Mpo
entrez
17523
canonical
uniprot
P11247
canonical
ensembl
ENSMUSG00000009350
resolver
ensp
ENSMUSP00000020779
resolver
ensp
ENSMUSP00000112837
resolver
enst
ENSMUST00000020779
resolver
enst
ENSMUST00000121303
resolver
genesymbol
Mpo
resolver
genesymbol_syn
mKIAA4033
resolver
uniprot
Q571G0
resolver
uniprot
Q5NCP1
resolver
uniprot
Q7TMS4
resolver
uniprot_entry
PERM_MOUSE
resolver
uniprot_entry
Q571G0_MOUSE
resolver
uniprot_entry
Q7TMS4_MOUSE
resolver
uniprot_sec
Q5NCP1
resolver
activity_regulation
ACTIVITY REGULATION: The peroxidase activity is inhibited by CP (ceruloplasmin). {ECO:0000269|PubMed:23306200}.
uniprot
proteins
amino_acid_sequence
MKLLLALAGLLAPLAMLQTSNGATPALLGEVENSVVLSCMEEAKQLVDRAYKERRESIKRSLQSGSASPTELLFYFKQPVAGTRTAVRAADYLHVALDLLKRKLQPLWPRPFNVTDVLTPAQLNLLSVSSGCAYQDVRVTCPPNDKYRTITGHCNNRRSPTLGASNRAFVRWLPAEYEDGVSMPFGWTPGVNRNGFKVPLARQVSNAIVRFPNDQLTKDQERALMFMQWGQFLDHDITLTPEPATRFSFFTGLNCETSCLQQPPCFPLKIPPNDPRIKNQKDCIPFFRSCPACTRNNITIRNQINALTSFVDASGVYGSEDPLARKLRNLTNQLGLLAINTRFQDNGRALMPFDSLHDDPCLLTNRSARIPCFLAGDMRSSEMPELTSMHTLFVREHNRLATQLKRLNPRWNGEKLYQEARKIVGAMVQIITYRDYLPLVLGPAAMKKYLPQYRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLNNQYRPTGPNPRVPLSKVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIVVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPSTVGELGTVLKNLELARKLMAQYGTPNNIDIWMGGVSEPLEPNGRVGQLLACLIGTQFRKLRDGDRFWWENPGVFSKQQRQALASISLPRIICDNTGITTVSKNNIFMSNTYPRDFVSCNTLPKLNLTSWKET
uniprot
proteins
ec_number
1.11.2.2
uniprot
proteins
function
FUNCTION: Peroxidase that plays a central role in the host defense system of polymorphonuclear leukocytes by mediating both (1) formation of neutrophil extracellular trap (NETs) and (2) microbicidal activity (PubMed:10085024, PubMed:11593004, PubMed:23306200). Promotes NET formation by mediating chromatin disassembly: translocates to the nucleus and specifically binds to nucleosomes, both as monomer and homodimer, leading to nucleosome unstacking and initial chromatin decondensation (By similarity). Homodimers clash with one end of the nucleosomal DNA, leading to DNA unwrapping, initiating complete disassembly of nucleosomes and chromatin transformation into NETs in an ATP-independent manner (By similarity). NETs, which are mainly composed of DNA fibers and globular proteins, are then extruded into the extracellular space by neutrophils to trap pathogens and release antimicrobial proteins to destroy them (By similarity). Participates to the microbicidal activity against a wide range of organisms by acting as a peroxidase that catalyzes the formation of oxidants in presence of hydrogen peroxide (PubMed:11593004). Mediates the formation of hypohalous acids, mainly hypochlorous acid (HOCl) in physiologic situations, that greatly enhance polymorphonuclear leukocyte microbicidal activity (PubMed:11593004, PubMed:23306200). In addition to hypochlorous acid, catalyzes formation of hypobromous acid (HOBr), hypoiodous acid (HOI) and hypothiocyanous acid (HOSCN) (By similarity). Also catalyzes oxidation of nitrite into the highly reactive nitrogen dioxide radical (By similarity). Formation of oxidants are widely believed to be responsible for much of the anti-bactericidal activity of neutrophils (By similarity). Oxidants, such as hypochlorous acid or nitrogen dioxide radical, can also oxidize amino acid residues on proteins and generate chlorination and nitration post-translational modifications, respectively (By similarity). Chlorination and nitration of