Myeloperoxidase precursor - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
    Myeloperoxidase
      Short name=MPO
    EC=1.11.1.7
Cleaved into the following 4 chains:
    1- Recommended name:
            89 kDa myeloperoxidase
    2- Recommended name:
            84 kDa myeloperoxidase
    3- Recommended name:
            Myeloperoxidase light chain
    4- Recommended name:
            Myeloperoxidase heavy chain

Gene names

Name:

MPO

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	745 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

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.
Catalytic activity	Donor + H₂O₂ = oxidized donor + 2 H₂O. Cl^- + H₂O₂ = HOCl + 2 H₂O.
Cofactor	Binds 1 calcium ion per heterodimer. Binds 1 heme B (iron-protoporphyrin IX) group covalently per heterodimer.
Subunit structure	Tetramer of two light chains and two heavy chains.
Subcellular location	Lysosome.
Involvement in disease	Defects in MPO are the cause of myeloperoxidase deficiency (MPD) [MIM:254600]. MPD is an autosomal recessive defect that results in disseminated candidiasis. Ref.22 Ref.23 Ref.24 Ref.25 Ref.26
Sequence similarities	Belongs to the peroxidase family. XPO subfamily.

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Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Lysosome
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein Oxidation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	anti-apoptosis Traceable author statement. Source: ProtInc defense response Ref.24 Traceable author statement. Source: ProtInc hydrogen peroxide catabolic process Inferred from direct assay. Source: UniProtKB low-density lipoprotein particle remodeling Inferred from direct assay. Source: UniProtKB oxidation reduction Inferred from direct assay. Source: UniProtKB
Cellular component	extracellular space Inferred from direct assay. Source: UniProtKB lysosome Ref.24 Traceable author statement. Source: ProtInc nucleus Traceable author statement. Source: ProtInc
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW chromatin binding Traceable author statement. Source: ProtInc heme binding Inferred from electronic annotation. Source: InterPro peroxidase activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform H17 (identifier: P05164-1) Also known as: B; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform H14 (identifier: P05164-2) The sequence of this isoform differs from the canonical sequence as follows: 1-95: Missing.

Isoform H7 (identifier: P05164-3) Also known as: A; The sequence of this isoform differs from the canonical sequence as follows: 182-182: N → NRCGWLGVAAGTGLREASRTPQASRCQRPVLPC

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 48

48

Ref.12

Chain

49 – 745

697

89 kDa myeloperoxidase

PRO_0000023651

Propeptide

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

Sites

Active site

261

1

Proton acceptor

Metal binding

262

1

Calcium

Metal binding

334

1

Calcium

Metal binding

336

1

Calcium; via carbonyl oxygen

Metal binding

338

1

Calcium

Metal binding

340

1

Calcium

Metal binding

502

1

Iron (heme axial ligand)

Binding site

260

1

Heme (covalent; via 3 links)

Binding site

408

1

Heme (covalent; via 3 links)

Binding site

409

1

Heme (covalent; via 3 links)

Site

405

1

Transition state stabilizer

Amino acid modifications

Modified residue

316

1

Cysteine sulfenic acid (-SOH)

Glycosylation

139

1

N-linked (GlcNAc...) Ref.16

Glycosylation

323

1

N-linked (GlcNAc...) Ref.17

Glycosylation

355

1

N-linked (GlcNAc...) Ref.18

Glycosylation

391

1

N-linked (GlcNAc...) Ref.18

Glycosylation

483

1

N-linked (GlcNAc...) Ref.16 Ref.17

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Interchain

Disulfide bond

387 ↔ 398

Disulfide bond

606 ↔ 663

Disulfide bond

704 ↔ 730

Natural variations

Alternative sequence

1 – 95

95

Missing in isoform H14.

VSP_007206

Alternative sequence

182

1

N → NRCGWLGVAAGTGLREASRT PQASRCQRPVLPC in isoform H7.

VSP_007207

Natural variant

53

1

V → F: dbSNP rs7208693. Ref.9

VAR_023995

Natural variant

173

1

Y → C in MPD; affects proteolytic processing and secretion. Ref.25

VAR_015377

Natural variant

251

1

M → T in MPD. Ref.26

VAR_015378

Natural variant

447

1

R → Q in a colorectal cancer sample; somatic mutation. Ref.27

VAR_036517

Natural variant

569

1

R → W in MPD; suppress post-translational processing. Ref.22 Ref.23 Ref.24

VAR_015379

Natural variant

604

1

R → C

VAR_023996

Natural variant

683

1

E → Q

VAR_023997

Natural variant

717

1

I → V: dbSNP rs2759. Ref.9

VAR_012066

Experimental info

Sequence conflict

36

1

L → V in CAA28565. Ref.4

Sequence conflict

36

1

L → V in CAA33438. Ref.7

Secondary structure

1

.

