ID PERM_HUMAN Reviewed; 745 AA. AC P05164; A1L4B8; Q14862; Q4PJH5; Q9UCL7; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 27-MAR-2024, entry version 245. DE RecName: Full=Myeloperoxidase; DE Short=MPO; DE EC=1.11.2.2 {ECO:0000269|PubMed:9922160}; DE Contains: DE RecName: Full=Myeloperoxidase; DE Contains: DE RecName: Full=89 kDa myeloperoxidase; DE Contains: DE RecName: Full=84 kDa myeloperoxidase; DE Contains: DE RecName: Full=Myeloperoxidase light chain; DE Contains: DE RecName: Full=Myeloperoxidase heavy chain; DE Flags: Precursor; GN Name=MPO {ECO:0000312|HGNC:HGNC:7218}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17). RX PubMed=3029127; DOI=10.1016/s0021-9258(18)61433-4; RA Morishita K., Kubota N., Asano S., Kaziro Y., Nagata S.; RT "Molecular cloning and characterization of cDNA for human RT myeloperoxidase."; RL J. Biol. Chem. 262:3844-3851(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2444596; DOI=10.1016/s0021-9258(18)48159-8; RA Morishita K., Tsuchiya M., Asano S., Kaziro Y., Nagata S.; RT "Chromosomal gene structure of human myeloperoxidase and regulation of its RT expression by granulocyte colony-stimulating factor."; RL J. Biol. Chem. 262:15208-15213(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17). RX PubMed=3654979; DOI=10.1172/jci113181; RA Seto P., Hirayu H., Magnusson R.P., Gestautas J., Portmann L., RA Degroot L.J., Rapoport B.; RT "Isolation of a complementary DNA clone for thyroid microsomal antigen. RT Homology with the gene for thyroid peroxidase."; RL J. Clin. Invest. 80:1205-1208(1987). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17). RX PubMed=3031585; DOI=10.1093/nar/15.5.2013; RA Johnson K.R., Nauseef W.M., Care A., Wheelock M.J., Shane S., Hudson S., RA Koeffler H.P., Selsted M., Miller C., Rovera G.; RT "Characterization of cDNA clones for human myeloperoxidase: predicted amino RT acid sequence and evidence for multiple mRNA species."; RL Nucleic Acids Res. 15:2013-2028(1987). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS H7; H14 AND H17), AND RP PROTEIN SEQUENCE OF 165-183; 216-222; 295-304; 311-331; 464-479; 662-676 RP AND 766-776. RC TISSUE=Leukemia; RX PubMed=2903767; DOI=10.1021/bi00416a013; RA Hashinaka K., Nishio C., Hur S.-J., Sakiyama F., Tsunasawa S., Yamada M.; RT "Multiple species of myeloperoxidase messenger RNAs produced by alternative RT splicing and differential polyadenylation."; RL Biochemistry 27:5906-5914(1988). RN [6] RP ERRATUM OF PUBMED:2903767. RA Hashinaka K., Nishio C., Hur S.-J., Sakiyama F., Tsunasawa S., Yamada M.; RL Biochemistry 27:9226-9226(1988). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2552418; DOI=10.1093/nar/17.19.7985; RA Johnson K.R., Gemperlein I., Hudson S., Shane S., Rovera G.; RT "Complete nucleotide sequence of the human myeloperoxidase gene."; RL Nucleic Acids Res. 17:7985-7986(1989). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17). RX PubMed=8383257; RA Hosokawa Y., Kawaguchi R., Hikiji K., Yamada M., Suzuki K., Nakagawa T., RA Yoshihara T., Yamaguchi K.; RT "Cloning and characterization of four types of cDNA encoding RT myeloperoxidase from human monocytic leukemia cell line, SKM-1."; RL Leukemia 7:441-445(1993). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-53; CYS-604; GLN-683 RP AND VAL-717. RG NIEHS SNPs program; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM H17). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [12] RP PROTEIN SEQUENCE OF 49-66. RX PubMed=2154223; DOI=10.1016/0006-291x(90)90888-t; RA Yamada M., Hur S.