ID   PON3_HUMAN              Reviewed;         354 AA.
AC   Q15166; A4D1H8; O75855; O76060; Q6IRU9; Q8IX97; Q9BZH9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 3.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Serum paraoxonase/lactonase 3;
DE            EC=3.1.1.2;
DE            EC=3.1.1.81;
DE            EC=3.1.8.1;
GN   Name=PON3;
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].
RC   TISSUE=Hepatoma;
RA   Reddy S.T., Wadleigh D.J., Grijalva V., Ng C., Hama S., Gangopadhyay A.,
RA   Khorsan R., Shih D., Lusis A.J., Navab M., Fogelman A.M.;
RT   "Human paraoxanase-3 is an HDL-associated enzyme.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Draganov D.I., Watson C.E.;
RT   "Human PON3 has lactonase activity.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-146 AND ASP-179.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 14-354.
RC   TISSUE=Liver;
RX   PubMed=8661009; DOI=10.1006/geno.1996.0225;
RA   Primo-Parmo S.L., Sorenson R.C., Teiber J., La Du B.N.;
RT   "The human serum paraoxonase/arylesterase gene (PON1) is one member of a
RT   multigene family.";
RL   Genomics 33:498-507(1996).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=15772423; DOI=10.1194/jlr.m400511-jlr200;
RA   Draganov D.I., Teiber J.F., Speelman A., Osawa Y., Sunahara R., La Du B.N.;
RT   "Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping
RT   and distinct substrate specificities.";
RL   J. Lipid Res. 46:1239-1247(2005).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Has low activity towards the organophosphate paraxon and
CC       aromatic carboxylic acid esters. Rapidly hydrolyzes lactones such as
CC       statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic lactones and
CC       5- or 6-member ring lactones with aliphatic substituents but not simple
CC       lactones or those with polar substituents.
CC       {ECO:0000269|PubMed:15772423}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+);
CC         Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2;
CC         Evidence={ECO:0000269|PubMed:15772423};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl
CC         alcohol.; EC=3.1.8.1; Evidence={ECO:0000269|PubMed:15772423};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine
CC         + H(+); Xref=Rhea:RHEA:22576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:55474, ChEBI:CHEBI:58921; EC=3.1.1.81;
CC         Evidence={ECO:0000269|PubMed:15772423};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15772423}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC   -!- PTM: The signal sequence is not cleaved. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the paraoxonase family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/pon3/";
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DR   EMBL; AF320003; AAK07629.1; -; mRNA.
DR   EMBL; AF329433; AAO15365.1; -; mRNA.
DR   EMBL; AY805220; AAV50000.1; -; Genomic_DNA.
DR   EMBL; AC004022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC005021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH236949; EAL24132.1; -; Genomic_DNA.
DR   EMBL; CH471091; EAW76768.1; -; Genomic_DNA.
DR   EMBL; BC070374; AAH70374.1; -; mRNA.
DR   EMBL; L48516; AAC41996.1; -; mRNA.
DR   CCDS; CCDS5639.1; -.
DR   RefSeq; NP_000931.1; NM_000940.2.
DR   AlphaFoldDB; Q15166; -.
DR   SMR; Q15166; -.
DR   BioGRID; 111442; 6.
DR   IntAct; Q15166; 3.
DR   STRING; 9606.ENSP00000265627; -.
DR   BindingDB; Q15166; -.
DR   ChEMBL; CHEMBL4295824; -.
DR   DrugBank; DB14598; Edetate calcium disodium anhydrous.
DR   DrugBank; DB14600; Edetate disodium anhydrous.
DR   DrugBank; DB00974; Edetic acid.
DR   DrugBank; DB00227; Lovastatin.
DR   GlyCosmos; Q15166; 3 sites, No reported glycans.
DR   GlyGen; Q15166; 3 sites.
DR   iPTMnet; Q15166; -.
DR   PhosphoSitePlus; Q15166; -.
DR   BioMuta; PON3; -.
DR   DMDM; 50403778; -.
DR   CPTAC; non-CPTAC-2696; -.
DR   CPTAC; non-CPTAC-2697; -.
DR   jPOST; Q15166; -.
DR   MassIVE; Q15166; -.
DR   MaxQB; Q15166; -.
DR   PaxDb; 9606-ENSP00000265627; -.
DR   PeptideAtlas; Q15166; -.
DR   ProteomicsDB; 60478; -.
DR   Antibodypedia; 15863; 328 antibodies from 30 providers.
DR   DNASU; 5446; -.
DR   Ensembl; ENST00000265627.10; ENSP00000265627.5; ENSG00000105852.11.
DR   GeneID; 5446; -.
DR   KEGG; hsa:5446; -.
DR   MANE-Select; ENST00000265627.10; ENSP00000265627.5; NM_000940.3; NP_000931.1.
DR   UCSC; uc003unt.4; human.
DR   AGR; HGNC:9206; -.
DR   CTD; 5446; -.