745

Helix Strand Turn

Details...

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Sequences

Sequence		Length	Mass (Da)
Isoform H17 (B) [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 348B1CE0A11038B4 Show »	FASTA	745	83,869
10 20 30 40 50 60 MGVPFFSSLR CMVDLGPCWA GGLTAEMKLL LALAGLLAIL ATPQPSEGAA PAVLGEVDTS 70 80 90 100 110 120 LVLSSMEEAK QLVDKAYKER RESIKQRLRS GSASPMELLS YFKQPVAATR TAVRAADYLH 130 140 150 160 170 180 VALDLLERKL RSLWRRPFNV TDVLTPAQLN VLSKSSGCAY QDVGVTCPEQ DKYRTITGMC 190 200 210 220 230 240 NNRRSPTLGA SNRAFVRWLP AEYEDGFSLP YGWTPGVKRN GFPVALARAV SNEIVRFPTD 250 260 270 280 290 300 QLTPDQERSL MFMQWGQLLD HDLDFTPEPA ARASFVTGVN CETSCVQQPP CFPLKIPPND 310 320 330 340 350 360 PRIKNQADCI PFFRSCPACP GSNITIRNQI NALTSFVDAS MVYGSEEPLA RNLRNMSNQL 370 380 390 400 410 420 GLLAVNQRFQ DNGRALLPFD NLHDDPCLLT NRSARIPCFL AGDTRSSEMP ELTSMHTLLL 430 440 450 460 470 480 REHNRLATEL KSLNPRWDGE RLYQEARKIV GAMVQIITYR DYLPLVLGPT AMRKYLPTYR 490 500 510 520 530 540 SYNDSVDPRI ANVFTNAFRY GHTLIQPFMF RLDNRYQPME PNPRVPLSRV FFASWRVVLE 550 560 570 580 590 600 GGIDPILRGL MATPAKLNRQ NQIAVDEIRE RLFEQVMRIG LDLPALNMQR SRDHGLPGYN 610 620 630 640 650 660 AWRRFCGLPQ PETVGQLGTV LRNLKLARKL MEQYGTPNNI DIWMGGVSEP LKRKGRVGPL 670 680 690 700 710 720 LACIIGTQFR KLRDGDRFWW ENEGVFSMQQ RQALAQISLP RIICDNTGIT TVSKNNIFMS 730 740 NSYPRDFVNC STLPALNLAS WREAS « Hide
Isoform H14. Checksum: 7A29F89DFE6B4916 Show »	FASTA	650	73,854
10 20 30 40 50 60 MELLSYFKQP VAATRTAVRA ADYLHVALDL LERKLRSLWR RPFNVTDVLT PAQLNVLSKS 70 80 90 100 110 120 SGCAYQDVGV TCPEQDKYRT ITGMCNNRRS PTLGASNRAF VRWLPAEYED GFSLPYGWTP 130 140 150 160 170 180 GVKRNGFPVA LARAVSNEIV RFPTDQLTPD QERSLMFMQW GQLLDHDLDF TPEPAARASF 190 200 210 220 230 240 VTGVNCETSC VQQPPCFPLK IPPNDPRIKN QADCIPFFRS CPACPGSNIT IRNQINALTS 250 260 270 280 290 300 FVDASMVYGS EEPLARNLRN MSNQLGLLAV NQRFQDNGRA LLPFDNLHDD PCLLTNRSAR 310 320 330 340 350 360 IPCFLAGDTR SSEMPELTSM HTLLLREHNR LATELKSLNP RWDGERLYQE ARKIVGAMVQ 370 380 390 400 410 420 IITYRDYLPL VLGPTAMRKY LPTYRSYNDS VDPRIANVFT NAFRYGHTLI QPFMFRLDNR 430 440 450 460 470 480 YQPMEPNPRV PLSRVFFASW RVVLEGGIDP ILRGLMATPA KLNRQNQIAV DEIRERLFEQ 490 500 510 520 530 540 VMRIGLDLPA LNMQRSRDHG LPGYNAWRRF CGLPQPETVG QLGTVLRNLK LARKLMEQYG 550 560 570 580 590 600 TPNNIDIWMG GVSEPLKRKG RVGPLLACII GTQFRKLRDG DRFWWENEGV FSMQQRQALA 610 620 630 640 650 QISLPRIICD NTGITTVSKN NIFMSNSYPR DFVNCSTLPA LNLASWREAS « Hide
Isoform H7 (A). Checksum: F15BC771A9C6F6A6 Show »	FASTA	777	87,248
10 20 30 40 50 60 MGVPFFSSLR CMVDLGPCWA GGLTAEMKLL LALAGLLAIL ATPQPSEGAA PAVLGEVDTS 70 80 90 100 110 120 LVLSSMEEAK QLVDKAYKER RESIKQRLRS GSASPMELLS YFKQPVAATR TAVRAADYLH 130 140 150 160 170 180 VALDLLERKL RSLWRRPFNV TDVLTPAQLN VLSKSSGCAY QDVGVTCPEQ DKYRTITGMC 190 200 210 220 230 240 NNRCGWLGVA AGTGLREASR TPQASRCQRP VLPCRRSPTL GASNRAFVRW LPAEYEDGFS 250 260 270 280 290 300 LPYGWTPGVK RNGFPVALAR AVSNEIVRFP TDQLTPDQER SLMFMQWGQL LDHDLDFTPE 310 320 330 340 350 360 PAARASFVTG VNCETSCVQQ PPCFPLKIPP NDPRIKNQAD CIPFFRSCPA CPGSNITIRN 370 380 390 400 410 420 QINALTSFVD ASMVYGSEEP LARNLRNMSN QLGLLAVNQR FQDNGRALLP FDNLHDDPCL 430 440 450 460 470 480 LTNRSARIPC FLAGDTRSSE MPELTSMHTL LLREHNRLAT ELKSLNPRWD GERLYQEARK 490 500 510 520 530 540 IVGAMVQIIT YRDYLPLVLG PTAMRKYLPT YRSYNDSVDP RIANVFTNAF RYGHTLIQPF 550 560 570 580 590 600 MFRLDNRYQP