-J., Toda H.; RT "Isolation and characterization of extracellular myeloperoxidase precursor RT in HL-60 cell cultures."; RL Biochem. Biophys. Res. Commun. 166:852-859(1990). RN [13] RP PROTEIN SEQUENCE OF 49-53, SUBUNIT, GLYCOSYLATION AT ASN-323; ASN-355; RP ASN-391; ASN-483 AND ASN-729, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=20332087; DOI=10.1074/jbc.m109.089748; RA Van Antwerpen P., Slomianny M.C., Boudjeltia K.Z., Delporte C., Faid V., RA Calay D., Rousseau A., Moguilevsky N., Raes M., Vanhamme L., RA Furtmueller P.G., Obinger C., Vanhaeverbeek M., Neve J., Michalski J.C.; RT "Glycosylation pattern of mature dimeric leukocyte and recombinant RT monomeric myeloperoxidase: glycosylation is required for optimal enzymatic RT activity."; RL J. Biol. Chem. 285:16351-16359(2010). RN [14] RP PROTEIN SEQUENCE OF 279-424. RC TISSUE=Leukocyte; RX PubMed=1334087; DOI=10.1016/s0021-9258(19)74037-x; RA Taylor K.L., Pohl J., Kinkade J.M. Jr.; RT "Unique autolytic cleavage of human myeloperoxidase. Implications for the RT involvement of active site MET409."; RL J. Biol. Chem. 267:25282-25288(1992). RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 548-629. RX PubMed=8390465; DOI=10.1016/s0021-9258(19)38674-0; RA Yamada M., Yoshida M., Hashinaka K.; RT "Identification of transcriptional cis-elements in introns 7 and 9 of the RT myeloperoxidase gene."; RL J. Biol. Chem. 268:13479-13485(1993). RN [16] RP NUCLEOTIDE SEQUENCE [MRNA] OF 588-745. RX PubMed=2884926; DOI=10.1016/0003-9861(87)90304-3; RA Yamada M., Hur S.-J., Hashinaka K., Tsuneoka K., Saeki T., Nishio C., RA Sakiyama F., Tsunasawa S.; RT "Isolation and characterization of a cDNA coding for human RT myeloperoxidase."; RL Arch. Biochem. Biophys. 255:147-155(1987). RN [17] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=9922160; DOI=10.1021/bi9818772; RA Furtmueller P.G., Burner U., Obinger C.; RT "Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and RT thiocyanate."; RL Biochemistry 37:17923-17930(1998). RN [18] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-139 AND ASN-483. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [19] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323 AND ASN-483. RC TISSUE=Saliva; RX PubMed=16740002; DOI=10.1021/pr050492k; RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.; RT "Identification of N-linked glycoproteins in human saliva by glycoprotein RT capture and mass spectrometry."; RL J. Proteome Res. 5:1493-1503(2006). RN [20] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-355 AND ASN-391. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [22] RP FUNCTION. RX PubMed=25698971; DOI=10.3389/fphys.2015.00011; RA Cederlund M., Deronic A., Pallon J., Soerensen O.E., Aakerstroem B.; RT "A1M/alpha1-microglobulin is proteolytically activated by myeloperoxidase, RT binds its heme group and inhibits low density lipoprotein oxidation."; RL Front. Physiol. 6:11-11(2015). RN [23] {ECO:0007744|PDB:1MHL} RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 167-744, AND OXIDATION AT RP CYS-316. RX PubMed=7840679; DOI=10.1006/abbi.1995.1086; RA Fenna R.E., Zeng J., Davey C.; RT "Structure of the green heme in myeloperoxidase."; RL Arch. Biochem. Biophys. 