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Myeloperoxidase (MPO) (EC 1.11.2.2) [Cleaved into: Myeloperoxidase; 89 kDa myeloperoxidase; 84 kDa myeloperoxidase; Myeloperoxidase light chain; Myeloperoxidase heavy chain]

 PERM_HUMAN              Reviewed;         745 AA.
P05164; A1L4B8; Q14862; Q4PJH5; Q9UCL7;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
30-AUG-2017, entry version 205.
RecName: Full=Myeloperoxidase;
Short=MPO;
EC=1.11.2.2 {ECO:0000269|PubMed:9922160};
Contains:
RecName: Full=Myeloperoxidase;
Contains:
RecName: Full=89 kDa myeloperoxidase;
Contains:
RecName: Full=84 kDa myeloperoxidase;
Contains:
RecName: Full=Myeloperoxidase light chain;
Contains:
RecName: Full=Myeloperoxidase heavy chain;
Flags: Precursor;
Name=MPO;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
PubMed=3029127;
Morishita K., Kubota N., Asano S., Kaziro Y., Nagata S.;
"Molecular cloning and characterization of cDNA for human
myeloperoxidase.";
J. Biol. Chem. 262:3844-3851(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2444596;
Morishita K., Tsuchiya M., Asano S., Kaziro Y., Nagata S.;
"Chromosomal gene structure of human myeloperoxidase and regulation of
its expression by granulocyte colony-stimulating factor.";
J. Biol. Chem. 262:15208-15213(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
PubMed=3654979; DOI=10.1172/JCI113181;
Seto P., Hirayu H., Magnusson R.P., Gestautas J., Portmann L.,
Degroot L.J., Rapoport B.;
"Isolation of a complementary DNA clone for thyroid microsomal
antigen. Homology with the gene for thyroid peroxidase.";
J. Clin. Invest. 80:1205-1208(1987).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
PubMed=3031585; DOI=10.1093/nar/15.5.2013;
Johnson K.R., Nauseef W.M., Care A., Wheelock M.J., Shane S.,
Hudson S., Koeffler H.P., Selsted M., Miller C., Rovera G.;
"Characterization of cDNA clones for human myeloperoxidase: predicted
amino acid sequence and evidence for multiple mRNA species.";
Nucleic Acids Res. 15:2013-2028(1987).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS H7; H14 AND H17),
AND PROTEIN SEQUENCE OF 165-183; 216-222; 295-304; 311-331; 464-479;
662-676 AND 766-776.
TISSUE=Leukemia;
PubMed=2903767; DOI=10.1021/bi00416a013;
Hashinaka K., Nishio C., Hur S.-J., Sakiyama F., Tsunasawa S.,
Yamada M.;
"Multiple species of myeloperoxidase messenger RNAs produced by
alternative splicing and differential polyadenylation.";
Biochemistry 27:5906-5914(1988).
[6]
ERRATUM.
Hashinaka K., Nishio C., Hur S.-J., Sakiyama F., Tsunasawa S.,
Yamada M.;
Biochemistry 27:9226-9226(1988).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2552418; DOI=10.1093/nar/17.19.7985;
Johnson K.R., Gemperlein I., Hudson S., Shane S., Rovera G.;
"Complete nucleotide sequence of the human myeloperoxidase gene.";
Nucleic Acids Res. 17:7985-7986(1989).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
PubMed=8383257;
Hosokawa Y., Kawaguchi R., Hikiji K., Yamada M., Suzuki K.,
Nakagawa T., Yoshihara T., Yamaguchi K.;
"Cloning and characterization of four types of cDNA encoding
myeloperoxidase from human monocytic leukemia cell line, SKM-1.";
Leukemia 7:441-445(1993).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-53; CYS-604;
GLN-683 AND VAL-717.
NIEHS SNPs program;
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM H17).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
PROTEIN SEQUENCE OF 49-66.
PubMed=2154223; DOI=10.1016/0006-291X(90)90888-T;
Yamada M., Hur S.-J., Toda H.;
"Isolation and characterization of extracellular myeloperoxidase
precursor in HL-60 cell cultures.";
Biochem. Biophys. Res. Commun. 166:852-859(1990).