MEPNPRVPLS RVFFASWRVV LEGGIDPILR GLMATPAKLN RQNQIAVDEI 610 620 630 640 650 660 RERLFEQVMR IGLDLPALNM QRSRDHGLPG YNAWRRFCGL PQPETVGQLG TVLRNLKLAR 670 680 690 700 710 720 KLMEQYGTPN NIDIWMGGVS EPLKRKGRVG PLLACIIGTQ FRKLRDGDRF WWENEGVFSM 730 740 750 760 770 QQRQALAQIS LPRIICDNTG ITTVSKNNIF MSNSYPRDFV NCSTLPALNL ASWREAS « Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of cDNA for human myeloperoxidase." Morishita K., Kubota N., Asano S., Kaziro Y., Nagata S. J. Biol. Chem. 262:3844-3851(1987) [PubMed: 3029127] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
[2]	"Chromosomal gene structure of human myeloperoxidase and regulation of its expression by granulocyte colony-stimulating factor." Morishita K., Tsuchiya M., Asano S., Kaziro Y., Nagata S. J. Biol. Chem. 262:15208-15213(1987) [PubMed: 2444596] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Isolation of a complementary DNA clone for thyroid microsomal antigen. Homology with the gene for thyroid peroxidase." Seto P., Hirayu H., Magnusson R.P., Gestautas J., Portmann L., Degroot L.J., Rapoport B. J. Clin. Invest. 80:1205-1208(1987) [PubMed: 3654979] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
[4]	"Characterization of cDNA clones for human myeloperoxidase: predicted amino acid sequence and evidence for multiple mRNA species." Johnson K.R., Nauseef W.M., Care A., Wheelock M.J., Shane S., Hudson S., Koeffler H.P., Selsted M., Miller C., Rovera G. Nucleic Acids Res. 15:2013-2028(1987) [PubMed: 3031585] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
[5]	"Multiple species of myeloperoxidase messenger RNAs produced by alternative splicing and differential polyadenylation." Hashinaka K., Nishio C., Hur S.-J., Sakiyama F., Tsunasawa S., Yamada M. Biochemistry 27:5906-5914(1988) [PubMed: 2903767] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS H7; H14 AND H17), PROTEIN SEQUENCE OF 165-183; 216-222; 295-304; 311-331; 464-479; 662-676 AND 766-776. Tissue: Leukemia.
[6]	Erratum Hashinaka K., Nishio C., Hur S.-J., Sakiyama F., Tsunasawa S., Yamada M. Biochemistry 27:9226-9226(1988)
[7]	"Complete nucleotide sequence of the human myeloperoxidase gene." Johnson K.R., Gemperlein I., Hudson S., Shane S., Rovera G. Nucleic Acids Res. 17:7985-7986(1989) [PubMed: 2552418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]	"Cloning and characterization of four types of cDNA encoding myeloperoxidase from human monocytic leukemia cell line, SKM-1." Hosokawa Y., Kawaguchi R., Hikiji K., Yamada M., Suzuki K., Nakagawa T., Yoshihara T., Yamaguchi K. Leukemia 7:441-445(1993) [PubMed: 8383257] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
[9]	NIEHS SNPs program Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PHE-53; CYS-604; GLN-683 AND VAL-717.
[10]	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. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM H17).
[12]	"Isolation and characterization of extracellular myeloperoxidase precursor in HL-60 cell cultures." Yamada M., Hur S.-J., Toda H. Biochem. Biophys. Res. Commun. 166:852-859(1990) [PubMed: 2154223] [Abstract] Cited for: PROTEIN SEQUENCE OF 49-66.
[13]	"Unique autolytic cleavage of human myeloperoxidase. Implications for the involvement of active site MET409." Taylor K.L., Pohl J., Kinkade J.M. Jr. J. Biol. Chem. 267:25282-25288(1992) [PubMed: 1334087] [Abstract] Cited for: PROTEIN SEQUENCE OF 279-424. Tissue: Leukocyte.
