PERE_MOUSE
ID PERE_MOUSE Reviewed; 716 AA.
AC P49290; Q5SW51; Q61798;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Eosinophil peroxidase;
DE Short=EPO;
DE EC=1.11.1.7;
DE Contains:
DE RecName: Full=Eosinophil peroxidase light chain;
DE Contains:
DE RecName: Full=Eosinophil peroxidase heavy chain;
DE Flags: Precursor;
GN Name=Epx; Synonyms=Eper;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Ohmori J., Itoh H., Tomita M., Nawa Y.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=8773591; DOI=10.1002/jlb.60.2.285;
RA Horton M.A., Larson K.A., Lee J.J., Lee N.A.;
RT "Cloning of the murine eosinophil peroxidase gene (mEPO): characterization
RT of a conserved subgroup of mammalian hematopoietic peroxidases.";
RL J. Leukoc. Biol. 60:285-294(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP FUNCTION, AND NITRATION.
RX PubMed=18694936; DOI=10.1074/jbc.m801196200;
RA Ulrich M., Petre A., Youhnovski N., Proemm F., Schirle M., Schumm M.,
RA Pero R.S., Doyle A., Checkel J., Kita H., Thiyagarajan N., Acharya K.R.,
RA Schmid-Grendelmeier P., Simon H.-U., Schwarz H., Tsutsui M., Shimokawa H.,
RA Bellon G., Lee J.J., Przybylski M., Doering G.;
RT "Post-translational tyrosine nitration of eosinophil granule toxins
RT mediated by eosinophil peroxidase.";
RL J. Biol. Chem. 283:28629-28640(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Mediates tyrosine nitration of secondary granule proteins in
CC mature resting eosinophils. {ECO:0000250, ECO:0000269|PubMed:18694936}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00298};
CC Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-
CC ProRule:PRU00298};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00298};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per
CC heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298};
CC -!- SUBUNIT: Tetramer of two light chains and two heavy chains.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic granules of
CC eosinophils.
CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00298}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40403.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D78353; BAA11370.1; -; mRNA.
DR EMBL; L77979; AAB40403.1; ALT_INIT; mRNA.
DR EMBL; AL606805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25220.1; -.
DR RefSeq; NP_031972.2; NM_007946.2.
DR AlphaFoldDB; P49290; -.
DR SMR; P49290; -.
DR BioGRID; 199492; 2.
DR STRING; 10090.ENSMUSP00000050497; -.
DR ChEMBL; CHEMBL4295770; -.
DR PeroxiBase; 3346; MmEPO.
DR CarbonylDB; P49290; -.
DR GlyGen; P49290; 5 sites.
DR iPTMnet; P49290; -.
DR PhosphoSitePlus; P49290; -.
DR CPTAC; non-CPTAC-3488; -.
DR EPD; P49290; -.
DR MaxQB; P49290; -.
DR PaxDb; P49290; -.
DR PRIDE; P49290; -.
DR ProteomicsDB; 289349; -.
DR Antibodypedia; 30927; 380 antibodies from 27 providers.
DR DNASU; 13861; -.
DR Ensembl; ENSMUST00000049768; ENSMUSP00000050497; ENSMUSG00000052234.
DR GeneID; 13861; -.
DR KEGG; mmu:13861; -.
DR UCSC; uc007kuw.1; mouse.
DR CTD; 8288; -.
DR MGI; MGI:107569; Epx.
DR VEuPathDB; HostDB:ENSMUSG00000052234; -.
DR eggNOG; KOG2408; Eukaryota.
DR GeneTree; ENSGT00940000156009; -.
DR HOGENOM; CLU_006087_1_1_1; -.
DR InParanoid; P49290; -.
DR OMA; CEGTDTD; -.
DR OrthoDB; 276568at2759; -.
DR PhylomeDB; P49290; -.
DR TreeFam; TF314316; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 13861; 0 hits in 73 CRISPR screens.
DR PRO; PR:P49290; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P49290; protein.
DR Bgee; ENSMUSG00000052234; Expressed in femorotibial joint and 18 other tissues.
DR Genevisible; P49290; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IDA:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0002215; P:defense response to nematode; IMP:MGI.
DR GO; GO:0072677; P:eosinophil migration; IMP:MGI.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032693; P:negative regulation of interleukin-10 production; IMP:MGI.
DR GO; GO:0032714; P:negative regulation of interleukin-5 production; IMP:MGI.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; IMP:MGI.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IMP:MGI.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR Gene3D; 1.10.640.10; -; 1.
DR InterPro; IPR029599; EPX/EPO.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR PANTHER; PTHR11475:SF63; PTHR11475:SF63; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Nitration; Oxidoreductase; Peroxidase; Reference proteome;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..140
FT /evidence="ECO:0000255"
FT /id="PRO_0000023642"
FT CHAIN 141..251
FT /note="Eosinophil peroxidase light chain"
FT /id="PRO_0000023643"
FT CHAIN 252..716
FT /note="Eosinophil peroxidase heavy chain"
FT /id="PRO_0000023644"
FT ACT_SITE 234
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 233
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 313
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 381
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 475
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT SITE 378
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT MOD_RES 489
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11678"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 709
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 142..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 254..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 258..282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 360..371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 579..636
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 677..702
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT CONFLICT 167
FT /note="A -> P (in Ref. 2; AAB40403)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="A -> P (in Ref. 2; AAB40403)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="M -> K (in Ref. 1; BAA11370)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="N -> Y (in Ref. 1; BAA11370)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 716 AA; 81380 MW; 9D1D1A88E6E259A1 CRC64;
MMQQLLALVG ALATLILTQH AEGTAPASPS PVEISVLRDC IAEAKLLVDT AYNHTQKSIM
QRLRSGSASP MDLLAYFKQP VAATRRVVQA ADYMHVALGL LEERLQPRGS RPFNATDVLT
EPQLRLLSQA SGCALQDQAE RCSNKYRTIT GRCNNKKHPW LGASNQALAR WLPAEYEDHR
SLPFGWTPGK RRNGFLLPLV RDVSNQIVRF PSKKLTSDRG RALMFMQWGQ FIDHDLDFSP
ESPARVAFSM GVDCEKTCAQ LPPCFPIKIP RNDPRIKNQR DCIPFFRSAP ACPQNRNKVR
NQINALTSFV DASMVYGSEV TLALRLRNRT NFLGLLATNQ RFQDNGRALL PFDNLHEDPC
LLTNRSARIP CFLAGDTRSS ETPKLTALHT LFVREHNRLA AELRRLNPHW SGDKLYNEAR
KIVGAMVQII TYRDFLPLVL GRARIRRTLG PYRGYCSNVD PRVANVFTLA FRFGHTMLQP
FMFRLDSQYR ASAPNSHVPL SSVFFASWRI IHEGGIDPIL RGLMATPAKL NRQDSMLVDE
LRDKLFQQVR RIGLDLAALN MQRSRDHGLP GYNAWRRFCG LSQPRNLAQL SRVLKNQDLA
RKFLRLYKTP DNIDIWVGAI AEPLLPGARV GPLLACLFEN QFRRARDGDR FWWQKWGVFT
KRQRKALRRI SLSRIVCDNT GITTVSRDIF RANIYPQGFV SCSRIPKLNL SAWRGK
