ID PERL_MESAU Reviewed; 710 AA. AC Q8R481; DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-NOV-2024, entry version 96. DE RecName: Full=Lactoperoxidase {ECO:0000303|Ref.1}; DE Short=LPO {ECO:0000303|Ref.1}; DE EC=1.11.1.7 {ECO:0000250|UniProtKB:P80025}; DE AltName: Full=Lacrimal gland peroxidase {ECO:0000303|PubMed:16469299}; DE Flags: Precursor; GN Name=LPO; OS Mesocricetus auratus (Golden hamster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; OC Cricetidae; Cricetinae; Mesocricetus. OX NCBI_TaxID=10036; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lacrimal gland; RA Paliwal A., Srikantan S., De P.K.; RT "cDNA cloning and regulation of a lactoperoxidase (LPO) from hamster RT lacrimal gland."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION. RC TISSUE=Lacrimal gland; RX PubMed=16469299; DOI=10.1016/j.bbrc.2006.01.095; RA Paliwal A., De P.K.; RT "Marked sexual dimorphism of lacrimal gland peroxidase in hamster: RT repression by androgens and estrogens."; RL Biochem. Biophys. Res. Commun. 341:1286-1293(2006). CC -!- FUNCTION: Heme-containing oxidoreductase which catalyzes the conversion CC of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid CC (OSCN(-)) in the presence of hydrogen peroxide (H2O2). Also involved in CC the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence CC of H2O2 (By similarity). Responsible for the inactivation of a wide CC range of micro-organisms and hence, important component of defense CC mechanism. May be implicated in airway host defense against infection CC (By similarity). May contribute to maintaining an appropriate H2O2 CC cellular level, therefore protecting cells from H2O2-caused injuries CC and inflammation (By similarity). {ECO:0000250|UniProtKB:P22079, CC ECO:0000250|UniProtKB:P80025, ECO:0000250|UniProtKB:Q5SW46}. 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:0000250|UniProtKB:P80025}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56137; CC Evidence={ECO:0000250|UniProtKB:P80025}; CC -!- CATALYTIC ACTIVITY: CC Reaction=thiocyanate + H2O2 + H(+) = hypothiocyanous acid + H2O; CC Xref=Rhea:RHEA:69416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:18022, ChEBI:CHEBI:133907; CC Evidence={ECO:0000250|UniProtKB:P80025}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69417; CC Evidence={ECO:0000250|UniProtKB:P80025}; CC -!- CATALYTIC ACTIVITY: CC Reaction=iodide + H2O2 = hypoiodite + H2O; Xref=Rhea:RHEA:69420, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, CC ChEBI:CHEBI:29232; Evidence={ECO:0000250|UniProtKB:P80025}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69421; CC Evidence={ECO:0000250|UniProtKB:P80025}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; CC Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE- CC ProRule:PRU00298}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per CC heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16469299}. Cytoplasm CC {ECO:0000250|UniProtKB:Q5SW46}. Note=Secreted by the lacrimal gland CC into tears. {ECO:0000269|PubMed:16469299}. CC -!- TISSUE SPECIFICITY: Expressed in the lacrimal gland with higher levels CC and 3-fold higher activity in adult females than males and secreted CC into tears (at protein level). {ECO:0000269|PubMed:16469299}. CC -!- INDUCTION: Repressed by the androgen dihydrotestosterone (DHT) and the CC estrogen estradiol (E2) (at protein level). CC {ECO:0000269|PubMed:16469299}. CC -!- MISCELLANEOUS: Thiocyanate (SCN(-)) and hypothiocyanite (OSCN(-)) are CC bound in the distal heme cavity. The iodide ion (I(-)) occupies a CC position which is stabilized by the interactions with heme moiety, His- CC 224, Arg-370 and Glu-373. Hydrogen peroxide is held between the heme CC iron and His-224. {ECO:0000250|UniProtKB:P80025}. CC -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF498045; AAM15535.1; -; mRNA. DR RefSeq; NP_001268330.1; NM_001281401.1. DR AlphaFoldDB; Q8R481; -. DR SMR; Q8R481; -. DR STRING; 10036.ENSMAUP00000025391; -. DR PeroxiBase; 4045; MauLPO. DR GlyCosmos; Q8R481; 5 sites, No reported glycans. DR GeneID; 101830444; -. DR KEGG; maua:101830444; -. DR CTD; 4025; -. DR eggNOG; KOG2408; Eukaryota. DR OrthoDB; 4560at2759; -. DR Proteomes; UP000189706; Unplaced. