ID J3KT11_HUMAN Unreviewed; 95 AA.
AC J3KT11;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Lactoperoxidase {ECO:0000256|ARBA:ARBA00017050};
DE Flags: Fragment;
GN Name=LPO {ECO:0000313|Ensembl:ENSP00000462752.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000462752.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000462752.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [2] {ECO:0000313|Ensembl:ENSP00000462752.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AC004687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; J3KT11; -.
DR SMR; J3KT11; -.
DR MassIVE; J3KT11; -.
DR PeptideAtlas; J3KT11; -.
DR Ensembl; ENST00000580890.5; ENSP00000462752.1; ENSG00000167419.11.
DR UCSC; uc060hxi.1; human.
DR HGNC; HGNC:6678; LPO.
DR VEuPathDB; HostDB:ENSG00000167419; -.
DR GeneTree; ENSGT00940000160488; -.
DR HOGENOM; CLU_2378117_0_0_1; -.
DR ChiTaRS; LPO; human.
DR Proteomes; UP000005640; Chromosome 17.
DR Bgee; ENSG00000167419; Expressed in parotid gland and 80 other cell types or tissues.
DR ExpressionAtlas; J3KT11; baseline and differential.
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:0006979; P:response to oxidative stress; IEA:InterPro.
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 SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 1: Evidence at protein level;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nitration {ECO:0000256|ARBA:ARBA00023074};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|MaxQB:J3KT11,
KW ECO:0007829|PeptideAtlas:J3KT11};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT NON_TER 1
FT /evidence="ECO:0000313|Ensembl:ENSP00000462752.1"
SQ SEQUENCE 95 AA; 10299 MW; CAAA4A7EF9166293 CRC64;
GCGAPAPVVR CDPCSPYRTI TGDCNNRRKP ALGAANRALA RWLPAEYEDG LSLPFGWTPG
KTRNGFPLPL AREVSNKIVG YLNEEGVLDQ NRSTL
//
