ID Q91WA0_MOUSE Unreviewed; 710 AA.
AC Q91WA0;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=Lactoperoxidase {ECO:0000256|ARBA:ARBA00017050};
GN Name=Lpo {ECO:0000313|EMBL:AAH16212.1, ECO:0000313|MGI:MGI:1923363};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH16212.1};
RN [1] {ECO:0000313|EMBL:AAH16212.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000313|EMBL:AAH16212.1};
RC TISSUE=Salivary gland {ECO:0000313|EMBL:AAH16212.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC016212; AAH16212.1; -; mRNA.
DR AlphaFoldDB; Q91WA0; -.
DR AGR; MGI:1923363; -.
DR MGI; MGI:1923363; Lpo.
DR ChiTaRS; Lpo; mouse.
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 2: Evidence at transcript level;
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 Peroxidase {ECO:0000313|EMBL:AAH16212.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..710
FT /note="Lactoperoxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014312466"
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:0000256|PIRSR:PIRSR619791-2"
SQ SEQUENCE 710 AA; 79922 MW; EB9BCF12472EC5DA CRC64;
MKVLLHLPAL LASLTLLQTA ASASDDPTAE TDIIHDTVEE VKVWVNKAFL DSRDRLKMAM
TTKIHSTRHL SDYLKHAKGR TRTAIRSGQV WEESLKKLSQ FLTNVTGQGL DLTSLSWEAG
CDPPAPTMTC NISSPYRTIT GYCNNRKNPA LGSANRALAR WLPAEYEDGL SLPYGWTPGK
MRNGFPLPQP REVSNQIAAY LNEEDVLDQK RSMLFMQWGQ IVDHDMDFAP ETEMGSDTYT
KAQCDEHCIQ GDNCFPIMFP PGDPKLKTQG KCMPFFRAGF VCPTPPYKSL AREQINALTS
FLDASLVYSP EPSLANRLRN LSSPLGLMAV NEEVSDNGRP FPPFVKMKPS PCEVINATAG
VPCFLAGDSR ASEQILLATS HTLFIREHNR LATELSRLNP HWDGETLYQE ARKIMGAFIQ
ITTFRDYLPI LLGDEMQKWI PPYQGYNESV DPRISNVFTF ALRFGHLEIP STVSRLDENY
QPWGSESELP LHTVFFNTWR LVKDGGIDPL VRGLLAKNAK LMHQNKMMTG ELRNKLFQPN
HTIHGFDLAS INIQRSRDHG QPGYNSWRAF CGLSQPKTLE ELSAVMKNEV LAKKLMDLYG
TPSNIDIWLG AVAEPLVHRG RVGPLLTCLL GQQFQRIRDG DRFWWENPGV FTEKQRESLQ
KMSFSRLVCD NTGIDKVPLN PFQANAYPHG FVDCSSIDKL DLSPWASVKE
//
