ID   PERL_HUMAN              Reviewed;         712 AA.
AC   P22079; A5JUY4; E7EMJ3; Q13408; Q3KNQ2;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2001, sequence version 2.
DT   24-JAN-2024, entry version 206.
DE   RecName: Full=Lactoperoxidase {ECO:0000303|PubMed:12626341};
DE            Short=LPO {ECO:0000303|PubMed:12626341};
DE            EC=1.11.1.7 {ECO:0000305|PubMed:12626341};
DE   AltName: Full=Salivary peroxidase {ECO:0000303|PubMed:8964511};
DE            Short=SPO {ECO:0000303|PubMed:8964511};
DE   Flags: Precursor;
GN   Name=LPO {ECO:0000312|HGNC:HGNC:6678}; Synonyms=SAPX;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Submandibular gland;
RX   PubMed=8964511; DOI=10.1016/0378-1119(96)00078-9;
RA   Kiser C., Caterina J., Engler J.A., Rahemtulla B., Rahemtulla F.;
RT   "Cloning and sequence analysis of the human salivary peroxidase-encoding
RT   cDNA.";
RL   Gene 173:261-264(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-421, AND ALTERNATIVE SPLICING.
RX   PubMed=19059195; DOI=10.1016/j.abb.2008.11.015;
RA   Fragoso M.A., Torbati A., Fregien N., Conner G.E.;
RT   "Molecular heterogeneity and alternative splicing of human
RT   lactoperoxidase.";
RL   Arch. Biochem. Biophys. 482:52-57(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-105; THR-244; GLN-414;
RP   MET-421; GLN-514; THR-614 AND ASN-700.
RG   NIEHS SNPs program;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
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).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 389-712, AND VARIANT MET-421.
RX   PubMed=2222811; DOI=10.1089/dna.1990.9.499;
RA   Dull T.J., Uyeda C., Strosberg A.D., Nedwin G., Seilhamer J.J.;
RT   "Molecular cloning of cDNAs encoding bovine and human lactoperoxidase.";
RL   DNA Cell Biol. 9:499-509(1990).
RN   [7]
RP   PROTEIN SEQUENCE OF N-TERMINUS, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX   PubMed=10715594; DOI=10.1016/s0955-2863(99)00082-0;
RA   Shin K., Tomita M., Loennerdal B.;
RT   "Identification of lactoperoxidase in mature human milk.";
RL   J. Nutr. Biochem. 11:94-102(2000).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12626341; DOI=10.1165/rcmb.2002-0152oc;
RA   Wijkstrom-Frei C., El-Chemaly S., Ali-Rachedi R., Gerson C., Cobas M.A.,
RA   Forteza R., Salathe M., Conner G.E.;
RT   "Lactoperoxidase and human airway host defense.";
RL   Am. J. Respir. Cell Mol. Biol. 29:206-212(2003).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212 AND ASN-358.
RC   TISSUE=Saliva;
RX   PubMed=16740002; DOI=10.1021/pr050492k;
RA   Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT   "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT   capture and mass spectrometry.";
RL   J. Proteome Res. 5:1493-1503(2006).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-358.
RC   TISSUE=Milk;
RX   PubMed=18780401; DOI=10.1002/pmic.200701057;
RA   Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT   "Identification of N-linked glycoproteins in human milk by hydrophilic
RT   interaction liquid chromatography and mass spectrometry.";
RL   Proteomics 8:3833-3847(2008).
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) (By similarity).
CC       Also involved in the conversion of iodide (I(-)) into hypoiodite
CC       (IO(-)) in the presence of H2O2 (By similarity). Responsible for the
CC       inactivation of a wide range of micro-organisms and hence, important
CC       component of defense mechanism (PubMed:12626341). Shows antibacterial
CC       properties against Pseudomonas aeruginosa (PubMed:12626341). The
CC       lactoperoxidase-SCN(-)-H2O2 system shows antibacterial properties
CC       against Burkholderia cepacia and Haemophilus influenzae in vitro
CC       (PubMed:12626341). Present in mammary and salivary gland secretions and
CC       may contribute to airway host defense against infection
CC       (PubMed:12626341). 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:P80025,
CC       ECO:0000250|UniProtKB:Q5SW46, ECO:0000269|PubMed:12626341}.
