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P11678

- PERE_HUMAN

UniProt

P11678 - PERE_HUMAN

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Protein

Eosinophil peroxidase

Gene

EPX

Organism
Homo sapiens (Human)
Status
Reviewed - 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 Ca(2+) 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)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
Complete GO annotation...

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.

GO - Cellular componenti

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

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

BioGridi113893. 1 interaction.
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.
GeneTreeiENSGT00550000074325.
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

« 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)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:
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_000502.4.
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:
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 .
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

BioGridi 113893. 1 interaction.
IntActi P11678. 3 interactions.
STRINGi 9606.ENSP00000225371.

Chemistry

ChEMBLi CHEMBL2438.
DrugBanki DB01065. Melatonin.

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.
GeneTreei ENSGT00550000074325.
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: November 26, 2014
This is version 154 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