316:653-656(1995). RN [24] {ECO:0007744|PDB:1CXP, ECO:0007744|PDB:1D2V} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 167-744, AND SUBUNIT. RX PubMed=10766826; DOI=10.1074/jbc.275.16.11964; RA Fiedler T.J., Davey C.A., Fenna R.E.; RT "X-ray crystal structure and characterization of halide-binding sites of RT human myeloperoxidase at 1.8-A resolution."; RL J. Biol. Chem. 275:11964-11971(2000). RN [25] {ECO:0007744|PDB:1D5L, ECO:0007744|PDB:1D7W, ECO:0007744|PDB:1DNU, ECO:0007744|PDB:1DNW} RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 167-744. RX PubMed=11705390; DOI=10.1021/bi0111808; RA Blair-Johnson M., Fiedler T., Fenna R.; RT "Human myeloperoxidase: structure of a cyanide complex and its interaction RT with bromide and thiocyanate substrates at 1.9 A resolution."; RL Biochemistry 40:13990-13997(2001). RN [26] {ECO:0007744|PDB:4EJX} RP X-RAY CRYSTALLOGRAPHY (4.69 ANGSTROMS) OF 165-278 AND 279-745 IN COMPLEX RP WITH HEME B AND CP, GLYCOSYLATION AT ASN-355; ASN-391 AND ASN-483, AND RP INTERACTION WITH CP. RX PubMed=23843990; DOI=10.1371/journal.pone.0067145; RA Samygina V.R., Sokolov A.V., Bourenkov G., Petoukhov M.V., Pulina M.O., RA Zakharova E.T., Vasilyev V.B., Bartunik H., Svergun D.I.; RT "Ceruloplasmin: macromolecular assemblies with iron-containing acute phase RT proteins."; RL PLoS ONE 8:e67145-e67145(2013). RN [27] RP VARIANT MPOD TRP-569. RX PubMed=8142659; RA Kizaki M., Miller C.W., Selsted M.E., Koeffler H.P.; RT "Myeloperoxidase (MPO) gene mutation in hereditary MPO deficiency."; RL Blood 83:1935-1940(1994). RN [28] RP VARIANT MPOD TRP-569. RX PubMed=7904599; DOI=10.1016/s0021-9258(17)42244-7; RA Nauseef W.M., Brigham S., Cogley M.; RT "Hereditary myeloperoxidase deficiency due to a missense mutation of RT arginine 569 to tryptophan."; RL J. Biol. Chem. 269:1212-1216(1994). RN [29] RP CHARACTERIZATION OF VARIANT MPOD TRP-569. RX PubMed=8621627; DOI=10.1074/jbc.271.16.9546; RA Nauseef W., Cogley M., McCormick S.; RT "Effect of the R569W missense mutation on the biosynthesis of RT myeloperoxidase."; RL J. Biol. Chem. 271:9546-9549(1996). RN [30] RP VARIANT MPOD CYS-173, AND CHARACTERIZATION OF VARIANT MPOD CYS-173. RX PubMed=9637725; DOI=10.1172/jci2649; RA DeLeo F.R., Goedken M., McCormick S.J., Nauseef W.M.; RT "A novel form of hereditary myeloperoxidase deficiency linked to RT endoplasmic reticulum/proteasome degradation."; RL J. Clin. Invest. 101:2900-2909(1998). RN [31] RP VARIANT MPOD THR-251. RX PubMed=9354683; RA Romano M., Dri P., Dadalt L., Patriarca P., Baralle F.E.; RT "Biochemical and molecular characterization of hereditary myeloperoxidase RT deficiency."; RL Blood 90:4126-4134(1997). RN [32] RP VARIANT [LARGE SCALE ANALYSIS] GLN-447. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [33] RP VARIANT MPOD TRP-569. RX PubMed=37198333; DOI=10.1007/s00439-023-02569-7; RA Smits D.J., Schot R., Popescu C.A., Dias K.R., Ades L., Briere L.C., RA Sweetser D.A., Kushima I., Aleksic B., Khan S., Karageorgou V., Ordonez N., RA Sleutels F.J.G.T., van der Kaay D.C.M., Van Mol C., Van Esch H., RA Bertoli-Avella A.M., Roscioli T., Mancini G.M.S.; RT "De novo MCM6 variants in neurodevelopmental disorders: a recognizable RT phenotype related to zinc binding residues."; RL Hum. Genet. 0:0-0(2023). 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:9922160). 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 (PubMed:25698971). CC {ECO:0000269|PubMed:25698971, ECO:0000269|PubMed:9922160}. 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:9922160}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Binds 1 Ca(2+) ion per monomer.; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per CC monomer.; CC -!