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P49290 (PERE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eosinophil peroxidase
Short name=EPO
EC=1.11.1.7

Cleaved into the following 2 chains:

  1. Eosinophil peroxidase light chain
  2. Eosinophil peroxidase heavy chain
Gene names
Name:Epx
Synonyms:Eper
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length716 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils By similarity. Ref.4

Catalytic activity

2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.

Cofactor

Binds 1 calcium ion per heterodimer By similarity.

Binds 1 heme B (iron-protoporphyrin IX) group covalently per heterodimer By similarity.

Subunit structure

Tetramer of two light chains and two heavy chains By similarity.

Subcellular location

Cytoplasmic granule. Note: Cytoplasmic granules of eosinophils.

Sequence similarities

Belongs to the peroxidase family. XPO subfamily.

Sequence caution

The sequence AAB40403.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 140122 Potential
PRO_0000023642
Chain141 – 251111Eosinophil peroxidase light chain
PRO_0000023643
Chain252 – 716465Eosinophil peroxidase heavy chain
PRO_0000023644

Sites

Active site2341Proton acceptor By similarity
Metal binding2351Calcium By similarity
Metal binding3071Calcium By similarity
Metal binding3091Calcium; via carbonyl oxygen By similarity
Metal binding3111Calcium By similarity
Metal binding3131Calcium By similarity
Metal binding4751Iron (heme axial ligand) By similarity
Binding site2331Heme (covalent; via 2 links) By similarity
Binding site3811Heme (covalent; via 2 links) By similarity
Site3781Transition state stabilizer By similarity

Amino acid modifications

Modified residue4891Nitrated tyrosine By similarity
Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation1141N-linked (GlcNAc...) Potential
Glycosylation3281N-linked (GlcNAc...) Potential
Glycosylation3641N-linked (GlcNAc...) Potential
Glycosylation7091N-linked (GlcNAc...) Potential
Disulfide bond142 ↔ 153 By similarity
Disulfide bond254 ↔ 264 By similarity
Disulfide bond258 ↔ 282 By similarity
Disulfide bond360 ↔ 371 By similarity
Disulfide bond579 ↔ 636 By similarity
Disulfide bond677 ↔ 702 By similarity

Experimental info

Sequence conflict1671A → P in AAB40403. Ref.2
Sequence conflict4001A → P in AAB40403. Ref.2
Sequence conflict5241M → K in BAA11370. Ref.1
Sequence conflict5311N → Y in BAA11370. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49290 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 9D1D1A88E6E259A1

FASTA71681,380
        10         20         30         40         50         60 
MMQQLLALVG ALATLILTQH AEGTAPASPS PVEISVLRDC IAEAKLLVDT AYNHTQKSIM 

        70         80         90        100        110        120 
QRLRSGSASP MDLLAYFKQP VAATRRVVQA ADYMHVALGL LEERLQPRGS RPFNATDVLT 

       130        140        150        160        170        180 
EPQLRLLSQA SGCALQDQAE RCSNKYRTIT GRCNNKKHPW LGASNQALAR WLPAEYEDHR 

       190        200        210        220        230        240 
SLPFGWTPGK RRNGFLLPLV RDVSNQIVRF PSKKLTSDRG RALMFMQWGQ FIDHDLDFSP 

       250        260        270        280        290        300 
ESPARVAFSM GVDCEKTCAQ LPPCFPIKIP RNDPRIKNQR DCIPFFRSAP ACPQNRNKVR 

       310        320        330        340        350        360 
NQINALTSFV DASMVYGSEV TLALRLRNRT NFLGLLATNQ RFQDNGRALL PFDNLHEDPC 

       370        380        390        400        410        420 
LLTNRSARIP CFLAGDTRSS ETPKLTALHT LFVREHNRLA AELRRLNPHW SGDKLYNEAR 

       430        440        450        460        470        480 
KIVGAMVQII TYRDFLPLVL GRARIRRTLG PYRGYCSNVD PRVANVFTLA FRFGHTMLQP 

       490        500        510        520        530        540 
FMFRLDSQYR ASAPNSHVPL SSVFFASWRI IHEGGIDPIL RGLMATPAKL NRQDSMLVDE 

       550        560        570        580        590        600 
LRDKLFQQVR RIGLDLAALN MQRSRDHGLP GYNAWRRFCG LSQPRNLAQL SRVLKNQDLA 

       610        620        630        640        650        660 
RKFLRLYKTP DNIDIWVGAI AEPLLPGARV GPLLACLFEN QFRRARDGDR FWWQKWGVFT 

       670        680        690        700        710 
KRQRKALRRI SLSRIVCDNT GITTVSRDIF RANIYPQGFV SCSRIPKLNL SAWRGK

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"Post-translational tyrosine nitration of eosinophil granule toxins mediated by eosinophil peroxidase."
Ulrich M., Petre A., Youhnovski N., Proemm F., Schirle M., Schumm M., Pero R.S., Doyle A., Checkel J., Kita H., Thiyagarajan N., Acharya K.R., Schmid-Grendelmeier P., Simon H.-U., Schwarz H., Tsutsui M., Shimokawa H., Bellon G. expand/collapse author list , Lee J.J., Przybylski M., Doering G.
J. Biol. Chem. 283:28629-28640(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, NITRATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D78353 mRNA. Translation: BAA11370.1.
L77979 mRNA. Translation: AAB40403.1. Different initiation.
AL606805 Genomic DNA. Translation: CAI25724.1.
IPIIPI00113854.
RefSeqNP_031972.2. NM_007946.2.
UniGeneMm.1315.

3D structure databases

ProteinModelPortalP49290.
SMRP49290. Positions 144-716.
ModBaseSearch...

Protein family/group databases

PeroxiBase3346. MmEPO.

PTM databases

PhosphoSiteP49290.

Proteomic databases

PaxDbP49290.
PRIDEP49290.

Protocols and materials databases

DNASU13861.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049768; ENSMUSP00000050497; ENSMUSG00000052234.
GeneID13861.
KEGGmmu:13861.

Organism-specific databases

CTD8288.
MGIMGI:107569. Epx.

Phylogenomic databases

eggNOGNOG262194.
GeneTreeENSGT00550000074325.
HOGENOMHOG000016084.
HOVERGENHBG000071.
InParanoidQ5SW51.
KOK10788.
OMARTITGRC.
OrthoDBEOG4ZGPBX.

Gene expression databases

ArrayExpressP49290.
BgeeP49290.
CleanExMM_EPX.
GenevestigatorP49290.
GermOnlineENSMUSG00000052234. Mus musculus.

Family and domain databases

Gene3D1.10.640.10. 1 hit.
InterProIPR010255. Haem_peroxidase.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_subgr.
[Graphical view]
PfamPF03098. An_peroxidase. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. False negative.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284746.
SOURCESearch...

Entry information

Entry namePERE_MOUSE
AccessionPrimary (citable) accession number: P49290
Secondary accession number(s): Q5SW51, Q61798
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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