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 07-APR-2021, entry version 88. DE RecName: Full=Lactoperoxidase {ECO:0000312|EMBL:AAM15535.1}; DE Short=LPO {ECO:0000312|EMBL:AAM15535.1}; DE EC=1.11.1.7 {ECO:0000250|UniProtKB:A5JUY8}; DE AltName: Full=Lacrimal gland peroxidase {ECO:0000312|EMBL:AAM15535.1}; DE Flags: Precursor; GN Name=LPO {ECO:0000312|EMBL:AAM15535.1}; 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 {ECO:0000312|EMBL:AAM15535.1}; RN [1] {ECO:0000312|EMBL:AAM15535.1} RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lacrimal gland {ECO:0000312|EMBL:AAM15535.1}; 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] {ECO:0000305} RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION. RC TISSUE=Lacrimal gland {ECO:0000303|PubMed:16469299}; 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: Antimicrobial agent which utilizes hydrogen peroxide and CC thiocyanate (SCN) to generate the antimicrobial substance CC hypothiocyanous acid (HOSCN). {ECO:0000250|UniProtKB:A5JUY8}. 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:A5JUY8}; 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}. CC Note=Secreted by the lacrimal gland into tears. CC {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 -!- 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 SMR; Q8R481; -. DR STRING; 10036.XP_005075849.1; -. DR PeroxiBase; 4045; MauLPO. DR GeneID; 101830444; -. DR CTD; 4025; -. DR eggNOG; KOG2408; Eukaryota. DR Proteomes; UP000189706; Genome assembly. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0036393; F:thiocyanate peroxidase activity; IEA:Ensembl. 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 Gene3D; 1.10.640.10; -; 1. DR InterPro; IPR019791; Haem_peroxidase_animal. DR InterPro; IPR010255; Haem_peroxidase_sf. DR InterPro; IPR037120; Haem_peroxidase_sf_animal. DR InterPro; IPR029587; LPO. DR PANTHER; PTHR11475:SF67; PTHR11475:SF67; 1. DR Pfam; PF03098; An_peroxidase; 1. DR PRINTS; PR00457; ANPEROXIDASE. DR SUPFAM; SSF48113; SSF48113; 1. DR PROSITE; PS50292; PEROXIDASE_3; 1. PE 1: Evidence at protein level; KW Antimicrobial; Calcium; Disulfide bond; Glycoprotein; Heme; Iron; KW 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 METAL 225 FT /note="Calcium" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT METAL 299 FT /note="Calcium" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT METAL 301 FT /note="Calcium; via carbonyl oxygen" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT METAL 303 FT /note="Calcium" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT METAL 305 FT /note="Calcium" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT METAL 466 FT /note="Iron (heme axial ligand)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT BINDING 223 FT /note="Heme; covalent" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00298" FT BINDING 373 FT /note="Heme; covalent" 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 //