PERM_MOUSE
ID PERM_MOUSE Reviewed; 718 AA.
AC P11247; Q5NCP1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Myeloperoxidase;
DE Short=MPO;
DE EC=1.11.2.2 {ECO:0000269|PubMed:11593004};
DE Contains:
DE RecName: Full=Myeloperoxidase light chain;
DE Contains:
DE RecName: Full=Myeloperoxidase heavy chain;
DE Flags: Precursor;
GN Name=Mpo;
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=C3H/HeJ;
RX PubMed=2548170; DOI=10.1093/nar/17.14.5852;
RA Venturelli D., Shirsat N., Gemperlein I., Bittenbender S., Rovera G.;
RT "Nucleotide sequence of cDNA for murine myeloperoxidase.";
RL Nucleic Acids Res. 17:5852-5852(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2552419; DOI=10.1093/nar/17.19.7987;
RA Venturelli D., Bittenbender S., Rovera G.;
RT "Sequence of the murine myeloperoxidase (MPO) gene.";
RL Nucleic Acids Res. 17:7987-7988(1989).
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 CATALYTIC ACTIVITY.
RX PubMed=11593004; DOI=10.1073/pnas.211190298;
RA Gaut J.P., Yeh G.C., Tran H.D., Byun J., Henderson J.P., Richter G.M.,
RA Brennan M.L., Lusis A.J., Belaaouaj A., Hotchkiss R.S., Heinecke J.W.;
RT "Neutrophils employ the myeloperoxidase system to generate antimicrobial
RT brominating and chlorinating oxidants during sepsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11961-11966(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and 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: Part of the host defense system of polymorphonuclear
CC leukocytes. It is responsible for microbicidal activity against a wide
CC range of organisms. In the stimulated PMN, MPO catalyzes the production
CC of hypohalous acids, primarily hypochlorous acid in physiologic
CC situations, and other toxic intermediates that greatly enhance PMN
CC microbicidal activity (PubMed:11593004). Mediates the proteolytic
CC cleavage of alpha-1-microglobulin to form t-alpha-1-microglobulin,
CC which potently inhibits oxidation of low density lipoprotein particles
CC and limits vascular damage (By similarity).
CC {ECO:0000250|UniProtKB:P05164, ECO:0000269|PubMed:11593004}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride + H(+) + H2O2 = H2O + hypochlorous acid;
CC Xref=Rhea:RHEA:28218, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17996, ChEBI:CHEBI:24757; EC=1.11.2.2;
CC Evidence={ECO:0000269|PubMed:11593004};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per monomer. {ECO:0000250};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per
CC monomer. {ECO:0000250};
CC -!- SUBUNIT: Homodimer; disulfide-linked. Each monomer consists of a light
CC and a heavy chain (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00298}.
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DR EMBL; X15313; CAA33373.1; -; mRNA.
DR EMBL; X15378; CAA33439.1; -; Genomic_DNA.
DR EMBL; AL604022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25217.1; -.
DR PIR; S06068; S06068.
DR RefSeq; NP_034954.2; NM_010824.2.
DR AlphaFoldDB; P11247; -.
DR SMR; P11247; -.
DR BioGRID; 201479; 2.
DR IntAct; P11247; 1.
DR STRING; 10090.ENSMUSP00000020779; -.
DR BindingDB; P11247; -.
DR ChEMBL; CHEMBL2440; -.
DR PeroxiBase; 3344; MmMPO.
DR CarbonylDB; P11247; -.
DR GlyConnect; 2522; 2 N-Linked glycans (2 sites).
DR GlyGen; P11247; 6 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; P11247; -.
DR PhosphoSitePlus; P11247; -.
DR CPTAC; non-CPTAC-3375; -.
DR MaxQB; P11247; -.
DR PaxDb; P11247; -.
DR PeptideAtlas; P11247; -.
DR PRIDE; P11247; -.
DR ProteomicsDB; 288034; -.
DR ABCD; P11247; 6 sequenced antibodies.
DR Antibodypedia; 3513; 1742 antibodies from 55 providers.
DR DNASU; 17523; -.
DR Ensembl; ENSMUST00000020779; ENSMUSP00000020779; ENSMUSG00000009350.
DR Ensembl; ENSMUST00000121303; ENSMUSP00000112837; ENSMUSG00000009350.
DR GeneID; 17523; -.
DR KEGG; mmu:17523; -.
DR UCSC; uc011ycc.1; mouse.
DR CTD; 4353; -.
DR MGI; MGI:97137; Mpo.
DR VEuPathDB; HostDB:ENSMUSG00000009350; -.
DR eggNOG; KOG2408; Eukaryota.
DR GeneTree; ENSGT00940000161343; -.