[13]
PROTEIN SEQUENCE OF 49-53, SUBUNIT, GLYCOSYLATION AT ASN-323; ASN-355;
ASN-391; ASN-483 AND ASN-729, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20332087; DOI=10.1074/jbc.M109.089748;
Van Antwerpen P., Slomianny M.C., Boudjeltia K.Z., Delporte C.,
Faid V., Calay D., Rousseau A., Moguilevsky N., Raes M., Vanhamme L.,
Furtmueller P.G., Obinger C., Vanhaeverbeek M., Neve J.,
Michalski J.C.;
"Glycosylation pattern of mature dimeric leukocyte and recombinant
monomeric myeloperoxidase: glycosylation is required for optimal
enzymatic activity.";
J. Biol. Chem. 285:16351-16359(2010).
[14]
PROTEIN SEQUENCE OF 279-424.
TISSUE=Leukocyte;
PubMed=1334087;
Taylor K.L., Pohl J., Kinkade J.M. Jr.;
"Unique autolytic cleavage of human myeloperoxidase. Implications for
the involvement of active site MET409.";
J. Biol. Chem. 267:25282-25288(1992).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 548-629.
PubMed=8390465;
Yamada M., Yoshida M., Hashinaka K.;
"Identification of transcriptional cis-elements in introns 7 and 9 of
the myeloperoxidase gene.";
J. Biol. Chem. 268:13479-13485(1993).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 588-745.
PubMed=2884926; DOI=10.1016/0003-9861(87)90304-3;
Yamada M., Hur S.-J., Hashinaka K., Tsuneoka K., Saeki T., Nishio C.,
Sakiyama F., Tsunasawa S.;
"Isolation and characterization of a cDNA coding for human
myeloperoxidase.";
Arch. Biochem. Biophys. 255:147-155(1987).
[17]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=9922160; DOI=10.1021/bi9818772;
Furtmueller P.G., Burner U., Obinger C.;
"Reaction of myeloperoxidase compound I with chloride, bromide,
iodide, and thiocyanate.";
Biochemistry 37:17923-17930(1998).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-139 AND ASN-483.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323 AND ASN-483.
TISSUE=Saliva;
PubMed=16740002; DOI=10.1021/pr050492k;
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,
Loo J.A.;
"Identification of N-linked glycoproteins in human saliva by
glycoprotein capture and mass spectrometry.";
J. Proteome Res. 5:1493-1503(2006).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-355 AND ASN-391.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 167-744, AND SUBUNIT.
PubMed=10766826; DOI=10.1074/jbc.275.16.11964;
Fiedler T.J., Davey C.A., Fenna R.E.;
"X-ray crystal structure and characterization of halide-binding sites
of human myeloperoxidase at 1.8-A resolution.";
J. Biol. Chem. 275:11964-11971(2000).
[23]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 167-744, AND OXIDATION AT
CYS-316.
PubMed=7840679; DOI=10.1006/abbi.1995.1086;
Fenna R.E., Zeng J., Davey C.;
"Structure of the green heme in myeloperoxidase.";
Arch. Biochem. Biophys. 316:653-656(1995).
[24]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 167-744.
PubMed=11705390; DOI=10.1021/bi0111808;
Blair-Johnson M., Fiedler T., Fenna R.;
"Human myeloperoxidase: structure of a cyanide complex and its
interaction with bromide and thiocyanate substrates at 1.9 A
resolution.";
Biochemistry 40:13990-13997(2001).
[25]
VARIANT MPOD TRP-569.
PubMed=8142659;
Kizaki M., Miller C.W., Selsted M.E., Koeffler H.P.;
"Myeloperoxidase (MPO) gene mutation in hereditary MPO deficiency.";
Blood 83:1935-1940(1994).
[26]
VARIANT MPOD TRP-569.
PubMed=7904599;
Nauseef W.M., Brigham S., Cogley M.;
"Hereditary myeloperoxidase deficiency due to a missense mutation of
arginine 569 to tryptophan.";
J. Biol. Chem. 269:1212-1216(1994).
[27]
CHARACTERIZATION OF VARIANT MPOD TRP-569.