DR   DisGeNET; 5446; -.
DR   GeneCards; PON3; -.
DR   HGNC; HGNC:9206; PON3.
DR   HPA; ENSG00000105852; Tissue enriched (liver).
DR   MalaCards; PON3; -.
DR   MIM; 602720; gene.
DR   neXtProt; NX_Q15166; -.
DR   OpenTargets; ENSG00000105852; -.
DR   Orphanet; 803; Amyotrophic lateral sclerosis.
DR   PharmGKB; PA33531; -.
DR   VEuPathDB; HostDB:ENSG00000105852; -.
DR   eggNOG; ENOG502S6UP; Eukaryota.
DR   GeneTree; ENSGT00390000008932; -.
DR   HOGENOM; CLU_049839_0_1_1; -.
DR   InParanoid; Q15166; -.
DR   OMA; MKIHDNW; -.
DR   OrthoDB; 2874974at2759; -.
DR   PhylomeDB; Q15166; -.
DR   TreeFam; TF322436; -.
DR   BRENDA; 3.1.1.2; 2681.
DR   BRENDA; 3.1.1.25; 2681.
DR   BRENDA; 3.1.8.1; 2681.
DR   PathwayCommons; Q15166; -.
DR   Reactome; R-HSA-2142688; Synthesis of 5-eicosatetraenoic acids.
DR   Reactome; R-HSA-9754706; Atorvastatin ADME.
DR   SignaLink; Q15166; -.
DR   BioGRID-ORCS; 5446; 9 hits in 1148 CRISPR screens.
DR   GeneWiki; PON3; -.
DR   GenomeRNAi; 5446; -.
DR   Pharos; Q15166; Tbio.
DR   PRO; PR:Q15166; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q15166; Protein.
DR   Bgee; ENSG00000105852; Expressed in right lobe of liver and 126 other cell types or tissues.
DR   ExpressionAtlas; Q15166; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
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; IBA:GO_Central.
DR   GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004063; F:aryldialkylphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004064; F:arylesterase activity; IDA:BHF-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IDA:BHF-UCL.
DR   GO; GO:0046395; P:carboxylic acid catabolic process; IDA:BHF-UCL.
DR   GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR   GO; GO:0032929; P:negative regulation of superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0003096; P:renal sodium ion transport; IEA:Ensembl.
DR   GO; GO:0009636; P:response to toxic substance; IBA:GO_Central.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR002640; Arylesterase.
DR   InterPro; IPR008364; Paraoxonase2.
DR   PANTHER; PTHR11799; PARAOXONASE; 1.
DR   PANTHER; PTHR11799:SF14; SERUM PARAOXONASE_LACTONASE 3; 1.
DR   Pfam; PF01731; Arylesterase; 1.
DR   PRINTS; PR01785; PARAOXONASE.
DR   PRINTS; PR01787; PARAOXONASE2.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR   Genevisible; Q15166; HS.
PE   1: Evidence at protein level;
KW   Calcium; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW   Phosphoprotein; Reference proteome; Secreted; Signal.
FT   CHAIN           1..354
FT                   /note="Serum paraoxonase/lactonase 3"
FT                   /id="PRO_0000223290"
FT   SIGNAL          1..?
FT                   /note="Not cleaved"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        114
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952"
FT   DISULFID        42..352
FT                   /evidence="ECO:0000250"
FT   VARIANT         146
FT                   /note="E -> K (in dbSNP:rs17878827)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_021082"
FT   VARIANT         179
FT                   /note="A -> D (in dbSNP:rs17883013)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_021083"
FT   CONFLICT        18
FT                   /note="G -> E (in Ref. 8; AAC41996)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        32
FT                   /note="R -> Q (in Ref. 8; AAC41996)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50
FT                   /note="S -> N (in Ref. 7; AAH70374)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        58..59
FT                   /note="LP -> FL (in Ref. 1; AAK07629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63
FT                   /note="A -> S (in Ref. 8; AAC41996)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68
FT                   /note="G -> E (in Ref. 8; AAC41996)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   354 AA;  39607 MW;  1B861B35E8533921 CRC64;
     MGKLVALVLL GVGLSLVGEM FLAFRERVNA SREVEPVEPE NCHLIEELES GSEDIDILPS
     GLAFISSGLK YPGMPNFAPD EPGKIFLMDL NEQNPRAQAL EISGGFDKEL FNPHGISIFI
     DKDNTVYLYV VNHPHMKSTV EIFKFEEQQR SLVYLKTIKH ELLKSVNDIV VLGPEQFYAT
     RDHYFTNSLL SFFEMILDLR WTYVLFYSPR EVKVVAKGFC SANGITVSAD QKYVYVADVA
     AKNIHIMEKH DNWDLTQLKV IQLGTLVDNL TVDPATGDIL AGCHPNPMKL LNYNPEDPPG
     SEVLRIQNVL SEKPRVSTVY ANNGSVLQGT SVASVYHGKI LIGTVFHKTL YCEL
//