566dbSNPEnsembl.1
Natural variantiVAR_025142292P → L.1 PublicationCorresponds to variant rs33971258dbSNPEnsembl.1
Natural variantiVAR_060197326R → H.1 PublicationCorresponds to variant rs35832094dbSNPEnsembl.1
Natural variantiVAR_060198326R → L.1 Publication1
Natural variantiVAR_025143326R → P.1 PublicationCorresponds to variant rs35832094dbSNPEnsembl.1
Natural variantiVAR_025144358P → L Associated with Japanese cedar pollinosis. 2 PublicationsCorresponds to variant rs35135976dbSNPEnsembl.1
Natural variantiVAR_025145364R → H.1 PublicationCorresponds to variant rs35232062dbSNPEnsembl.1
Natural variantiVAR_025146441K → T.1 PublicationCorresponds to variant rs35750729dbSNPEnsembl.1
Natural variantiVAR_050486458V → M.Corresponds to variant rs34817773dbSNPEnsembl.1
Natural variantiVAR_025147496H → Q.1 PublicationCorresponds to variant rs33955150dbSNPEnsembl.1
Natural variantiVAR_020031572N → Y.1 PublicationCorresponds to variant rs2302311dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_000502.5.
UniGeneiHs.279259.

Genome annotation databases

EnsembliENST00000225371; ENSP00000225371; ENSG00000121053.
GeneIDi8288.
KEGGihsa:8288.
UCSCiuc002ivq.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_000502.5.
UniGeneiHs.279259.

3D structure databases

ProteinModelPortaliP11678.
SMRiP11678.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113893. 2 interactors.
IntActiP11678. 3 interactors.
STRINGi9606.ENSP00000225371.

Chemistry databases

ChEMBLiCHEMBL2438.
DrugBankiDB01065. Melatonin.

Protein family/group databases

PeroxiBasei3317. HsEPO.

PTM databases

iPTMnetiP11678.
PhosphoSitePlusiP11678.

Polymorphism and mutation databases

BioMutaiEPX.
DMDMi1352738.

Proteomic databases

EPDiP11678.
PaxDbiP11678.
PeptideAtlasiP11678.
PRIDEiP11678.
TopDownProteomicsiP11678.

Protocols and materials databases

DNASUi8288.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000225371; ENSP00000225371; ENSG00000121053.
GeneIDi8288.
KEGGihsa:8288.
UCSCiuc002ivq.4. human.

Organism-specific databases

CTDi8288.
DisGeNETi8288.
GeneCardsiEPX.
H-InvDBHIX0202542.
HGNCiHGNC:3423. EPX.
HPAiHPA050507.
MalaCardsiEPX.
MIMi131399. gene.
261500. phenotype.
neXtProtiNX_P11678.
OpenTargetsiENSG00000121053.
PharmGKBiPA27841.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2408. Eukaryota.
ENOG410XPZ3. LUCA.
GeneTreeiENSGT00550000074325.
HOGENOMiHOG000016084.
HOVERGENiHBG000071.
InParanoidiP11678.
KOiK10788.
OMAiMHVALGL.
OrthoDBiEOG091G02JC.
PhylomeDBiP11678.
TreeFamiTF314316.

Enzyme and pathway databases

BioCyciZFISH:HS04462-MONOMER.
ReactomeiR-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

GeneWikiiEosinophil_peroxidase.
GenomeRNAii8288.
PROiP11678.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000121053.
CleanExiHS_EPO.
HS_EPX.
GenevisibleiP11678. HS.

Family and domain databases

Gene3Di1.10.640.10. 1 hit.
InterProiIPR029599. EPX/EPO.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
[Graphical view]
PANTHERiPTHR11475:SF63. PTHR11475:SF63. 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...

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: November 30, 2016
This is version 173 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

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 one 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.