PubMed=8621627; DOI=10.1074/jbc.271.16.9546;
Nauseef W., Cogley M., McCormick S.;
"Effect of the R569W missense mutation on the biosynthesis of
myeloperoxidase.";
J. Biol. Chem. 271:9546-9549(1996).
[28]
VARIANT MPOD CYS-173, AND CHARACTERIZATION OF VARIANT MPOD CYS-173.
PubMed=9637725; DOI=10.1172/JCI2649;
DeLeo F.R., Goedken M., McCormick S.J., Nauseef W.M.;
"A novel form of hereditary myeloperoxidase deficiency linked to
endoplasmic reticulum/proteasome degradation.";
J. Clin. Invest. 101:2900-2909(1998).
[29]
VARIANT MPOD THR-251.
PubMed=9354683;
Romano M., Dri P., Dadalt L., Patriarca P., Baralle F.E.;
"Biochemical and molecular characterization of hereditary
myeloperoxidase deficiency.";
Blood 90:4126-4134(1997).
[30]
VARIANT [LARGE SCALE ANALYSIS] GLN-447.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Part 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. {ECO:0000269|PubMed:9922160}.
-!- CATALYTIC ACTIVITY: Cl(-) + H(2)O(2) + H(+) = HClO + H(2)O.
{ECO:0000269|PubMed:9922160}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 1 Ca(2+) ion per monomer.;
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently
per monomer.;
-!- SUBUNIT: Homodimer; disulfide-linked. Each monomer consists of a
light and a heavy chain. {ECO:0000269|PubMed:10766826,
ECO:0000269|PubMed:20332087}.
-!- SUBCELLULAR LOCATION: Lysosome.
-!- ALTERNATIVE PRODUCTS:
Event=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;
-!- DISEASE: Myeloperoxidase 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:8621627,
ECO:0000269|PubMed:9354683, ECO:0000269|PubMed:9637725}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00298}.
-!- WEB RESOURCE: Name=MPObase; Note=MPO mutation db;
URL="http://structure.bmc.lu.se/idbase/MPObase/";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mpo/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Myeloperoxidase entry;
URL="https://en.wikipedia.org/wiki/Myeloperoxidase";
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EMBL; J02694; AAA59896.1; -; mRNA.
EMBL; M17176; AAA60346.1; -; Genomic_DNA.
EMBL; M17170; AAA60346.1; JOINED; Genomic_DNA.
EMBL; M17171; AAA60346.1; JOINED; Genomic_DNA.
EMBL; M17172; AAA60346.1; JOINED; Genomic_DNA.
EMBL; M17173; AAA60346.1; JOINED; Genomic_DNA.
EMBL; M17174; AAA60346.1; JOINED; Genomic_DNA.
EMBL; M17175; AAA60346.1; JOINED; Genomic_DNA.
EMBL; X04876; CAA28565.1; -; mRNA.
EMBL; M19507; AAA59863.1; -; mRNA.
EMBL; M19508; AAA59864.1; -; Genomic_DNA.
EMBL; M19508; AAA59865.1; -; Genomic_DNA.
EMBL; X15377; CAA33438.1; -; Genomic_DNA.
EMBL; S56200; AAB25582.1; -; mRNA.
EMBL; DQ088846; AAY68218.1; -; Genomic_DNA.
EMBL; CH471109; EAW94470.1; -; Genomic_DNA.
EMBL; BC130476; AAI30477.1; -; mRNA.
EMBL; D14466; BAA03362.1; -; Genomic_DNA.
CCDS; CCDS11604.1; -. [P05164-1]
PIR; A29467; OPHUM.
PIR; B28894; B28894.
PIR; D28894; D28894.
RefSeq; NP_000241.1; NM_000250.1. [P05164-1]
UniGene; Hs.458272; -.
PDB; 1CXP; X-ray; 1.80 A; A/B=167-270, C/D=279-744.
PDB; 1D2V; X-ray; 1.75 A; A/B=167-270, C/D=279-744.
PDB; 1D5L; X-ray; 1.90 A; A/B=167-270, C/D=279-744.
PDB; 1D7W; X-ray; 1.90 A; A/B=167-270, C/D=279-744.
PDB; 1DNU; X-ray; 1.85 A; A/B=167-270, C/D=279-744.
PDB; 1DNW; X-ray; 1.90 A; A/B=167-270, C/D=279-744.
PDB; 1MHL; X-ray; 2.25 A; A/B=165-272, C/D=279-744.