[14]	"Identification of transcriptional cis-elements in introns 7 and 9 of the myeloperoxidase gene." Yamada M., Yoshida M., Hashinaka K. J. Biol. Chem. 268:13479-13485(1993) [PubMed: 8390465] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 548-629.
[15]	"Isolation and characterization of a cDNA coding for human myeloperoxidase." Yamada M., Hur S.-J., Hashinaka K., Tsuneoka K., Saeki T., Nishio C., Sakiyama F., Tsunasawa S. Arch. Biochem. Biophys. 255:147-155(1987) [PubMed: 2884926] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 588-745.
[16]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-139 AND ASN-483, MASS SPECTROMETRY. Tissue: Plasma.
[17]	"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry." Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A. J. Proteome Res. 5:1493-1503(2006) [PubMed: 16740002] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323 AND ASN-483, MASS SPECTROMETRY. Tissue: Saliva.
[18]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-355 AND ASN-391, MASS SPECTROMETRY. Tissue: Liver.
[19]	"X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8-A resolution." Fiedler T.J., Davey C.A., Fenna R.E. J. Biol. Chem. 275:11964-11971(2000) [PubMed: 10766826] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 167-744.
[20]	"Structure of the green heme in myeloperoxidase." Fenna R.E., Zeng J., Davey C. Arch. Biochem. Biophys. 316:653-656(1995) [PubMed: 7840679] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 167-744.
[21]	"Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution." Blair-Johnson M., Fiedler T., Fenna R. Biochemistry 40:13990-13997(2001) [PubMed: 11705390] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 167-744.
[22]	"Myeloperoxidase (MPO) gene mutation in hereditary MPO deficiency." Kizaki M., Miller C.W., Selsted M.E., Koeffler H.P. Blood 83:1935-1940(1994) [PubMed: 8142659] [Abstract] Cited for: VARIANT MPD TRP-569.
[23]	"Hereditary myeloperoxidase deficiency due to a missense mutation of arginine 569 to tryptophan." Nauseef W.M., Brigham S., Cogley M. J. Biol. Chem. 269:1212-1216(1994) [PubMed: 7904599] [Abstract] Cited for: VARIANT MPD TRP-569.
[24]	"Effect of the R569W missense mutation on the biosynthesis of myeloperoxidase." Nauseef W., Cogley M., McCormick S. J. Biol. Chem. 271:9546-9549(1996) [PubMed: 8621627] [Abstract] Cited for: CHARACTERIZATION OF VARIANT MPD TRP-569.
[25]	"A novel form of hereditary myeloperoxidase deficiency linked to endoplasmic reticulum/proteasome degradation." DeLeo F.R., Goedken M., McCormick S.J., Nauseef W.M. J. Clin. Invest. 101:2900-2909(1998) [PubMed: 9637725] [Abstract] Cited for: VARIANT MPD CYS-173, CHARACTERIZATION OF VARIANT MPD CYS-173.
[26]	"Biochemical and molecular characterization of hereditary myeloperoxidase deficiency." Romano M., Dri P., Dadalt L., Patriarca P., Baralle F.E. Blood 90:4126-4134(1997) [PubMed: 9354683] [Abstract] Cited for: VARIANT MPD THR-251.
[27]	"The consensus coding sequences of human breast and colorectal cancers." 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. Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-447.
+	Additional computationally mapped references.

