ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P05164


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PERM_HUMAN
Primary accession number P05164
Secondary accession numbers Q14862 Q4PJH5
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 109)
Name and origin of the protein
Protein name Myeloperoxidase [Precursor]
Synonyms MPO
EC 1.11.1.7
Contains 89 kDa myeloperoxidase
84 kDa myeloperoxidase
Myeloperoxidase light chain
Myeloperoxidase heavy chain
Gene name
Name: MPO
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
PubMed=3029127 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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).
DOI=10.1093/nar/15.5.2013; PubMed=3031585 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1093/nar/17.19.7985; PubMed=2552418 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
PubMed=3654979 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
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;
DOI=10.1021/bi00416a013; PubMed=2903767 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
ERRATUM.
Hashinaka K., Nishio C., Hur S.-J., Sakiyama F., Tsunasawa S., Yamada M.;
Biochemistry 27:9226-9226(1988).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
PubMed=8383257 [NCBI, ExPASy, EBI, Israel, Japan]
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.
Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N., Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 548-629.
PubMed=8390465 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 588-745.
DOI=10.1016/0003-9861(87)90304-3; PubMed=2884926 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
PROTEIN SEQUENCE OF N-TERMINUS, AND PROTEIN SEQUENCE OF 49-68.
DOI=10.1016/0006-291X(90)90888-T; PubMed=2154223 [NCBI, ExPASy, EBI, Israel, Japan]
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]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-139 AND ASN-483, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323 AND ASN-483, AND MASS SPECTROMETRY.
TISSUE=Saliva;
DOI=10.1021/pr050492k; PubMed=16740002 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 167-744.
DOI=10.1074/jbc.275.16.11964; PubMed=10766826 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[16]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 167-744.
DOI=10.1006/abbi.1995.1086; PubMed=7840679 [NCBI, ExPASy, EBI, Israel, Japan]
Fenna R.E., Zeng J., Davey C.;
"Structure of the green heme in myeloperoxidase.";
Arch. Biochem. Biophys. 316:653-656(1995).
[17]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 167-744.
DOI=10.1021/bi0111808; PubMed=11705390 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[18]
VARIANT MPD TRP-569.
PubMed=8142659 [NCBI, ExPASy, EBI, Israel, Japan]
Kizaki M., Miller C.W., Selsted M.E., Koeffler H.P.;
"Myeloperoxidase (MPO) gene mutation in hereditary MPO deficiency.";
Blood 83:1935-1940(1994).
[19]
VARIANT MPD TRP-569.
PubMed=7904599 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[20]
CHARACTERIZATION OF VARIANT MPD TRP-569.
DOI=10.1074/jbc.271.16.9546; PubMed=8621627 [NCBI, ExPASy, EBI, Israel, Japan]
Nauseef W., Cogley M., McCormick S.;
"Effect of the R569W missense mutation on the biosynthesis of myeloperoxidase.";
J. Biol. Chem. 271:9546-9549(1996).
[21]
VARIANT MPD CYS-173, AND CHARACTERIZATION OF VARIANT MPD CYS-173.
PubMed=9637725 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[22]
VARIANT MPD THR-251.
PubMed=9354683 [NCBI, ExPASy, EBI, Israel, Japan]
Romano M., Dri P., Dadalt L., Patriarca P., Baralle F.E.;
"Biochemical and molecular characterization of hereditary myeloperoxidase deficiency.";
Blood 90:4126-4134(1997).
[23]
VARIANT [LARGE SCALE ANALYSIS] GLN-447.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J02694; AAA59896.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17176; AAA60346.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17170; AAA60346.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17171; AAA60346.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17172; AAA60346.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17173; AAA60346.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17174; AAA60346.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17175; AAA60346.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04876; CAA28565.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15377; CAA33438.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19507; AAA59863.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19508; AAA59864.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19508; AAA59865.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S56200; AAB25582.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ088846; AAY68218.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D14466; BAA03362.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A29467; OPHUM.
B28894; B28894.
D28894; D28894.
RefSeq NP_000241.1; -.
UniGene Hs.458272
3D structure databases
PDB
1CXP; X-ray; 1.80 A; A/B=167-270, C/D=279-744.[ExPASy / RCSB / EBI]
1D2V; X-ray; 1.75 A; A/B=167-270, C/D=279-744.[ExPASy / RCSB / EBI]
1D5L; X-ray; 1.90 A; A/B=167-270, C/D=279-744.[ExPASy / RCSB / EBI]
1D7W; X-ray; 1.90 A; A/B=167-270, C/D=279-744.[ExPASy / RCSB / EBI]
1DNU; X-ray; 1.85 A; A/B=167-270, C/D=279-744.[ExPASy / RCSB / EBI]
1DNW; X-ray; 1.90 A; A/B=167-270, C/D=279-744.[ExPASy / RCSB / EBI]
1MHL; X-ray; 2.25 A; A/B=165-272, C/D=279-744.[ExPASy / RCSB / EBI]
1MYP; X-ray; 3.00 A; A/B=165-272, C/D=279-744.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1CXP; -.
1D2V; -.
1D5L; -.
1D7W; -.
1DNU; -.
1DNW; -.
1MHL; -.
1MYP; -.
ModBase P05164.
Protein family/group databases
PeroxiBase 3315; HsMPO.