the lipid-free form of APOA1 impairs cholesterol transport (By similarity). Superoxides generated by MPO can also promote dioxygenation of tryptophan residues on proteins (By similarity). Also able to oxidize melatonin into N1-acetyl-N2-formyl-5-methoxykynuramine either in presence of hydrogen peroxide or superoxide (By similarity). Oxidizes urate into 5-hydroxyisourate (By similarity). Functions as a nitric oxide (NO) oxidase during inflammation, by catalytically consuming NO, impairing NO's ability to maintain vascular tone and function (By similarity). May also mediate the proteolytic cleavage of alpha-1-microglobulin to form t-alpha-1-microglobulin, which potently inhibits oxidation of low-density lipoprotein particles and limits vascular damage (By similarity). {ECO:0000250|UniProtKB:P05164, ECO:0000269|PubMed:10085024, ECO:0000269|PubMed:11593004, ECO:0000269|PubMed:23306200}.; FUNCTION: [Myeloperoxidase light chain]: Light chain of the mature myeloperoxidase. {ECO:0000250|UniProtKB:P05164}.; FUNCTION: [Myeloperoxidase heavy chain]: Heavy chain of the mature myeloperoxidase. {ECO:0000250|UniProtKB:P05164}.
uniprot
proteins
mass_dalton
81182
uniprot
proteins
post_translational_modification
PTM: Mature myeloperoxidase is a homodimer linked by disulfide bond, with each monomer composed of a heavy and light chain. Myeloperoxidase encompasses a series of critical proteolytic processing steps during maturation: after cotranslational cleavage of the signal peptide and N-linked glycosylation followed by limited deglucosylation, myeloperoxidase acquires heme in the endoplasmic reticulum (ER) to form the 84 kDa myeloperoxidase (also named promyeloperoxidase). A proconvertase then eliminates the propeptide region (49-164) in a post-ER compartment producing an intermediate species that is subsequently processed by cysteine proteases to the light chain and heavy chain followed by homodimerization. {ECO:0000250|UniProtKB:P05164}.; PTM: Myeloperoxidase monomers are linked by an interchain disulfide bond at Cys-293. During maturation, the 84 kDa myeloperoxidase (also named promyeloperoxidase) precursor contains a disulfide bond between Cys-132 and Cys-293 that prevents homodimerization. {ECO:0000250|UniProtKB:P05164}.
uniprot
proteins
protein_family
Peroxidase family
uniprot
proteins
protein_family
XPO subfamily
uniprot
proteins
pubmed
10085024
uniprot
proteins
pubmed
11593004
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23306200
uniprot
proteins
pubmed
2548170
uniprot
proteins
pubmed
2552419
uniprot
proteins
pubmed
33234591
uniprot
proteins
sequence_length
718
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P05164}. Cytolytic granule {ECO:0000250|UniProtKB:P05164}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:P05164}. Secreted {ECO:0000250|UniProtKB:P05164}. Nucleus {ECO:0000250|UniProtKB:P05164}. Chromosome {ECO:0000250|UniProtKB:P05164}. Note=Localizes to azurophil granules, a type of primary lysosome found in neutrophils and monocytes that contains antimicrobial proteins (By similarity). A substantial fraction is also constitutively secreted by normal bone marrow granulocyte precursors (By similarity). During formation of neutrophil extracellular traps (NETs), translocates into the nucleus and associates to chromatin, leading to chromatin dislocation and its transformation into NETs (By similarity). Core component of NETs (By similarity). {ECO:0000250|UniProtKB:P05164}.
uniprot
proteins