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P11247 (PERM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Myeloperoxidase
Short name=MPO
EC=1.11.2.2

Cleaved into the following 2 chains:

  1. Myeloperoxidase light chain
  2. Myeloperoxidase heavy chain
Gene names
Name:Mpo
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length718 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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 By similarity.

Catalytic activity

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

Cl- + H2O2 = HOCl + 2 H2O.

Cofactor

Binds 1 calcium ion per monomer By similarity.

Binds 1 heme B (iron-protoporphyrin IX) group covalently per monomer By similarity.

Subunit structure

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

Subcellular location

Lysosome.

Sequence similarities

Belongs to the peroxidase family. XPO subfamily.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentLysosome
   DomainSignal
   LigandCalcium
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   PTMDisulfide bond
Glycoprotein
Oxidation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to fungus

Inferred from mutant phenotype PubMed 10085024. Source: MGI

hydrogen peroxide catabolic process

Inferred from direct assay PubMed 10085024. Source: MGI

hypochlorous acid biosynthetic process

Inferred from mutant phenotype PubMed 10085024. Source: MGI

low-density lipoprotein particle remodeling

Inferred from electronic annotation. Source: Compara

negative regulation of growth of symbiont in host

Inferred from mutant phenotype PubMed 10085024. Source: MGI

removal of superoxide radicals

Inferred from mutant phenotype PubMed 10085024. Source: MGI

respiratory burst involved in defense response

Inferred from mutant phenotype PubMed 10085024. Source: MGI

response to yeast

Inferred from mutant phenotype PubMed 10085024. Source: MGI

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: Compara

lysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 14651853. Source: MGI

secretory granule

Inferred from electronic annotation. Source: Compara

   Molecular_functionheme binding

Inferred from electronic annotation. Source: InterPro

heparin binding

Inferred from electronic annotation. Source: Compara

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peroxidase activity

Inferred from direct assay PubMed 10085024PubMed 11792727PubMed 11980719PubMed 15159534. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515
Propeptide16 – 138123 Potential
PRO_0000023657
Chain139 – 718580Myeloperoxidase
PRO_0000023658
Chain139 – 252114Myeloperoxidase light chain
PRO_0000023659
Chain253 – 718466Myeloperoxidase heavy chain
PRO_0000023660

Sites

Active site2351Proton acceptor By similarity
Metal binding2361Calcium By similarity
Metal binding3081Calcium By similarity
Metal binding3101Calcium; via carbonyl oxygen By similarity
Metal binding3121Calcium By similarity
Metal binding3141Calcium By similarity
Metal binding4761Iron (heme axial ligand) By similarity
Binding site2341Heme (covalent; via 3 links) By similarity
Binding site3821Heme (covalent; via 3 links) By similarity
Binding site3831Heme (covalent; via 3 links) By similarity
Site3791Transition state stabilizer By similarity

Amino acid modifications

Modified residue2901Cysteine sulfenic acid (-SOH) By similarity
Glycosylation1131N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation3291N-linked (GlcNAc...) Potential
Glycosylation3651N-linked (GlcNAc...) Potential
Glycosylation4571N-linked (GlcNAc...) Potential
Glycosylation7111N-linked (GlcNAc...) Potential
Disulfide bond141 ↔ 154 By similarity
Disulfide bond255 ↔ 265 By similarity
Disulfide bond259 ↔ 283 By similarity
Disulfide bond361 ↔ 372 By similarity
Disulfide bond580 ↔ 637 By similarity
Disulfide bond678 ↔ 704 By similarity

Experimental info

Sequence conflict611S → T in CAA33373. Ref.1
Sequence conflict611S → T in CAA33439. Ref.2
Sequence conflict1381R → G in CAA33373. Ref.1
Sequence conflict1381R → G in CAA33439. Ref.2
Sequence conflict3391I → V in CAA33373. Ref.1
Sequence conflict3391I → V in CAA33439. Ref.2
Sequence conflict494 – 4952GP → AA in CAA33373. Ref.1
Sequence conflict494 – 4952GP → AA in CAA33439. Ref.2
Sequence conflict6761I → L in CAA33373. Ref.1
Sequence conflict6761I → L in CAA33439. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P11247 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: E6763BE528E2ED83

