PERL_MESAU
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 03-AUG-2022, entry version 90.
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=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:0000250|UniProtKB:P80025};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69417;
CC Evidence={ECO:0000250|UniProtKB:P80025};
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: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}.
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DR EMBL; AF498045; AAM15535.1; -; mRNA.
DR RefSeq; NP_001268330.1; NM_001281401.1.
DR AlphaFoldDB; Q8R481; -.
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; Unplaced.
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; 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
