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Protein

Eosinophil peroxidase

Gene

EPX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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: GO_Central

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase, Peroxidase
Biological processHydrogen peroxide
LigandCalcium, Heme, Iron, Metal-binding

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000121053.5
HGNCiHGNC:3423 EPX
MIMi131399 gene
neXtProtiNX_P11678

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 dbSNP:rs121434566EnsemblClinVar.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...) asparagineSequence analysis1
Glycosylationi113N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi141 ↔ 152PROSITE-ProRule annotation
Disulfide bondi253 ↔ 263PROSITE-ProRule annotation
Disulfide bondi257 ↔ 281PROSITE-ProRule annotation
Glycosylationi327N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi359 ↔ 370PROSITE-ProRule annotation
Glycosylationi363N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei488Nitrated tyrosine1 Publication1
Disulfide bondi578 ↔ 635PROSITE-ProRule annotation
Disulfide bondi676 ↔ 701PROSITE-ProRule annotation
Glycosylationi700N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi708N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration

Proteomic databases

EPDiP11678
PaxDbiP11678
PeptideAtlasiP11678
PRIDEiP11678
ProteomicsDBi52797
TopDownProteomicsiP11678

PTM databases

GlyConnecti1208
iPTMnetiP11678
PhosphoSitePlusiP11678

Expressioni

Gene expression databases

BgeeiENSG00000121053 Expressed in 49 organ(s), highest expression level in trabecular bone tissue
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
OMAiQLPPCFP
OrthoDBiEOG091G02JC
PhylomeDBiP11678
TreeFamiTF314316

Family and domain databases

Gene3Di1.10.640.10, 1 hit
InterProiView protein in InterPro
IPR029599 EPX/EPO
IPR010255 Haem_peroxidase
IPR019791 Haem_peroxidase_animal
IPR037120 Haem_peroxidase_sf
PANTHERiPTHR11475:SF63 PTHR11475:SF63, 1 hit
PfamiView protein in Pfam
PF03098 An_peroxidase, 1 hit
PRINTSiPR00457 ANPEROXIDASE
SUPFAMiSSF48113 SSF48113, 1 hit
PROSITEiView protein in PROSITE
PS00435 PEROXIDASE_1, 1 hit
PS50292 PEROXIDASE_3, 1 hit

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 dbSNP:rs34553736Ensembl.1
Natural variantiVAR_02513840I → M1 PublicationCorresponds to variant dbSNP:rs11079339Ensembl.1
Natural variantiVAR_025139122Q → H1 PublicationCorresponds to variant dbSNP:rs11652709Ensembl.1
Natural variantiVAR_025140249A → E1 PublicationCorresponds to variant dbSNP:rs35896669Ensembl.1
Natural variantiVAR_025141276K → R1 PublicationCorresponds to variant dbSNP:rs35074452Ensembl.1
Natural variantiVAR_015376286R → H in EPXD. 1 PublicationCorresponds to variant dbSNP:rs121434566EnsemblClinVar.1
Natural variantiVAR_025142292P → L1 PublicationCorresponds to variant dbSNP:rs33971258Ensembl.1
Natural variantiVAR_060197326R → H1 PublicationCorresponds to variant dbSNP:rs35832094Ensembl.1
Natural variantiVAR_060198326R → L1 Publication1
Natural variantiVAR_025143326R → P1 PublicationCorresponds to variant dbSNP:rs35832094Ensembl.1
Natural variantiVAR_025144358P → L Associated with Japanese cedar pollinosis. 2 PublicationsCorresponds to variant dbSNP:rs35135976Ensembl.1
Natural variantiVAR_025145364R → H1 PublicationCorresponds to variant dbSNP:rs35232062Ensembl.1
Natural variantiVAR_025146441K → T1 PublicationCorresponds to variant dbSNP:rs35750729Ensembl.1
Natural variantiVAR_050486458V → M. Corresponds to variant dbSNP:rs34817773Ensembl.1
Natural variantiVAR_025147496H → Q1 PublicationCorresponds to variant dbSNP:rs33955150Ensembl.1
Natural variantiVAR_020031572N → Y1 PublicationCorresponds to variant dbSNP:rs2302311Ensembl.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

Similar proteinsi

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

GlyConnecti1208
iPTMnetiP11678
PhosphoSitePlusiP11678

Polymorphism and mutation databases

BioMutaiEPX
DMDMi1352738

Proteomic databases

EPDiP11678
PaxDbiP11678
PeptideAtlasiP11678
PRIDEiP11678
ProteomicsDBi52797
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
EuPathDBiHostDB:ENSG00000121053.5
GeneCardsiEPX
H-InvDBiHIX0202542
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
OMAiQLPPCFP
OrthoDBiEOG091G02JC
PhylomeDBiP11678
TreeFamiTF314316

Enzyme and pathway databases

ReactomeiR-HSA-6798695 Neutrophil degranulation

Miscellaneous databases

ChiTaRSiEPX human
GeneWikiiEosinophil_peroxidase
GenomeRNAii8288
PROiPR:P11678
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000121053 Expressed in 49 organ(s), highest expression level in trabecular bone tissue
CleanExiHS_EPO
HS_EPX
GenevisibleiP11678 HS

Family and domain databases

Gene3Di1.10.640.10, 1 hit
InterProiView protein in InterPro
IPR029599 EPX/EPO
IPR010255 Haem_peroxidase
IPR019791 Haem_peroxidase_animal
IPR037120 Haem_peroxidase_sf
PANTHERiPTHR11475:SF63 PTHR11475:SF63, 1 hit
PfamiView protein in Pfam
PF03098 An_peroxidase, 1 hit
PRINTSiPR00457 ANPEROXIDASE
SUPFAMiSSF48113 SSF48113, 1 hit
PROSITEiView protein in PROSITE
PS00435 PEROXIDASE_1, 1 hit
PS50292 PEROXIDASE_3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPERE_HUMAN
AccessioniPrimary (citable) accession number: P11678
Secondary accession number(s): Q4TVP3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: February 1, 1996
Last modified: November 7, 2018
This is version 185 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
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Main funding by: National Institutes of Health

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