FASTA71881,182
        10         20         30         40         50         60 
MKLLLALAGL LAPLAMLQTS NGATPALLGE VENSVVLSCM EEAKQLVDRA YKERRESIKR 

        70         80         90        100        110        120 
SLQSGSASPT ELLFYFKQPV AGTRTAVRAA DYLHVALDLL KRKLQPLWPR PFNVTDVLTP 

       130        140        150        160        170        180 
AQLNLLSVSS GCAYQDVRVT CPPNDKYRTI TGHCNNRRSP TLGASNRAFV RWLPAEYEDG 

       190        200        210        220        230        240 
VSMPFGWTPG VNRNGFKVPL ARQVSNAIVR FPNDQLTKDQ ERALMFMQWG QFLDHDITLT 

       250        260        270        280        290        300 
PEPATRFSFF TGLNCETSCL QQPPCFPLKI PPNDPRIKNQ KDCIPFFRSC PACTRNNITI 

       310        320        330        340        350        360 
RNQINALTSF VDASGVYGSE DPLARKLRNL TNQLGLLAIN TRFQDNGRAL MPFDSLHDDP 

       370        380        390        400        410        420 
CLLTNRSARI PCFLAGDMRS SEMPELTSMH TLFVREHNRL ATQLKRLNPR WNGEKLYQEA 

       430        440        450        460        470        480 
RKIVGAMVQI ITYRDYLPLV LGPAAMKKYL PQYRSYNDSV DPRIANVFTN AFRYGHTLIQ 

       490        500        510        520        530        540 
PFMFRLNNQY RPTGPNPRVP LSKVFFASWR VVLEGGIDPI LRGLMATPAK LNRQNQIVVD 

       550        560        570        580        590        600 
EIRERLFEQV MRIGLDLPAL NMQRSRDHGL PGYNAWRRFC GLPQPSTVGE LGTVLKNLEL 

       610        620        630        640        650        660 
ARKLMAQYGT PNNIDIWMGG VSEPLEPNGR VGQLLACLIG TQFRKLRDGD RFWWENPGVF 

       670        680        690        700        710 
SKQQRQALAS ISLPRIICDN TGITTVSKNN IFMSNTYPRD FVSCNTLPKL NLTSWKET

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X15313 mRNA. Translation: CAA33373.1.
X15378 Genomic DNA. Translation: CAA33439.1.
AL604022 Genomic DNA. Translation: CAI35961.1.
IPIIPI00113480.
PIRS06068.
RefSeqNP_034954.2. NM_010824.2.
UniGeneMm.4668.

3D structure databases

ProteinModelPortalP11247.
SMRP11247. Positions 131-717.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000103563.

Protein family/group databases

PeroxiBase3344. MmMPO.

PTM databases

PhosphoSiteP11247.

Proteomic databases

PaxDbP11247.
PRIDEP11247.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020779; ENSMUSP00000020779; ENSMUSG00000009350.
ENSMUST00000121303; ENSMUSP00000112837; ENSMUSG00000009350.
GeneID17523.
KEGGmmu:17523.
UCSCuc011ycc.1. mouse.

Organism-specific databases

CTD4353.
MGIMGI:97137. Mpo.

Phylogenomic databases

eggNOGNOG262194.
GeneTreeENSGT00550000074325.
HOGENOMHOG000016084.
HOVERGENHBG000071.
InParanoidQ5NCP1.
KOK10789.
OMAKSSGCAY.
OrthoDBEOG4ZGPBX.

Gene expression databases

ArrayExpressP11247.
BgeeP11247.
CleanExMM_MPO.
GenevestigatorP11247.
GermOnlineENSMUSG00000009350. Mus musculus.

Family and domain databases

Gene3D1.10.640.10. 2 hits.
InterProIPR010255. Haem_peroxidase.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_subgr.
[Graphical view]
PfamPF03098. An_peroxidase. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. False negative.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL2440.
ChiTaRSMPO. mouse.
NextBio292132.
SOURCESearch...

Entry information

Entry namePERM_MOUSE
AccessionPrimary (citable) accession number: P11247
Secondary accession number(s): Q5NCP1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 27, 2011
Last modified: May 29, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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