- SUBUNIT: Homodimer; disulfide-linked. Each monomer consists of a light CC and a heavy chain. Found in a complex with CP and LTF; interacts CC directly with CP, which protects CP antioxidant properties by MPO CC (PubMed:23843990). {ECO:0000269|PubMed:10766826, CC ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990}. CC -!- INTERACTION: CC P05164; P27918: CFP; NbExp=4; IntAct=EBI-2556173, EBI-9038570; CC P05164; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-2556173, EBI-357085; CC -!- SUBCELLULAR LOCATION: Lysosome. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=H17; Synonyms=B; CC IsoId=P05164-1; Sequence=Displayed; CC Name=H14; CC IsoId=P05164-2; Sequence=VSP_007206; CC Name=H7; Synonyms=A; CC IsoId=P05164-3; Sequence=VSP_007207; CC -!- DISEASE: Myeloperoxidase deficiency (MPOD) [MIM:254600]: A disorder CC characterized by decreased myeloperoxidase activity in neutrophils and CC monocytes that results in disseminated candidiasis. CC {ECO:0000269|PubMed:37198333, ECO:0000269|PubMed:7904599, CC ECO:0000269|PubMed:8142659, ECO:0000269|PubMed:8621627, CC ECO:0000269|PubMed:9354683, ECO:0000269|PubMed:9637725}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00298}. CC -!- WEB RESOURCE: Name=MPObase; Note=MPO mutation db; CC URL="http://structure.bmc.lu.se/idbase/MPObase/"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/mpo/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Myeloperoxidase entry; CC URL="https://en.wikipedia.org/wiki/Myeloperoxidase"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J02694; AAA59896.1; -; mRNA. DR EMBL; M17176; AAA60346.1; -; Genomic_DNA. DR EMBL; M17170; AAA60346.1; JOINED; Genomic_DNA. DR EMBL; M17171; AAA60346.1; JOINED; Genomic_DNA. DR EMBL; M17172; AAA60346.1; JOINED; Genomic_DNA. DR EMBL; M17173; AAA60346.1; JOINED; Genomic_DNA. DR EMBL; M17174; AAA60346.1; JOINED; Genomic_DNA. DR EMBL; M17175; AAA60346.1; JOINED; Genomic_DNA. DR EMBL; X04876; CAA28565.1; -; mRNA. DR EMBL; M19507; AAA59863.1; -; mRNA. DR EMBL; M19508; AAA59864.1; -; Genomic_DNA. DR EMBL; M19508; AAA59865.1; -; Genomic_DNA. DR EMBL; X15377; CAA33438.1; -; Genomic_DNA. DR EMBL; S56200; AAB25582.1; -; mRNA. DR EMBL; DQ088846; AAY68218.1; -; Genomic_DNA. DR EMBL; CH471109; EAW94470.1; -; Genomic_DNA. DR EMBL; BC130476; AAI30477.1; -; mRNA. DR EMBL; D14466; BAA03362.1; -; Genomic_DNA. DR CCDS; CCDS11604.1; -. [P05164-1] DR PIR; A29467; OPHUM. DR PIR; B28894; B28894. DR PIR; D28894; D28894. DR RefSeq; NP_000241.1; NM_000250.1. [P05164-1] DR PDB; 1CXP; X-ray; 1.80 A; A/B=167-270, C/D=279-744. DR PDB; 1D2V; X-ray; 1.75 A; A/B=167-270, C/D=279-744. DR PDB; 1D5L; X-ray; 1.90 A; A/B=167-270, C/D=279-744. DR PDB; 1D7W; X-ray; 1.90 A; A/B=167-270, C/D=279-744. DR PDB; 1DNU; X-ray; 1.85 A; A/B=167-270, C/D=279-744. DR PDB; 1DNW; X-ray; 1.90 A; A/B=167-270, C/D=279-744. DR PDB; 1MHL; X-ray; 2.25 A; A/B=165-272, C/D=279-744. DR PDB; 1MYP; X-ray; 3.00 A; A/B=165-272, C/D=279-744. DR PDB; 3F9P; X-ray; 2.93 A; A/B=165-278, C/D=279-745. DR PDB; 3ZS0; X-ray; 2.30 A; A/B=165-272, C/D=279-745. DR PDB; 3ZS1; X-ray; 2.60 A; A/B=165-278, C/D=279-745. DR PDB; 4C1M; X-ray; 2.00 A; A/B=165-272, C/D=279-745. DR 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. DR PDB; 4EJX; X-ray; 4.69 A; B=165-278, D=279-745. DR PDB; 5FIW; X-ray; 1.70 A; A/B=167-271, C/D=279-744. DR PDB; 5MFA; X-ray; 1.20 A; A=49-745. DR PDB; 5UZU; X-ray; 2.40 A; A=167-744. DR PDB; 6AZP; X-ray; 2.29 A; A=167-743. DR PDB; 6BMT; X-ray; 2.40 A; A=1-745. DR PDB; 7OIH; X-ray; 2.60 A; A/B/C/D/E/F/G/H=166-744. DR PDBsum; 1CXP; -. DR PDBsum; 1D2V; -. DR PDBsum; 1D5L; -. DR PDBsum; 1D7W; -. DR PDBsum; 1DNU; -. DR PDBsum; 