PTM databases
GlycoSuiteDB P05164; -.
PhosphoSite P05164; -.
Polymorphism databases
NIEHS-SNPs MPO.
Organism-specific databases
H-InvDB HIX0039242; -.
HGNC HGNC:7218; MPO.
GeneLynx MPO; Homo sapiens.
GenAtlas MPO.
HPA CAB000059; -.
MIM 254600; phenotype. [NCBI / EBI]
606989; gene. [NCBI / EBI]
Orphanet 2587; Myeloperoxidase deficiency.
PharmGKB PA243; -.
GeneCards P05164.
Gene expression databases
ArrayExpress P05164; -.
CleanEx HS_MPO; -.
GermOnline ENSG00000005381; Homo sapiens.
Ontologies
GO
GO:0005764; Cellular component: lysosome (traceable author statement from ProtInc).
GO:0005634; Cellular component: nucleus (traceable author statement from ProtInc).
GO:0003682; Molecular function: chromatin binding (traceable author statement from ProtInc).
GO:0004601; Molecular function: peroxidase activity (traceable author statement from ProtInc).
GO:0006916; Biological process: anti-apoptosis (traceable author statement from ProtInc).
GO:0006952; Biological process: defense response (traceable author statement from ProtInc).
GO:0006979; Biological process: response to oxidative stress (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR002007; Haem_peroxidase_animal.
IPR002016; Haem_peroxidase_pln/fun/bac.
Graphical view of domain structure.
Gene3D G3DSA:1.10.640.10; Haem_peroxidase_animal; 1.
Pfam PF03098; An_peroxidase; 1.
Pfam graphical view of domain structure.
PRINTS PR00457; ANPEROXIDASE.
PROSITE PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; FALSE_NEG.
PS50292; PEROXIDASE_3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P05164.
Genome annotation databases
Ensembl ENSG00000005381; Homo sapiens. [Contig view]
GeneID 4353; -.
KEGG hsa:4353; -.
Phylogenomic databases
HOVERGEN P05164; -.
Other
DrugBank DB00535; Cefdinir.
LinkHub P05164; -.
SOURCE MPO; Homo sapiens.
ProtoNet P05164.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Calcium; Direct protein sequencing; Disease mutation; Glycoprotein; Heme; Hydrogen peroxide; Iron; Lysosome; Metal-binding; Oxidation; Oxidoreductase; Peroxidase; Polymorphism; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    48  48      
CHAIN   49   745  697     89 kDa myeloperoxidase. PRO_0000023651
PROPEP   49   164  116      PRO_0000023652
CHAIN   155   745  591     84 kDa myeloperoxidase. PRO_0000023653
CHAIN   165   745  581     Myeloperoxidase. PRO_0000023654
CHAIN   165   278  114     Myeloperoxidase light chain. PRO_0000023655
CHAIN   279   745  467     Myeloperoxidase heavy chain. 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  1     Transition state stabilizer. 
MOD_RES   316   316        Cysteine sulfenic acid (-SOH). 
CARBOHYD   139   139        N-linked (GlcNAc...). 
CARBOHYD   323   323        N-linked (GlcNAc...). 
CARBOHYD   355   355        N-linked (GlcNAc...). 
CARBOHYD   391   391        N-linked (GlcNAc...). 
CARBOHYD   483   483        N-linked (GlcNAc...) [GlycoSuiteDB]. CAR_000220
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). VSP_007206
VAR_SEQ   182   182        N -> NRCGWLGVAAGTGLREASRTPQASRCQRPVLPC (in isoform H7). VSP_007207
VARIANT   53    53  1     V -> F (in dbSNP:rs7208693 [NCBI]). VAR_023995 
VARIANT   173   173  1     Y -> C (in MPD; affects proteolytic processing and secretion). VAR_015377 [3D]
VARIANT   251   251  1     M -> T (in MPD). VAR_015378 [3D]
VARIANT   447   447  1     R -> Q (in a colorectal cancer sample; somatic mutation). VAR_036517 [3D]
VARIANT   569   569  1     R -> W (in MPD; suppress post-translational processing). VAR_015379 [3D]
VARIANT   604   604  1     R -> C. VAR_023996 [3D]
VARIANT   683   683  1     E -> Q. VAR_023997 [3D]
VARIANT   717   717  1     I -> V (in dbSNP:rs2759 [NCBI]). VAR_012066 [3D]
CONFLICT   36    36        L -> V (in Ref. 3 and 4). 
STRAND   181   185  5      
TURN   186   189  4      
STRAND   191   194  4      
STRAND   206   208  3      
HELIX   227   234  8      
HELIX   239   241  3      
STRAND   244   249  6      
HELIX   250   263  14      
TURN   281   283  3      
STRAND   317   319  3      
STRAND   323   325  3      
STRAND   329   331  3      
HELIX   340   343  4      
HELIX   347   353  7      
STRAND   358   360  3      
HELIX   386   389  4      
TURN   392   394  3      
TURN   404   407  4      
HELIX   410   433  24      
HELIX   439   460  22      
HELIX   463   467  5      
HELIX   469   475  7      
HELIX   492   497  6      
HELIX   498   504  7      
STRAND   507   510  4      
STRAND   516   518  3      
STRAND   523   526  4      
HELIX