PDB; 1MYP; X-ray; 3.00 A; A/B=165-272, C/D=279-744.
PDB; 3F9P; X-ray; 2.93 A; A/B=165-278, C/D=279-745.
PDB; 3ZS0; X-ray; 2.30 A; A/B=165-272, C/D=279-745.
PDB; 3ZS1; X-ray; 2.60 A; A/B=165-278, C/D=279-745.
PDB; 4C1M; X-ray; 2.00 A; A/B=165-272, C/D=279-745.
PDB; 4DL1; X-ray; 2.00 A; A/B/E/F/I/J/M/N=167-270, C/D/G/H/K/L/O/P=279-744.
PDB; 4EJX; X-ray; 4.69 A; B=165-278, D=279-745.
PDB; 5FIW; X-ray; 1.70 A; A/B=167-271, C/D=279-744.
PDB; 5MFA; X-ray; 1.20 A; A=49-745.
PDBsum; 1CXP; -.
PDBsum; 1D2V; -.
PDBsum; 1D5L; -.
PDBsum; 1D7W; -.
PDBsum; 1DNU; -.
PDBsum; 1DNW; -.
PDBsum; 1MHL; -.
PDBsum; 1MYP; -.
PDBsum; 3F9P; -.
PDBsum; 3ZS0; -.
PDBsum; 3ZS1; -.
PDBsum; 4C1M; -.
PDBsum; 4DL1; -.
PDBsum; 4EJX; -.
PDBsum; 5FIW; -.
PDBsum; 5MFA; -.
ProteinModelPortal; P05164; -.
SMR; P05164; -.
BioGrid; 110493; 6.
IntAct; P05164; 3.
MINT; MINT-1522833; -.
STRING; 9606.ENSP00000225275; -.
BindingDB; P05164; -.
ChEMBL; CHEMBL2439; -.
DrugBank; DB00233; Aminosalicylic Acid.
DrugBank; DB00006; Bivalirudin.
DrugBank; DB02300; Calcipotriol.
DrugBank; DB06774; Capsaicin.
DrugBank; DB00958; Carboplatin.
DrugBank; DB00833; Cefaclor.
DrugBank; DB00535; Cefdinir.
DrugBank; DB00515; Cisplatin.
DrugBank; DB00847; Cysteamine.
DrugBank; DB00250; Dapsone.
DrugBank; DB05161; Elafin.
DrugBank; DB01225; Enoxaparin.
DrugBank; DB04827; Ethyl carbamate.
DrugBank; DB00062; Human Serum Albumin.
DrugBank; DB00583; L-Carnitine.
DrugBank; DB01065; Melatonin.
DrugBank; DB00244; Mesalazine.
DrugBank; DB00461; Nabumetone.
DrugBank; DB04821; Nomifensine.
DrugBank; DB00104; Octreotide.
DrugBank; DB00526; Oxaliplatin.
DrugBank; DB00550; Propylthiouracil.
DrugBank; DB00208; Ticlopidine.
DrugBank; DB06823; Tiopronin.
DrugBank; DB00500; Tolmetin.
GuidetoPHARMACOLOGY; 2789; -.
PeroxiBase; 3315; HsMPO.
iPTMnet; P05164; -.
PhosphoSitePlus; P05164; -.
SwissPalm; P05164; -.
UniCarbKB; P05164; -.
BioMuta; MPO; -.
DMDM; 129825; -.
EPD; P05164; -.
PaxDb; P05164; -.
PeptideAtlas; P05164; -.
PRIDE; P05164; -.
DNASU; 4353; -.
Ensembl; ENST00000225275; ENSP00000225275; ENSG00000005381. [P05164-1]
GeneID; 4353; -.
KEGG; hsa:4353; -.
UCSC; uc002ivu.1; human. [P05164-1]
CTD; 4353; -.
DisGeNET; 4353; -.
GeneCards; MPO; -.
H-InvDB; HIX0039242; -.
HGNC; HGNC:7218; MPO.
HPA; CAB000059; -.
HPA; HPA021147; -.
HPA; HPA061464; -.
MalaCards; MPO; -.
MIM; 254600; phenotype.
MIM; 606989; gene.
neXtProt; NX_P05164; -.