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:0000305|PubMed:12626341};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56137;
CC         Evidence={ECO:0000305|PubMed:12626341};
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; Evidence={ECO:0000255|PROSITE-
CC         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; Evidence={ECO:0000255|PROSITE-
CC         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:12626341}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q5SW46}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1;
CC         IsoId=P22079-1; Sequence=Displayed;
CC       Name=2; Synonyms=V3;
CC         IsoId=P22079-2; Sequence=VSP_044473;
CC   -!- TISSUE SPECIFICITY: Mammary gland, milk and salivary gland. Found in
CC       bronchial submucosal glands. {ECO:0000269|PubMed:10715594,
CC       ECO:0000269|PubMed:12626341}.
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       226, Arg-372 and Glu-375. Hydrogen peroxide is held between the heme
CC       iron and His-226. {ECO:0000250|UniProtKB:P80025}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. XPO subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00298}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/lpo/";
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; U39573; AAC50717.1; -; mRNA.
DR   EMBL; EF579964; ABQ53140.1; -; mRNA.
DR   EMBL; AY324876; AAP72968.1; -; Genomic_DNA.
DR   EMBL; AC004687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC005962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC107166; AAI07167.1; -; mRNA.
DR   EMBL; BC107167; AAI07168.1; -; mRNA.
DR   EMBL; M58151; AAA63213.1; -; mRNA.
DR   CCDS; CCDS32689.1; -. [P22079-1]
DR   CCDS; CCDS54149.1; -. [P22079-2]
DR   PIR; JC4935; JC4935.
DR   RefSeq; NP_001153574.1; NM_001160102.1. [P22079-2]
DR   RefSeq; NP_006142.1; NM_006151.2. [P22079-1]
DR   AlphaFoldDB; P22079; -.
DR   SMR; P22079; -.
DR   BioGRID; 110207; 11.
DR   IntAct; P22079; 1.
DR   STRING; 9606.ENSP00000262290; -.
DR   BindingDB; P22079; -.
DR   ChEMBL; CHEMBL5898; -.
DR   DrugCentral; P22079; -.
DR   PeroxiBase; 3316; HsLPO.
DR   GlyConnect; 2939; 2 N-Linked glycans (1 site).
DR   GlyCosmos; P22079; 4 sites, 4 glycans.
DR   GlyGen; P22079; 5 sites, 4 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P22079; -.
DR   PhosphoSitePlus; P22079; -.
DR   BioMuta; LPO; -.
DR   DMDM; 12643419; -.
DR   MassIVE; P22079; -.
DR   PaxDb; 9606-ENSP00000262290; -.
DR   PeptideAtlas; P22079; -.
DR   PRIDE; P22079; -.
DR   ProteomicsDB; 16955; -.
DR   ProteomicsDB; 53957; -. [P22079-1]
DR   Antibodypedia; 18358; 295 antibodies from 32 providers.
DR   DNASU; 4025; -.
DR   Ensembl; ENST00000262290.9; ENSP00000262290.4; ENSG00000167419.11. [P22079-1]
DR   Ensembl; ENST00000421678.6; ENSP00000400245.2; ENSG00000167419.11. [P22079-2]
DR   Ensembl; ENST00000582328.5; ENSP00000464636.1; ENSG00000167419.11. [P22079-2]
DR   GeneID; 4025; -.
DR   KEGG; hsa:4025; -.
DR   MANE-Select; ENST00000262290.9; ENSP00000262290.4; NM_006151.3; NP_006142.1.
DR   UCSC; uc002ivt.3; human. [P22079-1]
DR   AGR; HGNC:6678; -.
DR   CTD; 4025; -.
DR   DisGeNET; 4025; -.
DR   GeneCards; LPO; -.
DR   HGNC; HGNC:6678; LPO.
DR   HPA; ENSG00000167419; Tissue enriched (salivary).
DR   MIM; 150205; gene.
DR   MIM; 170990; gene.
DR   neXtProt; NX_P22079; -.
DR   OpenTargets; ENSG00000167419; -.
DR   PharmGKB; PA30439; -.
DR   VEuPathDB; HostDB:ENSG00000167419; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   GeneTree; ENSGT00940000160488; -.
DR   HOGENOM; CLU_006087_1_0_1; -.
DR   InParanoid; P22079; -.
DR   OMA; QNKMMTR; -.
DR   OrthoDB; 4560at2759; -.
DR   PhylomeDB; P22079; -.
DR   TreeFam; TF314316; -.
DR   PathwayCommons; P22079; -.
DR   Reactome; R-HSA-8941413; Events associated with phagocytolytic activity of PMN cells.
DR   SignaLink; P22079; -.
DR   BioGRID-ORCS; 4025; 42 hits in 1147 CRISPR screens.
DR   ChiTaRS; LPO; human.
DR   GeneWiki; Lactoperoxidase; -.
DR   GenomeRNAi; 4025; -.