1DNW; -. DR PDBsum; 1MHL; -. DR PDBsum; 1MYP; -. DR PDBsum; 3F9P; -. DR PDBsum; 3ZS0; -. DR PDBsum; 3ZS1; -. DR PDBsum; 4C1M; -. DR PDBsum; 4DL1; -. DR PDBsum; 4EJX; -. DR PDBsum; 5FIW; -. DR PDBsum; 5MFA; -. DR PDBsum; 5UZU; -. DR PDBsum; 6AZP; -. DR PDBsum; 6BMT; -. DR PDBsum; 7OIH; -. DR AlphaFoldDB; P05164; -. DR SASBDB; P05164; -. DR SMR; P05164; -. DR BioGRID; 110493; 71. DR CORUM; P05164; -. DR IntAct; P05164; 22. DR MINT; P05164; -. DR STRING; 9606.ENSP00000225275; -. DR BindingDB; P05164; -. DR ChEMBL; CHEMBL2439; -. DR DrugBank; DB06111; AB192. DR DrugBank; DB00233; Aminosalicylic acid. DR DrugBank; DB00006; Bivalirudin. DR DrugBank; DB02300; Calcipotriol. DR DrugBank; DB06774; Capsaicin. DR DrugBank; DB00958; Carboplatin. DR DrugBank; DB06468; Cariporide. DR DrugBank; DB00833; Cefaclor. DR DrugBank; DB00535; Cefdinir. DR DrugBank; DB00515; Cisplatin. DR DrugBank; DB00847; Cysteamine. DR DrugBank; DB00250; Dapsone. DR DrugBank; DB05161; Elafin. DR DrugBank; DB01225; Enoxaparin. DR DrugBank; DB00583; Levocarnitine. DR DrugBank; DB01065; Melatonin. DR DrugBank; DB00461; Nabumetone. DR DrugBank; DB04821; Nomifensine. DR DrugBank; DB00104; Octreotide. DR DrugBank; DB00526; Oxaliplatin. DR DrugBank; DB00550; Propylthiouracil. DR DrugBank; DB00208; Ticlopidine. DR DrugBank; DB06823; Tiopronin. DR DrugBank; DB00500; Tolmetin. DR DrugBank; DB04827; Urethane. DR DrugCentral; P05164; -. DR GuidetoPHARMACOLOGY; 2789; -. DR PeroxiBase; 3315; HsMPO. DR GlyConnect; 428; 30 N-Linked glycans (5 sites), 2 O-Linked glycans (2 sites). DR GlyCosmos; P05164; 8 sites, 38 glycans. DR GlyGen; P05164; 8 sites, 37 N-linked glycans (5 sites), 2 O-linked glycans (2 sites). DR iPTMnet; P05164; -. DR PhosphoSitePlus; P05164; -. DR SwissPalm; P05164; -. DR BioMuta; MPO; -. DR DMDM; 129825; -. DR EPD; P05164; -. DR jPOST; P05164; -. DR MassIVE; P05164; -. DR PaxDb; 9606-ENSP00000225275; -. DR PeptideAtlas; P05164; -. DR PRIDE; P05164; -. DR ProteomicsDB; 51811; -. [P05164-1] DR ProteomicsDB; 51812; -. [P05164-2] DR ProteomicsDB; 51813; -. [P05164-3] DR Pumba; P05164; -. DR ABCD; P05164; 1 sequenced antibody. DR Antibodypedia; 3513; 2060 antibodies from 55 providers. DR CPTC; P05164; 3 antibodies. DR DNASU; 4353; -. DR Ensembl; ENST00000225275.4; ENSP00000225275.3; ENSG00000005381.9. [P05164-1] DR GeneID; 4353; -. DR KEGG; hsa:4353; -. DR MANE-Select; ENST00000225275.4; ENSP00000225275.3; NM_000250.2; NP_000241.1. DR UCSC; uc002ivu.1; human. [P05164-1] DR AGR; HGNC:7218; -. DR CTD; 4353; -. DR DisGeNET; 4353; -. DR GeneCards; MPO; -. DR HGNC; HGNC:7218; MPO. DR HPA; ENSG00000005381; Tissue enriched (bone). DR MalaCards; MPO; -. DR MIM; 254600; phenotype. DR MIM; 606989; gene. DR neXtProt; NX_P05164; -. DR OpenTargets; ENSG00000005381; -. DR Orphanet; 2587; Myeloperoxidase deficiency. DR PharmGKB; PA243; -. DR VEuPathDB; HostDB:ENSG00000005381; -. DR eggNOG; KOG2408; Eukaryota. DR GeneTree; ENSGT00940000161343; -. DR HOGENOM; CLU_006087_1_1_1; -. DR InParanoid; P05164; -. DR OMA; RYQPMGP; -. DR OrthoDB; 4560at2759; -. DR PhylomeDB; P05164; -. DR TreeFam; TF314316; -. DR BioCyc; MetaCyc:HS00140-MONOMER; -. DR BRENDA; 1.11.2.2; 2681. DR PathwayCommons; P05164; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-8941413; Events associated with phagocytolytic activity of PMN cells. DR SignaLink; P05164; -. DR SIGNOR; P05164; -. DR BioGRID-ORCS; 4353; 15 hits in 1153 CRISPR screens. DR ChiTaRS; MPO; human. DR EvolutionaryTrace; P05164; -. DR GeneWiki; Myeloperoxidase; -. DR GenomeRNAi; 4353; -. DR Pharos; P05164; Tchem. DR PRO; PR:P05164; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P05164; Protein. DR Bgee; ENSG00000005381; Expressed in trabecular bone tissue and 101 other cell types or tissues. DR ExpressionAtlas; P05164; baseline and differential. DR GO; GO:0042582; C:azurophil granule; IDA:UniProtKB. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005764; C:lysosome; TAS:ProtInc. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0097013; C:phagocytic vesicle lumen; TAS:Reactome. DR GO; GO:0030141; C:secretory granule; IDA:MGI. DR GO; GO:0003682; F:chromatin binding; TAS:ProtInc. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0008201; F:heparin binding; IDA:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004601; F:peroxidase activity; IDA:BHF-UCL. DR GO; GO:0006952; P:defense response; TAS:ProtInc. DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central. DR GO; GO:0050832; P:defense response to fungus; IEA:Ensembl. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:BHF-UCL. DR GO; GO:0002149; P:hypochlorous acid biosynthetic process; IEA:Ensembl. DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IDA:BHF-UCL. DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc. DR GO; GO:0019430; P:removal of superoxide radicals; IEA:Ensembl. DR GO; GO:0002679; P:respiratory burst involved in defense response; IEA:Ensembl. 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; TAS:UniProtKB. DR GO; GO:0001878; P:response to yeast; IEA:Ensembl. DR CDD; cd09824; myeloperoxidase_like; 1. DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1. DR InterPro; IPR019791; Haem_peroxidase_animal. DR InterPro; IPR010255; Haem_peroxidase_sf. DR InterPro; IPR037120; Haem_peroxidase_sf_animal. DR PANTHER; PTHR11475:SF108; MYELOPEROXIDASE; 1. DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1. DR Pfam; PF03098; An_peroxidase; 1. DR PRINTS; PR00457; ANPEROXIDASE. DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1. DR PROSITE; PS00435; PEROXIDASE_1; 1. DR PROSITE; PS50292; PEROXIDASE_3; 1. DR Genevisible; P05164; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Direct protein sequencing; KW Disease variant; Disulfide bond; Glycoprotein; Heme; Hydrogen peroxide; KW Iron; Lysosome; Metal-binding; Oxidation; Oxidoreductase; Peroxidase; KW Reference proteome; Signal. FT SIGNAL 1..48 FT /evidence="ECO:0000269|PubMed:20332087, FT ECO:0000269|PubMed:2154223" FT CHAIN 49..745 FT /note="89 kDa myeloperoxidase" FT /id="PRO_0000023651" FT CHAIN 155..745 FT /note="84 kDa myeloperoxidase" FT /id="PRO_0000023653" FT CHAIN 165..745 FT /note="Myeloperoxidase" FT /id="PRO_0000023654" FT CHAIN 165..278 FT /note="Myeloperoxidase light chain" FT /id="PRO_0000023655" FT CHAIN 279..745 FT /note="Myeloperoxidase heavy chain" FT /id="PRO_0000023656" FT ACT_SITE 261 FT /note="Proton acceptor" FT BINDING 260 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:23843990, FT ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, FT ECO:0007744|PDB:4EJX" FT BINDING 262 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 334 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:10766826, FT ECO:0000269|PubMed:11705390, ECO:0000269|PubMed:7840679, FT ECO:0007744|PDB:1CXP, ECO:0007744|PDB:1D2V, FT ECO:0007744|PDB:1D7W, ECO:0007744|PDB:1DNU, FT ECO:0007744|PDB:1DNW, ECO:0007744|PDB:1MHL" FT BINDING 336 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:10766826, FT ECO:0000269|PubMed:11705390, ECO:0000269|PubMed:7840679, FT ECO:0007744|PDB:1CXP, ECO:0007744|PDB:1D2V, FT