OpenTargets; ENSG00000005381; -.
Orphanet; 2587; Myeloperoxidase deficiency.
PharmGKB; PA243; -.
eggNOG; KOG2408; Eukaryota.
eggNOG; ENOG410XPZ3; LUCA.
GeneTree; ENSGT00550000074325; -.
HOGENOM; HOG000016084; -.
HOVERGEN; HBG000071; -.
InParanoid; P05164; -.
KO; K10789; -.
OMA; KVFFASW; -.
OrthoDB; EOG091G02JC; -.
PhylomeDB; P05164; -.
TreeFam; TF314316; -.
BioCyc; MetaCyc:HS00140-MONOMER; -.
BRENDA; 1.11.2.2; 2681.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SIGNOR; P05164; -.
ChiTaRS; MPO; human.
EvolutionaryTrace; P05164; -.
GeneWiki; Myeloperoxidase; -.
GenomeRNAi; 4353; -.
PMAP-CutDB; P05164; -.
PRO; PR:P05164; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000005381; -.
CleanEx; HS_MPO; -.
ExpressionAtlas; P05164; baseline and differential.
Genevisible; P05164; HS.
GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005764; C:lysosome; TAS:ProtInc.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0030141; C:secretory granule; IDA:MGI.
GO; GO:0003682; F:chromatin binding; TAS:ProtInc.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0008201; F:heparin binding; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004601; F:peroxidase activity; IDA:BHF-UCL.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006952; P:defense response; TAS:ProtInc.
GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
GO; GO:0050832; P:defense response to fungus; IEA:Ensembl.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:BHF-UCL.
GO; GO:0002149; P:hypochlorous acid biosynthetic process; IEA:Ensembl.
GO; GO:0034374; P:low-density lipoprotein particle remodeling; IDA:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0055114; P:oxidation-reduction process; IDA:BHF-UCL.
GO; GO:0019430; P:removal of superoxide radicals; IEA:Ensembl.
GO; GO:0002679; P:respiratory burst involved in defense response; IEA:Ensembl.
GO; GO:0032094; P:response to food; IEA:Ensembl.
GO; GO:1990268; P:response to gold nanoparticle; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; TAS:UniProtKB.
GO; GO:0001878; P:response to yeast; IEA:Ensembl.
Gene3D; 1.10.640.10; -; 1.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR019791; Haem_peroxidase_animal.
InterPro; IPR029609; MPO.
PANTHER; PTHR11475:SF93; PTHR11475:SF93; 1.
Pfam; PF03098; An_peroxidase; 1.
PRINTS; PR00457; ANPEROXIDASE.
SUPFAM; SSF48113; SSF48113; 1.
PROSITE; PS00435; PEROXIDASE_1; 1.
PROSITE; PS50292; PEROXIDASE_3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Heme; Hydrogen peroxide; Iron; Lysosome; Metal-binding;
Oxidation; Oxidoreductase; Peroxidase; Polymorphism;
Reference proteome; Signal.
SIGNAL 1 48 {ECO:0000269|PubMed:20332087,
ECO:0000269|PubMed:2154223}.
CHAIN 49 745 89 kDa myeloperoxidase.
/FTId=PRO_0000023651.
CHAIN 155 745 84 kDa myeloperoxidase.
/FTId=PRO_0000023653.
CHAIN 165 745 Myeloperoxidase.
/FTId=PRO_0000023654.
CHAIN 165 278 Myeloperoxidase light chain.
/FTId=PRO_0000023655.
CHAIN 279 745 Myeloperoxidase heavy chain.
/FTId=PRO_0000023656.
ACT_SITE 261 261 Proton acceptor.
METAL 262 262 Calcium.
METAL 334 334 Calcium.
METAL 336 336 Calcium; via carbonyl oxygen.
METAL 338 338 Calcium.
METAL 340 340 Calcium.
METAL 502 502 Iron (heme axial ligand).
BINDING 260 260 Heme (covalent; via 3 links).
BINDING 408 408 Heme (covalent; via 3 links).
BINDING 409 409 Heme (covalent; via 3 links).
SITE 405 405 Transition state stabilizer.
MOD_RES 316 316 Cysteine sulfenic acid (-SOH).
{ECO:0000269|PubMed:7840679}.