DR   Pharos; P22079; Tbio.
DR   PRO; PR:P22079; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; P22079; Protein.
DR   Bgee; ENSG00000167419; Expressed in parotid gland and 80 other cell types or tissues.
DR   ExpressionAtlas; P22079; baseline and differential.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
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:0036393; F:thiocyanate peroxidase activity; IDA:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR   GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IDA:UniProtKB.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; NAS:UniProtKB.
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.
DR   Genevisible; P22079; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Antimicrobial; Calcium; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Heme;
KW   Hydrogen peroxide; Iron; Metal-binding; Nitration; Oxidoreductase;
KW   Peroxidase; Phosphoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PROPEP          27..80
FT                   /evidence="ECO:0000305|PubMed:10715594"
FT                   /id="PRO_0000023649"
FT   CHAIN           81..712
FT                   /note="Lactoperoxidase"
FT                   /evidence="ECO:0000305|PubMed:10715594"
FT                   /id="PRO_0000023650"
FT   ACT_SITE        226
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         225
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:P80025"
FT   BINDING         227
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         307
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   BINDING         375
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:P80025"
FT   BINDING         468
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            372
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   MOD_RES         315
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P80025"
FT   MOD_RES         482
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P11678"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16740002"
FT   CARBOHYD        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        358
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16740002,
FT                   ECO:0000269|PubMed:18780401"
FT   DISULFID        132..145
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   DISULFID        246..256
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   DISULFID        250..274
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   DISULFID        354..365
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   DISULFID        573..630
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   DISULFID        671..696
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   VAR_SEQ         26..108
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_044473"
FT   VARIANT         105
FT                   /note="T -> I (in dbSNP:rs8178318)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_018809"
FT   VARIANT         244
FT                   /note="A -> T (in dbSNP:rs8178338)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_018810"
FT   VARIANT         414
FT                   /note="R -> Q (in dbSNP:rs8178355)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_018811"
FT   VARIANT         421
FT                   /note="V -> M (in dbSNP:rs2301870)"
FT                   /evidence="ECO:0000269|PubMed:19059195,
FT                   ECO:0000269|PubMed:2222811, ECO:0000269|Ref.3"
FT                   /id="VAR_018812"
FT   VARIANT         514
FT                   /note="R -> Q (in dbSNP:rs8178401)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_018813"
FT   VARIANT         614
FT                   /note="I -> T (in dbSNP:rs8178408)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_018814"
FT   VARIANT         700
FT                   /note="D -> N (in dbSNP:rs8178412)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_018815"
FT   CONFLICT        255
FT                   /note="N -> S (in Ref. 2; ABQ53140)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        678
FT                   /note="K -> M (in Ref. 2; ABQ53140)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   712 AA;  80288 MW;  BC7AA410997198C0 CRC64;
     MRVLLHLPAL LASLILLQAA ASTTRAQTTR TSAISDTVSQ AKVQVNKAFL DSRTRLKTAM
     SSETPTSRQL SEYLKHAKGR TRTAIRNGQV WEESLKRLRQ KASLTNVTDP SLDLTSLSLE
     VGCGAPAPVV RCDPCSPYRT ITGDCNNRRK PALGAANRAL ARWLPAEYED GLSLPFGWTP
     GKTRNGFPLP LAREVSNKIV GYLNEEGVLD QNRSLLFMQW GQIVDHDLDF APDTELGSSE
     YSKAQCDEYC IQGDNCFPIM FPPNDPKAGT QGKCMPFFRA GFVCPTPPYK SLAREQINAL
     TSFLDASFVY SSEPSLASRL RNLSSPLGLM AVNQEVSDHG LPYLPYDSKK PSPCEFINTT
     ARVPCFLAGD SRASEHILLA TSHTLFLREH NRLARELKRL NPQWDGEKLY QEARKILGAF
     VQIITFRDYL PILLGDHMQK WIPPYQGYSE SVDPRISNVF TFAFRFGHLE VPSSMFRLDE
     NYQPWGPEPE LPLHTLFFNT WRMVKDGGID PLVRGLLAKK SKLMKQNKMM TGELRNKLFQ
     PTHRIHGFDL AAINTQRCRD HGQPGYNSWR AFCDLSQPQT LEELNTVLKS KMLAKKLLGL
     YGTPDNIDIW IGAIAEPLVE RGRVGPLLAC LLGKQFQQIR DGDRFWWENP GVFTNEQKDS
     LQKMSFSRLV CDNTRITKVP RDPFWANSYP YDFVDCSAID KLDLSPWASV KN
//