PERM_HUMAN
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 03-AUG-2022, entry version 236.
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;
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]
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 [24]
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 [25]
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]
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 [27]
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 [28]
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 [29]
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 [30]
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 [31]
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).
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. {ECO:0000269|PubMed:10766826,
CC ECO:0000269|PubMed:20332087}.
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:7904599, ECO:0000269|PubMed:8142659,
CC ECO:0000269|PubMed:8621627, ECO:0000269|PubMed:9354683,
CC ECO:0000269|PubMed:9637725}. Note=The disease is caused by variants
CC affecting the gene represented in this 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";
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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 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 AlphaFoldDB; P05164; -.
DR SASBDB; P05164; -.
DR SMR; P05164; -.
DR BioGRID; 110493; 66.
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; DB00244; Mesalazine.
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 GlyGen; P05164; 8 sites, 36 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; P05164; -.
DR PeptideAtlas; P05164; -.
DR PRIDE; P05164; -.
DR ProteomicsDB; 51811; -. [P05164-1]
DR ProteomicsDB; 51812; -. [P05164-2]
DR ProteomicsDB; 51813; -. [P05164-3]
DR ABCD; P05164; 1 sequenced antibody.
DR Antibodypedia; 3513; 1742 antibodies from 55 providers.
DR CPTC; P05164; 3 antibodies.
DR DNASU; 4353; -.
DR Ensembl; ENST00000225275.4; ENSP00000225275.3; ENSG00000005381.8. [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 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; FSLPYGW; -.
DR OrthoDB; 276568at2759; -.
DR PhylomeDB; P05164; -.
DR TreeFam; TF314316; -.
DR BioCyc; MetaCyc:HS00140-MON; -.
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; 14 hits in 1070 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 100 other tissues.
DR ExpressionAtlas; P05164; baseline and differential.
DR Genevisible; P05164; HS.
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:0007568; P:aging; IEA:Ensembl.
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 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 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 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 BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 338
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 408
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
FT BINDING 409
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /note="covalent"
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 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"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:20332087"
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 /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:7904599,
FT ECO:0000269|PubMed:8142659, 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
