ID   A0A2K6BBG3_MACNE        Unreviewed;       629 AA.
AC   A0A2K6BBG3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Lactoperoxidase {ECO:0000256|ARBA:ARBA00017050};
GN   Name=LPO {ECO:0000313|Ensembl:ENSMNEP00000008758.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000008758.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000008758.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC         H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00034001};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56137;
CC         Evidence={ECO:0000256|ARBA:ARBA00034001};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + H2O2 + thiocyanate = H2O + hypothiocyanous acid;
CC         Xref=Rhea:RHEA:69416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:18022, ChEBI:CHEBI:133907;
CC         Evidence={ECO:0000256|ARBA:ARBA00034077};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69417;
CC         Evidence={ECO:0000256|ARBA:ARBA00034077};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O2 + iodide = H2O + hypoiodite; Xref=Rhea:RHEA:69420,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382,
CC         ChEBI:CHEBI:29232; Evidence={ECO:0000256|ARBA:ARBA00034063};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69421;
CC         Evidence={ECO:0000256|ARBA:ARBA00034063};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   AlphaFoldDB; A0A2K6BBG3; -.
DR   Ensembl; ENSMNET00000032928.1; ENSMNEP00000008758.1; ENSMNEG00000028850.1.
DR   GeneTree; ENSGT00940000160488; -.
DR   OMA; QNKMMTR; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000028850; Expressed in bone marrow.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd09824; myeloperoxidase_like; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   PANTHER; PTHR11475:SF67; LACTOPEROXIDASE; 1.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   4: Predicted;
KW   Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Nitration {ECO:0000256|ARBA:ARBA00023074};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..629
FT                   /note="Lactoperoxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014331104"
FT   BINDING         385
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                   /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ   SEQUENCE   629 AA;  71172 MW;  7575FC95EEF3D599 CRC64;
     MRILLHLPAL LASFILLQAA ASATRDPSLD LTSLSLEVGC GAPAPVVRCD PCSPYRTITG
     DCNNRRKPAL GAANRALARW LPAEYEDGLS LPFGWTPGKM RNGFPLPLAR EVSNKIVGYL
     NEEGVLDQNR SLFFMQWGQI VDHDLDFAPD TELGSSEYSK AQCDEYCIQG DNCFPIMFPP
     NDPKARTQGK CMPFFRAGFV CPTPPYKSLA REQINALTSF LDASFVYSSE PSLASRLRNL
     SSPLGLMAVN QEVSDHGLPY LPYDSKKPSP CEFINTTARV PCFLAGDSRA SEHILLATSH
     TLFLREHNRL ARELKRLNPQ WDGEKLYQEA RKILGAFVQI ITFRDYLPIL LGDHMQKWIP
     PYQGYNESVD PRISNVFTFA FRFGHLEVPS SVFRLDENYQ PWGPEPELPL HTLFFNTWRM
     VKDGGIDPLV RGLLAKKSKL MKQNKMMTGE LRNKLFQPTH RIHGFDLAAI NTQRCRDHGQ
     PGYNSWRAFC DLSQPQTLEE LNTVLKNKML AKKLLGLYGT PDNIDIWIGA IAEPLVERGR
     VGPLLACLLG KQFQQIRDGD RFWWENPGVF TKEQKDSLRK MSFSRLVCDN TRITKVPRDP
     FRANSYPYDF ADCSAIDKLD LSPWASVKN
//