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. 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:0004601; F:peroxidase activity; ISS:UniProtKB. DR GO; GO:0036393; F:thiocyanate peroxidase activity; ISS:UniProtKB. DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl. DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IEA:Ensembl. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR CDD; cd09824; myeloperoxidase_like; 1. DR FunFam; 1.10.640.10:FF:000001; Peroxidasin homolog; 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 InterPro; IPR050702; Peroxidase/ROS_Generation. 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 1: Evidence at protein level; KW Antimicrobial; Calcium; Cytoplasm; Disulfide bond; Glycoprotein; Heme; KW Iron; Metal-binding; Nitration; Oxidoreductase; Peroxidase; Phosphoprotein; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT PROPEP 23..98 FT /evidence="ECO:0000250|UniProtKB:P80025" FT /id="PRO_0000433299" FT CHAIN 99..710 FT /note="Lactoperoxidase" FT /evidence="ECO:0000250|UniProtKB:P80025" FT /id="PRO_0000433300" FT ACT_SITE 224 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT BINDING 223 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /note="covalent" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT BINDING 225 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT BINDING 299 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT BINDING 301 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT BINDING 303 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT BINDING 305 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT BINDING 373 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /note="covalent" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT BINDING 466 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:0000255|PROSITE-ProRule:PRU00298" FT SITE 370 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT MOD_RES 313 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P80025" FT MOD_RES 480 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:P11678" FT CARBOHYD 25 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 104 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 131 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 238 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 320 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 130..143 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT DISULFID 244..254 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT DISULFID 248..272 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT DISULFID 352..363 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT DISULFID 571..628 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT DISULFID 669..694 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" SQ SEQUENCE 710 AA; 80219 MW; AD8C9359DB1C270F CRC64; MKVLLRLPAL LASLTLLQMA ASTRNATRTA TIRETVDEVK VQVNKAFLDS RDRLKTDMSN LAPTVRHLSG YLKQAKGRTR TAIRVGQVWE QSLKRLRRMV PLTNVTGQGL DLTSLSWEVG CGHPAPTVTC NISNPYRTIT GDCNNRKNPE LGSANRALAR WLPAEYEDGL SLPFGWTPGK TRNGFPLPQP RDVSNQVLDY LNEEEILDQN RSLLFMQWGQ IVDHDLDFAP ETEMGSDNYS KAQCDELCIQ GDNCFPIMFP KGDPKLKTQG KCLPFFRAGF VCPTSPYQSL AREQINALTS FMDASMVYGS EPSLANRLRN LSSPLGLMAV NEEVSDHGRP LLPFVNVKPS PCEVINRTAG VPCFLAGDSR ASEQILLATS HTLFLREHNR LARELSRLNP QWDGEKLYQE ARRIMGALIQ IITFRDYLPI LLGDELQKWI PPYQGYKETV DPRISNVFTF AFRFGHLEVP STVSRLDENY QPWGSEPELP LHKLFFNTWR VVKDGGIDPL VRGLLAKKAK LAHQDKMMTG ELRNMLFQPN HTVHGFDLAA INIQRCRDHG QPGYNSWRAF CGLSQPKTLE ELSAVLRNEV LAKKLMDLYG TPDNIDIWLG AIAEPLVRRG RVGPLLTCLL GQQFQRIRDG DRFWWENPGV FTEKQRDSLQ KMSFSRLVCD NTGINKVPLN PFQPNSYPHS FVDCSAIEKL DLTPWASVKK //