CARBOHYD 139 139 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16740002,
ECO:0000269|PubMed:20332087}.
CARBOHYD 355 355 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:20332087}.
CARBOHYD 391 391 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:20332087}.
CARBOHYD 483 483 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:16740002,
ECO:0000269|PubMed:20332087}.
/FTId=CAR_000220.
CARBOHYD 729 729 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20332087}.
DISULFID 167 180
DISULFID 281 291
DISULFID 285 309
DISULFID 319 319 Interchain.
DISULFID 387 398
DISULFID 606 663
DISULFID 704 730
VAR_SEQ 1 95 Missing (in isoform H14).
{ECO:0000303|PubMed:2903767}.
/FTId=VSP_007206.
VAR_SEQ 182 182 N -> NRCGWLGVAAGTGLREASRTPQASRCQRPVLPC
(in isoform H7).
{ECO:0000303|PubMed:2903767}.
/FTId=VSP_007207.
VARIANT 53 53 V -> F (in dbSNP:rs7208693).
{ECO:0000269|Ref.9}.
/FTId=VAR_023995.
VARIANT 173 173 Y -> C (in MPOD; affects proteolytic
processing and secretion;
dbSNP:rs78950939).
{ECO:0000269|PubMed:9637725}.
/FTId=VAR_015377.
VARIANT 251 251 M -> T (in MPOD; dbSNP:rs56378716).
{ECO:0000269|PubMed:9354683}.
/FTId=VAR_015378.
VARIANT 447 447 R -> Q (in a colorectal cancer sample;
somatic mutation; dbSNP:rs762688992).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036517.
VARIANT 569 569 R -> W (in MPOD; suppress post-
translational processing;
dbSNP:rs119468010).
{ECO:0000269|PubMed:7904599,
ECO:0000269|PubMed:8142659,
ECO:0000269|PubMed:8621627}.
/FTId=VAR_015379.
VARIANT 604 604 R -> C (in dbSNP:rs35670089).
{ECO:0000269|Ref.9}.
/FTId=VAR_023996.
VARIANT 683 683 E -> Q (in dbSNP:rs35702888).
{ECO:0000269|Ref.9}.
/FTId=VAR_023997.
VARIANT 717 717 I -> V (in dbSNP:rs2759).
{ECO:0000269|Ref.9}.
/FTId=VAR_012066.
CONFLICT 36 36 L -> V (in Ref. 4; CAA28565 and 7;
CAA33438). {ECO:0000305}.
STRAND 181 185 {ECO:0000244|PDB:5FIW}.
TURN 186 189 {ECO:0000244|PDB:5FIW}.
STRAND 191 194 {ECO:0000244|PDB:5FIW}.
STRAND 206 208 {ECO:0000244|PDB:5FIW}.
STRAND 218 223 {ECO:0000244|PDB:1MYP}.
HELIX 227 234 {ECO:0000244|PDB:5FIW}.
HELIX 239 241 {ECO:0000244|PDB:5FIW}.
STRAND 244 249 {ECO:0000244|PDB:5FIW}.
HELIX 250 263 {ECO:0000244|PDB:5FIW}.
TURN 281 283 {ECO:0000244|PDB:5FIW}.
STRAND 317 319 {ECO:0000244|PDB:5FIW}.
STRAND 323 325 {ECO:0000244|PDB:5FIW}.
STRAND 329 331 {ECO:0000244|PDB:5FIW}.
STRAND 335 338 {ECO:0000244|PDB:5FIW}.
HELIX 340 343 {ECO:0000244|PDB:5FIW}.
HELIX 347 352 {ECO:0000244|PDB:5FIW}.
STRAND 357 360 {ECO:0000244|PDB:5FIW}.
STRAND 371 374 {ECO:0000244|PDB:1MYP}.
HELIX 386 389 {ECO:0000244|PDB:5FIW}.
TURN 392 394 {ECO:0000244|PDB:5FIW}.
STRAND 401 403 {ECO:0000244|PDB:1MYP}.
TURN 404 407 {ECO:0000244|PDB:5FIW}.
HELIX 410 433 {ECO:0000244|PDB:5FIW}.
HELIX 439 460 {ECO:0000244|PDB:5FIW}.