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Web resources

MPObase

MPO mutation db

NIEHS-SNPs

Wikipedia

Myeloperoxidase entry

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Cross-references

Sequence databases

J02694 mRNA. Translation: AAA59896.1.
M17176

M17175 Genomic DNA. Translation: AAA60346.1.
X04876 mRNA. Translation: CAA28565.1.
M19507 mRNA. Translation: AAA59863.1.
M19508 Genomic DNA. Translation: AAA59864.1.
M19508 Genomic DNA. Translation: AAA59865.1.
X15377 Genomic DNA. Translation: CAA33438.1.
S56200 mRNA. Translation: AAB25582.1.
DQ088846 Genomic DNA. Translation: AAY68218.1.
CH471109 Genomic DNA. Translation: EAW94470.1.
BC130476 mRNA. Translation: AAI30477.1.
D14466 Genomic DNA. Translation: BAA03362.1.

IPI

IPI00007244.
IPI00236554.
IPI00236556.

PIR

OPHUM. A29467.
B28894.
D28894.

RefSeq

NP_000241.1.

UniGene

Hs.458272

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CXP	X-ray	1.80	A/B	167-270	[»]
			C/D	279-744	[»]
1D2V	X-ray	1.75	A/B	167-270	[»]
			C/D	279-744	[»]
1D5L	X-ray	1.90	A/B	167-270	[»]
			C/D	279-744	[»]
1D7W	X-ray	1.90	A/B	167-270	[»]
			C/D	279-744	[»]
1DNU	X-ray	1.85	A/B	167-270	[»]
			C/D	279-744	[»]
1DNW	X-ray	1.90	A/B	167-270	[»]
			C/D	279-744	[»]
1MHL	X-ray	2.25	A/B	165-272	[»]
			C/D	279-744	[»]
1MYP	X-ray	3.00	A/B	165-272	[»]
			C/D	279-744	[»]
3F9P	X-ray	2.93	A/B	165-278	[»]
			C/D	279-745	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P05164.

Protein family/group databases

PeroxiBase

3315. HsMPO.

PTM databases

GlycoSuiteDB

P05164.

PhosphoSite

P05164.

Proteomic databases

PRIDE

P05164.

Genome annotation databases

Ensembl

ENST00000225275; ENSP00000225275; ENSG00000005381; Homo sapiens. [Genome view]
ENST00000340482; ENSP00000344419; ENSG00000005381; Homo sapiens. [Genome view]
ENST00000393105; ENSP00000376817; ENSG00000005381; Homo sapiens. [Genome view]

GeneID

4353.

KEGG

hsa:4353.

UCSC

uc002ivu.1. human.

Organism-specific databases

CTD

4353.

GeneCards

GC17M053702.

H-InvDB

HIX0039242.

HGNC

HGNC:7218. MPO.

HPA

CAB000059.
HPA021147.

MIM

254600. phenotype.
606989. gene.

Orphanet

2587. Myeloperoxidase deficiency.

PharmGKB

PA243.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P05164.

OMA

KSSGCAY.

Enzyme and pathway databases

BRENDA

1.11.1.7. 247.

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.
il23pathway. IL23-mediated signaling events.

Gene expression databases

ArrayExpress

P05164.

Bgee

P05164.

CleanEx

HS_MPO.

Genevestigator

P05164.

GermOnline

ENSG00000005381. Homo sapiens.

Family and domain databases

InterPro

IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_sg.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]

Gene3D

G3DSA:1.10.640.10. Haem_peroxidase_animal. 1 hit.

Pfam

PF03098. An_peroxidase. 1 hit.
[Graphical view]

PRINTS

PR00457. ANPEROXIDASE.

PROSITE

PS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. False negative.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00535. Cefdinir.

NextBio

17126.

PMAP-CutDB

P05164.

SOURCE

Search...

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Entry information

Entry name

PERM_HUMAN

Accession

Primary (citable) accession number: P05164
Secondary accession number(s): A1L4B8

Q9UCL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	November 3, 2009
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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