DR HOGENOM; CLU_006087_1_1_1; -.
DR InParanoid; P11247; -.
DR OMA; FSLPYGW; -.
DR OrthoDB; 276568at2759; -.
DR PhylomeDB; P11247; -.
DR TreeFam; TF314316; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8941413; Events associated with phagocytolytic activity of PMN cells.
DR BioGRID-ORCS; 17523; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Mpo; mouse.
DR PRO; PR:P11247; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P11247; protein.
DR Bgee; ENSMUSG00000009350; Expressed in femorotibial joint and 75 other tissues.
DR ExpressionAtlas; P11247; baseline and differential.
DR Genevisible; P11247; MM.
DR GO; GO:0042582; C:azurophil granule; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IDA:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IMP:MGI.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:MGI.
DR GO; GO:0002149; P:hypochlorous acid biosynthetic process; IMP:MGI.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; ISO:MGI.
DR GO; GO:0019430; P:removal of superoxide radicals; IMP:MGI.
DR GO; GO:0002679; P:respiratory burst involved in defense response; IMP:MGI.
DR GO; GO:0032094; P:response to food; IEA:Ensembl.
DR GO; GO:1990268; P:response to gold nanoparticle; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR GO; GO:0001878; P:response to yeast; IMP:MGI.
DR Gene3D; 1.10.640.10; -; 1.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR029609; MPO.
DR PANTHER; PTHR11475:SF108; PTHR11475:SF108; 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 Lysosome; Metal-binding; Oxidation; Oxidoreductase; Peroxidase;
KW Reference proteome; Signal.
FT SIGNAL 1..15
FT PROPEP 16..138
FT /evidence="ECO:0000255"
FT /id="PRO_0000023657"
FT CHAIN 139..718
FT /note="Myeloperoxidase"
FT /id="PRO_0000023658"
FT CHAIN 139..252
FT /note="Myeloperoxidase light chain"
FT /id="PRO_0000023659"
FT CHAIN 253..718
FT /note="Myeloperoxidase heavy chain"
FT /id="PRO_0000023660"
FT ACT_SITE 235
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 234
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 310
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 312
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT BINDING 382
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 476
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 379
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT MOD_RES 290
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000250"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 711
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 141..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 255..265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 259..283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 361..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 580..637
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT DISULFID 678..704
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT CONFLICT 61
FT /note="S -> T (in Ref. 1; CAA33373 and 2; CAA33439)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="R -> G (in Ref. 1; CAA33373 and 2; CAA33439)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="I -> V (in Ref. 1; CAA33373 and 2; CAA33439)"
FT /evidence="ECO:0000305"
FT CONFLICT 494..495
FT /note="GP -> AA (in Ref. 1; CAA33373 and 2; CAA33439)"
FT /evidence="ECO:0000305"
FT CONFLICT 676
FT /note="I -> L (in Ref. 1; CAA33373 and 2; CAA33439)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 718 AA; 81182 MW; E6763BE528E2ED83 CRC64;
MKLLLALAGL LAPLAMLQTS NGATPALLGE VENSVVLSCM EEAKQLVDRA YKERRESIKR
SLQSGSASPT ELLFYFKQPV AGTRTAVRAA DYLHVALDLL KRKLQPLWPR PFNVTDVLTP
AQLNLLSVSS GCAYQDVRVT CPPNDKYRTI TGHCNNRRSP TLGASNRAFV RWLPAEYEDG
VSMPFGWTPG VNRNGFKVPL ARQVSNAIVR FPNDQLTKDQ ERALMFMQWG QFLDHDITLT
PEPATRFSFF TGLNCETSCL QQPPCFPLKI PPNDPRIKNQ KDCIPFFRSC PACTRNNITI
RNQINALTSF VDASGVYGSE DPLARKLRNL TNQLGLLAIN TRFQDNGRAL MPFDSLHDDP
CLLTNRSARI PCFLAGDMRS SEMPELTSMH TLFVREHNRL ATQLKRLNPR WNGEKLYQEA
RKIVGAMVQI ITYRDYLPLV LGPAAMKKYL PQYRSYNDSV DPRIANVFTN AFRYGHTLIQ
PFMFRLNNQY RPTGPNPRVP LSKVFFASWR VVLEGGIDPI LRGLMATPAK LNRQNQIVVD
EIRERLFEQV MRIGLDLPAL NMQRSRDHGL PGYNAWRRFC GLPQPSTVGE LGTVLKNLEL
ARKLMAQYGT PNNIDIWMGG VSEPLEPNGR VGQLLACLIG TQFRKLRDGD RFWWENPGVF
SKQQRQALAS ISLPRIICDN TGITTVSKNN IFMSNTYPRD FVSCNTLPKL NLTSWKET