HELIX 463 467 {ECO:0000244|PDB:5FIW}.
HELIX 469 475 {ECO:0000244|PDB:5FIW}.
HELIX 494 497 {ECO:0000244|PDB:5FIW}.
HELIX 498 504 {ECO:0000244|PDB:5FIW}.
STRAND 507 510 {ECO:0000244|PDB:5FIW}.
STRAND 516 518 {ECO:0000244|PDB:5FIW}.
STRAND 523 526 {ECO:0000244|PDB:5FIW}.
HELIX 527 529 {ECO:0000244|PDB:5FIW}.
TURN 530 532 {ECO:0000244|PDB:5FIW}.
HELIX 534 539 {ECO:0000244|PDB:5FIW}.
HELIX 544 551 {ECO:0000244|PDB:5FIW}.
STRAND 552 556 {ECO:0000244|PDB:5FIW}.
HELIX 566 569 {ECO:0000244|PDB:5FIW}.
TURN 573 576 {ECO:0000244|PDB:5FIW}.
STRAND 577 579 {ECO:0000244|PDB:5FIW}.
HELIX 583 593 {ECO:0000244|PDB:5FIW}.
HELIX 599 605 {ECO:0000244|PDB:5FIW}.
HELIX 614 621 {ECO:0000244|PDB:5FIW}.
HELIX 624 634 {ECO:0000244|PDB:5FIW}.
HELIX 637 639 {ECO:0000244|PDB:5FIW}.
HELIX 642 648 {ECO:0000244|PDB:5FIW}.
STRAND 655 657 {ECO:0000244|PDB:5FIW}.
HELIX 659 674 {ECO:0000244|PDB:5FIW}.
TURN 683 685 {ECO:0000244|PDB:1D2V}.
HELIX 688 694 {ECO:0000244|PDB:5FIW}.
HELIX 699 706 {ECO:0000244|PDB:5FIW}.
STRAND 711 713 {ECO:0000244|PDB:5FIW}.
TURN 717 719 {ECO:0000244|PDB:5FIW}.
TURN 723 726 {ECO:0000244|PDB:5FIW}.
STRAND 727 729 {ECO:0000244|PDB:5FIW}.
HELIX 730 732 {ECO:0000244|PDB:5FIW}.
HELIX 739 741 {ECO:0000244|PDB:5FIW}.
SEQUENCE 745 AA; 83869 MW; 348B1CE0A11038B4 CRC64;
MGVPFFSSLR CMVDLGPCWA GGLTAEMKLL LALAGLLAIL ATPQPSEGAA PAVLGEVDTS
LVLSSMEEAK QLVDKAYKER RESIKQRLRS GSASPMELLS YFKQPVAATR TAVRAADYLH
VALDLLERKL RSLWRRPFNV TDVLTPAQLN VLSKSSGCAY QDVGVTCPEQ DKYRTITGMC
NNRRSPTLGA SNRAFVRWLP AEYEDGFSLP YGWTPGVKRN GFPVALARAV SNEIVRFPTD
QLTPDQERSL MFMQWGQLLD HDLDFTPEPA ARASFVTGVN CETSCVQQPP CFPLKIPPND
PRIKNQADCI PFFRSCPACP GSNITIRNQI NALTSFVDAS MVYGSEEPLA RNLRNMSNQL
GLLAVNQRFQ DNGRALLPFD NLHDDPCLLT NRSARIPCFL AGDTRSSEMP ELTSMHTLLL
REHNRLATEL KSLNPRWDGE RLYQEARKIV GAMVQIITYR DYLPLVLGPT AMRKYLPTYR
SYNDSVDPRI ANVFTNAFRY GHTLIQPFMF RLDNRYQPME PNPRVPLSRV FFASWRVVLE
GGIDPILRGL MATPAKLNRQ NQIAVDEIRE RLFEQVMRIG LDLPALNMQR SRDHGLPGYN
AWRRFCGLPQ PETVGQLGTV LRNLKLARKL MEQYGTPNNI DIWMGGVSEP LKRKGRVGPL
LACIIGTQFR KLRDGDRFWW ENEGVFSMQQ RQALAQISLP RIICDNTGIT TVSKNNIFMS
NSYPRDFVNC STLPALNLAS WREAS


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