ECO:0007744|PDB:1D7W, ECO:0007744|PDB:1DNU, FT ECO:0007744|PDB:1DNW, ECO:0007744|PDB:1MHL" FT BINDING 338 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:10766826, FT ECO:0000269|PubMed:11705390, ECO:0000269|PubMed:7840679, FT ECO:0007744|PDB:1CXP, ECO:0007744|PDB:1D2V, FT ECO:0007744|PDB:1D7W, ECO:0007744|PDB:1DNU, FT ECO:0007744|PDB:1DNW, ECO:0007744|PDB:1MHL" FT BINDING 340 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:10766826, FT ECO:0000269|PubMed:11705390, ECO:0000269|PubMed:7840679, FT ECO:0007744|PDB:1CXP, ECO:0007744|PDB:1D2V, FT ECO:0007744|PDB:1D7W, ECO:0007744|PDB:1DNU, FT ECO:0007744|PDB:1DNW, ECO:0007744|PDB:1MHL" FT BINDING 408 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:23843990, FT ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, FT ECO:0007744|PDB:4EJX" FT BINDING 409 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:23843990, FT ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, FT ECO:0007744|PDB:4EJX" FT BINDING 502 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:0000269|PubMed:23843990, FT ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, FT ECO:0007744|PDB:4EJX" FT SITE 405 FT /note="Transition state stabilizer" FT MOD_RES 316 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000269|PubMed:7840679" FT CARBOHYD 139 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 323 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16740002, FT ECO:0000269|PubMed:20332087" FT CARBOHYD 355 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, FT ECO:0007744|PDB:4EJX" FT CARBOHYD 391 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, FT ECO:0007744|PDB:4EJX" FT CARBOHYD 483 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087, FT ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4EJX" FT /id="CAR_000220" FT CARBOHYD 729 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:20332087" FT DISULFID 167..180 FT DISULFID 281..291 FT DISULFID 285..309 FT DISULFID 319 FT /note="Interchain" FT DISULFID 387..398 FT DISULFID 606..663 FT DISULFID 704..730 FT VAR_SEQ 1..95 FT /note="Missing (in isoform H14)" FT /evidence="ECO:0000303|PubMed:2903767" FT /id="VSP_007206" FT VAR_SEQ 182 FT /note="N -> NRCGWLGVAAGTGLREASRTPQASRCQRPVLPC (in isoform FT H7)" FT /evidence="ECO:0000303|PubMed:2903767" FT /id="VSP_007207" FT VARIANT 53 FT /note="V -> F (in dbSNP:rs7208693)" FT /evidence="ECO:0000269|Ref.9" FT /id="VAR_023995" FT VARIANT 173 FT /note="Y -> C (in MPOD; affects proteolytic processing and FT secretion; dbSNP:rs78950939)" FT /evidence="ECO:0000269|PubMed:9637725" FT /id="VAR_015377" FT VARIANT 251 FT /note="M -> T (in MPOD; dbSNP:rs56378716)" FT /evidence="ECO:0000269|PubMed:9354683" FT /id="VAR_015378" FT VARIANT 447 FT /note="R -> Q (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs762688992)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036517" FT VARIANT 569 FT /note="R -> W (in MPOD; suppress post-translational FT processing; dbSNP:rs119468010)" FT /evidence="ECO:0000269|PubMed:37198333, FT ECO:0000269|PubMed:7904599, ECO:0000269|PubMed:8142659, FT ECO:0000269|PubMed:8621627" FT /id="VAR_015379" FT VARIANT 604 FT /note="R -> C (in dbSNP:rs35670089)" FT /evidence="ECO:0000269|Ref.9" FT /id="VAR_023996" FT VARIANT 683 FT /note="E -> Q (in dbSNP:rs35702888)" FT /evidence="ECO:0000269|Ref.9" FT /id="VAR_023997" FT VARIANT 717 FT /note="I -> V (in dbSNP:rs2759)" FT /evidence="ECO:0000269|Ref.9" FT /id="VAR_012066" FT CONFLICT 36 FT /note="L -> V (in Ref. 4; CAA28565 and 7; CAA33438)" FT /evidence="ECO:0000305" FT TURN 159..164 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 181..185 FT /evidence="ECO:0007829|PDB:5MFA" FT TURN 186..189 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 191..194 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 218..223 FT /evidence="ECO:0007829|PDB:1MYP" FT HELIX 227..234 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 239..241 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 244..249 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 250..263 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 271..275 FT /evidence="ECO:0007829|PDB:5MFA" FT TURN 281..283 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 317..319 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 323..325 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 329..331 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 335..338 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 340..343 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 347..352 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 357..360 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 371..374 FT /evidence="ECO:0007829|PDB:1MYP" FT HELIX 387..389 FT /evidence="ECO:0007829|PDB:5MFA" FT TURN 392..394 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 401..403 FT /evidence="ECO:0007829|PDB:1MYP" FT TURN 404..407 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 410..433 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 439..460 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 463..467 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 469..475 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 492..497 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 498..504 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 507..510 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 516..518 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 523..526 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 527..529 FT /evidence="ECO:0007829|PDB:5MFA" FT TURN 530..532 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 534..539 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 544..552 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 553..556 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 566..569 FT /evidence="ECO:0007829|PDB:5MFA" FT TURN 573..576 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 577..579 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 583..593 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 599..605 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 614..621 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 624..634 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 637..639 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 642..648 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 655..657 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 659..674 FT /evidence="ECO:0007829|PDB:5MFA" FT TURN 683..685 FT /evidence="ECO:0007829|PDB:1D2V" FT HELIX 688..694 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 699..706 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 711..713 FT /evidence="ECO:0007829|PDB:5MFA" FT TURN 717..719 FT /evidence="ECO:0007829|PDB:5MFA" FT TURN 723..726 FT /evidence="ECO:0007829|PDB:5MFA" FT STRAND 727..729 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 730..732 FT /evidence="ECO:0007829|PDB:5MFA" FT HELIX 739..741 FT /evidence="ECO:0007829|PDB:5MFA" SQ 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 //