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Protein

Myeloperoxidase

Gene

Mpo

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

Cl- + H2O2 + H+ = HClO + H2O.
Cl- + H2O2 = HOCl + 2 H2O.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 1 Ca2+ ion per monomer.By similarity
  • heme bBy similarityNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per monomer.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei234 – 2341Heme (covalent; via 3 links)By similarity
Active sitei235 – 2351Proton acceptorPROSITE-ProRule annotation
Metal bindingi236 – 2361CalciumPROSITE-ProRule annotation
Metal bindingi308 – 3081CalciumPROSITE-ProRule annotation
Metal bindingi310 – 3101Calcium; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi312 – 3121CalciumPROSITE-ProRule annotation
Metal bindingi314 – 3141CalciumPROSITE-ProRule annotation
Sitei379 – 3791Transition state stabilizerPROSITE-ProRule annotation
Binding sitei382 – 3821Heme (covalent; via 3 links)By similarity
Binding sitei383 – 3831Heme (covalent; via 3 links)By similarity
Metal bindingi476 – 4761Iron (heme axial ligand)PROSITE-ProRule annotation

GO - Molecular functioni

  1. heme binding Source: InterPro
  2. heparin binding Source: MGI
  3. metal ion binding Source: UniProtKB-KW
  4. peroxidase activity Source: MGI

GO - Biological processi

  1. aging Source: Ensembl
  2. defense response to fungus Source: MGI
  3. hydrogen peroxide catabolic process Source: MGI
  4. hypochlorous acid biosynthetic process Source: MGI
  5. low-density lipoprotein particle remodeling Source: MGI
  6. negative regulation of growth of symbiont in host Source: MGI
  7. oxidation-reduction process Source: MGI
  8. removal of superoxide radicals Source: MGI
  9. respiratory burst involved in defense response Source: MGI
  10. response to food Source: Ensembl
  11. response to gold nanoparticle Source: Ensembl
  12. response to lipopolysaccharide Source: Ensembl
  13. response to mechanical stimulus Source: Ensembl
  14. response to yeast Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Protein family/group databases

PeroxiBasei3344. MmMPO.

Names & Taxonomyi

Protein namesi
Recommended name:
Myeloperoxidase (EC:1.11.2.2)
Short name:
MPO
Cleaved into the following 2 chains:
Gene namesi
Name:Mpo
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:97137. Mpo.

Subcellular locationi

GO - Cellular componenti

  1. azurophil granule Source: UniProtKB
  2. extracellular space Source: MGI
  3. extracellular vesicular exosome Source: MGI
  4. mitochondrion Source: MGI
  5. nucleus Source: MGI
  6. secretory granule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Add
BLAST
Propeptidei16 – 138123Sequence AnalysisPRO_0000023657Add
BLAST
Chaini139 – 718580MyeloperoxidasePRO_0000023658Add
BLAST
Chaini139 – 252114Myeloperoxidase light chainPRO_0000023659Add
BLAST
Chaini253 – 718466Myeloperoxidase heavy chainPRO_0000023660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi141 ↔ 154PROSITE-ProRule annotation
Disulfide bondi255 ↔ 265PROSITE-ProRule annotation
Disulfide bondi259 ↔ 283PROSITE-ProRule annotation
Modified residuei290 – 2901Cysteine sulfenic acid (-SOH)By similarity
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi329 – 3291N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi361 ↔ 372PROSITE-ProRule annotation
Glycosylationi365 – 3651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi457 – 4571N-linked (GlcNAc...)Sequence Analysis
Modified residuei490 – 4901Nitrated tyrosineBy similarity
Disulfide bondi580 ↔ 637PROSITE-ProRule annotation
Disulfide bondi678 ↔ 704PROSITE-ProRule annotation
Glycosylationi711 – 7111N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration, Oxidation

Proteomic databases

MaxQBiP11247.
PaxDbiP11247.
PRIDEiP11247.

PTM databases

PhosphoSiteiP11247.

Expressioni

Gene expression databases

BgeeiP11247.
CleanExiMM_MPO.
ExpressionAtlasiP11247. baseline and differential.
GenevestigatoriP11247.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Each monomer consists of a light and a heavy chain (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000103563.

Structurei

3D structure databases

ProteinModelPortaliP11247.
SMRiP11247. Positions 131-717.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. XPO subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG262194.
GeneTreeiENSGT00550000074325.
HOGENOMiHOG000016084.
HOVERGENiHBG000071.
InParanoidiP11247.
KOiK10789.
OMAiKSSGCAY.
OrthoDBiEOG7M0NQW.
TreeFamiTF314316.

