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MGP001957

UniProt Annotations

Entry Information
Gene Namemyeloperoxidase
Protein EntryPERM_HUMAN
UniProt IDP05164
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=3; Name=H17; Synonyms=B; IsoId=P05164-1; Sequence=Displayed; Name=H14; IsoId=P05164-2; Sequence=VSP_007206; Name=H7; Synonyms=A; IsoId=P05164-3; Sequence=VSP_007207;
Catalytic ActivityCl(-) + H(2)O(2) + H(+) = HClO + H(2)O.
Catalytic ActivityCl(-) + H(2)O(2) = HOCl + 2 H(2)O.
CofactorName=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per monomer.;
CofactorName=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per monomer.;
DiseaseMyeloperoxidase deficiency (MPOD) [MIM:254600]: A disorder characterized by decreased myeloperoxidase activity in neutrophils and monocytes that results in disseminated candidiasis. {ECO:0000269|PubMed:7904599, ECO:0000269|PubMed:8142659, ECO:0000269|PubMed:9354683, ECO:0000269|PubMed:9637725}. Note=The disease is caused by mutations affecting the gene represented in this entry.
FunctionPart of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity.
SimilarityBelongs to the peroxidase family. XPO subfamily. {ECO:0000255|PROSITE-ProRule:PRU00298}.
Subcellular LocationLysosome.
SubunitHomodimer; disulfide-linked. Each monomer consists of a light and a heavy chain. {ECO:0000269|PubMed:10766826, ECO:0000269|PubMed:20332087}.
Web ResourceName=MPObase; Note=MPO mutation db; URL="http://structure.bmc.lu.se/idbase/MPObase/";
Web ResourceName=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/mpo/";
Web ResourceName=Wikipedia; Note=Myeloperoxidase entry; URL="http://en.wikipedia.org/wiki/Myeloperoxidase";
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