PERL_HUMAN
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 03-AUG-2022, entry version 198.
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;
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: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/";
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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; 10.
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 GlyGen; P22079; 4 sites, 3 N-linked glycans (1 site).
DR iPTMnet; P22079; -.
DR PhosphoSitePlus; P22079; -.
DR BioMuta; LPO; -.
DR DMDM; 12643419; -.
DR MassIVE; P22079; -.
DR PaxDb; P22079; -.
DR PeptideAtlas; P22079; -.
DR PRIDE; P22079; -.
DR ProteomicsDB; 16955; -.
DR ProteomicsDB; 53957; -. [P22079-1]
DR Antibodypedia; 18358; 277 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 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; 276568at2759; -.
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; 38 hits in 1067 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 79 other tissues.
DR ExpressionAtlas; P22079; baseline and differential.
DR Genevisible; P22079; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
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 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 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