Family and domain databases

Gene3Di1.10.640.10. 2 hits.
InterProiIPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR029609. MPO.
[Graphical view]
PANTHERiPTHR11475:SF46. PTHR11475:SF46. 1 hit.
PfamiPF03098. An_peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11247-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLLALAGL LAPLAMLQTS NGATPALLGE VENSVVLSCM EEAKQLVDRA
60 70 80 90 100
YKERRESIKR SLQSGSASPT ELLFYFKQPV AGTRTAVRAA DYLHVALDLL
110 120 130 140 150
KRKLQPLWPR PFNVTDVLTP AQLNLLSVSS GCAYQDVRVT CPPNDKYRTI
160 170 180 190 200
TGHCNNRRSP TLGASNRAFV RWLPAEYEDG VSMPFGWTPG VNRNGFKVPL
210 220 230 240 250
ARQVSNAIVR FPNDQLTKDQ ERALMFMQWG QFLDHDITLT PEPATRFSFF
260 270 280 290 300
TGLNCETSCL QQPPCFPLKI PPNDPRIKNQ KDCIPFFRSC PACTRNNITI
310 320 330 340 350
RNQINALTSF VDASGVYGSE DPLARKLRNL TNQLGLLAIN TRFQDNGRAL
360 370 380 390 400
MPFDSLHDDP CLLTNRSARI PCFLAGDMRS SEMPELTSMH TLFVREHNRL
410 420 430 440 450
ATQLKRLNPR WNGEKLYQEA RKIVGAMVQI ITYRDYLPLV LGPAAMKKYL
460 470 480 490 500
PQYRSYNDSV DPRIANVFTN AFRYGHTLIQ PFMFRLNNQY RPTGPNPRVP
510 520 530 540 550
LSKVFFASWR VVLEGGIDPI LRGLMATPAK LNRQNQIVVD EIRERLFEQV
560 570 580 590 600
MRIGLDLPAL NMQRSRDHGL PGYNAWRRFC GLPQPSTVGE LGTVLKNLEL
610 620 630 640 650
ARKLMAQYGT PNNIDIWMGG VSEPLEPNGR VGQLLACLIG TQFRKLRDGD
660 670 680 690 700
RFWWENPGVF SKQQRQALAS ISLPRIICDN TGITTVSKNN IFMSNTYPRD
710
FVSCNTLPKL NLTSWKET
Length:718
Mass (Da):81,182
Last modified:July 27, 2011 - v2
Checksum:iE6763BE528E2ED83
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611S → T in CAA33373 (PubMed:2548170).Curated
Sequence conflicti61 – 611S → T in CAA33439 (PubMed:2552419).Curated
Sequence conflicti138 – 1381R → G in CAA33373 (PubMed:2548170).Curated
Sequence conflicti138 – 1381R → G in CAA33439 (PubMed:2552419).Curated
Sequence conflicti339 – 3391I → V in CAA33373 (PubMed:2548170).Curated
Sequence conflicti339 – 3391I → V in CAA33439 (PubMed:2552419).Curated
Sequence conflicti494 – 4952GP → AA in CAA33373 (PubMed:2548170).Curated
Sequence conflicti494 – 4952GP → AA in CAA33439 (PubMed:2552419).Curated
Sequence conflicti676 – 6761I → L in CAA33373 (PubMed:2548170).Curated
Sequence conflicti676 – 6761I → L in CAA33439 (PubMed:2552419).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15313 mRNA. Translation: CAA33373.1.
X15378 Genomic DNA. Translation: CAA33439.1.
AL604022 Genomic DNA. Translation: CAI35961.1.
CCDSiCCDS25217.1.
PIRiS06068.
RefSeqiNP_034954.2. NM_010824.2.
XP_006532467.1. XM_006532404.1.
XP_006532468.1. XM_006532405.1.
UniGeneiMm.4668.

Genome annotation databases

EnsembliENSMUST00000020779; ENSMUSP00000020779; ENSMUSG00000009350.
ENSMUST00000121303; ENSMUSP00000112837; ENSMUSG00000009350.
GeneIDi17523.
KEGGimmu:17523.
UCSCiuc011ycc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15313 mRNA. Translation: CAA33373.1.
X15378 Genomic DNA. Translation: CAA33439.1.
AL604022 Genomic DNA. Translation: CAI35961.1.
CCDSiCCDS25217.1.
PIRiS06068.
RefSeqiNP_034954.2. NM_010824.2.
XP_006532467.1. XM_006532404.1.
XP_006532468.1. XM_006532405.1.
UniGeneiMm.4668.

3D structure databases

ProteinModelPortaliP11247.
SMRiP11247. Positions 131-717.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000103563.

Chemistry

ChEMBLiCHEMBL2440.

Protein family/group databases

PeroxiBasei3344. MmMPO.

PTM databases

PhosphoSiteiP11247.

Proteomic databases

MaxQBiP11247.
PaxDbiP11247.
PRIDEiP11247.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020779; ENSMUSP00000020779; ENSMUSG00000009350.
ENSMUST00000121303; ENSMUSP00000112837; ENSMUSG00000009350.
GeneIDi17523.
KEGGimmu:17523.
UCSCiuc011ycc.1. mouse.

Organism-specific databases

CTDi4353.
MGIiMGI:97137. Mpo.

Phylogenomic databases

eggNOGiNOG262194.
GeneTreeiENSGT00550000074325.
HOGENOMiHOG000016084.
HOVERGENiHBG000071.
InParanoidiP11247.
KOiK10789.
OMAiKSSGCAY.
OrthoDBiEOG7M0NQW.
TreeFamiTF314316.

Miscellaneous databases

NextBioi292132.
PROiP11247.
SOURCEiSearch...

Gene expression databases

BgeeiP11247.
CleanExiMM_MPO.
ExpressionAtlasiP11247. baseline and differential.
GenevestigatoriP11247.

Family and domain databases

Gene3Di1.10.640.10. 2 hits.
InterProiIPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR029609. MPO.
[Graphical view]
PANTHERiPTHR11475:SF46. PTHR11475:SF46. 1 hit.
PfamiPF03098. An_peroxidase. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiPERM_MOUSE
AccessioniPrimary (citable) accession number: P11247
Secondary accession number(s): Q5NCP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 27, 2011
Last modified: March 4, 2015
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.