LY96_HUMAN
ID LY96_HUMAN Reviewed; 160 AA.
AC Q9Y6Y9; B3Y6A5; E5RJJ7;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Lymphocyte antigen 96;
DE Short=Ly-96;
DE AltName: Full=ESOP-1 {ECO:0000303|PubMed:10891475};
DE AltName: Full=Protein MD-2 {ECO:0000303|PubMed:10359581};
DE Flags: Precursor;
GN Name=LY96; Synonyms=ESOP1, MD2;
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), VARIANT GLY-56, FUNCTION,
RP INTERACTION WITH TLR4, AND SUBCELLULAR LOCATION.
RC TISSUE=Uterus;
RX PubMed=10359581; DOI=10.1084/jem.189.11.1777;
RA Shimazu R., Akashi S., Ogata H., Nagai Y., Fukudome K., Miyake K.,
RA Kimoto M.;
RT "MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-
RT like receptor 4.";
RL J. Exp. Med. 189:1777-1782(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-56.
RX PubMed=10891475;
RA Kato K., Morrison A.M., Nakano T., Tashiro K., Honjo T.;
RT "ESOP-1, a secreted protein expressed in the hematopoietic, nervous, and
RT reproductive systems of embryonic and adult mice.";
RL Blood 96:362-364(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF CYS-95, AND VARIANT
RP GLY-56.
RX PubMed=11435474; DOI=10.1084/jem.194.1.79;
RA Schromm A.B., Lien E., Henneke P., Chow J.C., Yoshimura A., Heine H.,
RA Latz E., Monks B.G., Schwartz D.A., Miyake K., Golenbock D.T.;
RT "Molecular genetic analysis of an endotoxin nonresponder mutant cell line.
RT A point mutation in a conserved region of MD-2 abolishes endotoxin-induced
RT signaling.";
RL J. Exp. Med. 194:79-88(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-56.
RX PubMed=18810425; DOI=10.1007/s00251-008-0332-0;
RA Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T., Kimura A.;
RT "Natural selection in the TLR-related genes in the course of primate
RT evolution.";
RL Immunogenetics 60:727-735(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-56.
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 [7]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11274165; DOI=10.1074/jbc.m009164200;
RA da Silva Correia J., Soldau K., Christen U., Tobias P.S., Ulevitch R.J.;
RT "Lipopolysaccharide is in close proximity to each of the proteins in its
RT membrane receptor complex. transfer from CD14 to TLR4 and MD-2.";
RL J. Biol. Chem. 276:21129-21135(2001).
RN [8]
RP INTERACTION WITH TLR2 AND TLR4, AND FUNCTION.
RX PubMed=11160242; DOI=10.4049/jimmunol.166.3.1938;
RA Dziarski R., Wang Q., Miyake K., Kirschning C.J., Gupta D.;
RT "MD-2 enables Toll-like receptor 2 (TLR2)-mediated responses to
RT lipopolysaccharide and enhances TLR2-mediated responses to Gram-positive
RT and Gram-negative bacteria and their cell wall components.";
RL J. Immunol. 166:1938-1944(2001).
RN [9]
RP DISULFIDE BONDS, GLYCOSYLATION, SUBCELLULAR LOCATION, FUNCTION, AND
RP INTERACTION WITH TLR4.
RX PubMed=11593030; DOI=10.1073/pnas.211445098;
RA Visintin A., Mazzoni A., Spitzer J.A., Segal D.M.;
RT "Secreted MD-2 is a large polymeric protein that efficiently confers
RT lipopolysaccharide sensitivity to Toll-like receptor 4.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12156-12161(2001).
RN [10]
RP INTERCHAIN DISULFIDE BOND.
RX PubMed=12642668; DOI=10.1073/pnas.0630495100;
RA Mullen G.E.D., Kennedy M.N., Visintin A., Mazzoni A., Leifer C.A.,
RA Davies D.R., Segal D.M.;
RT "The role of disulfide bonds in the assembly and function of MD-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:3919-3924(2003).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 19-158 IN COMPLEX WITH TLR4 AND
RP LIPOPOLYSACCHARIDE ANALOG, AND SUBUNIT.
RX PubMed=17803912; DOI=10.1016/j.cell.2007.08.002;
RA Kim H.M., Park B.S., Kim J.-I., Kim S.E., Lee J., Oh S.C., Enkhbayar P.,
RA Matsushima N., Lee H., Yoo O.J., Lee J.-O.;
RT "Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist
RT Eritoran.";
RL Cell 130:906-917(2007).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-160 IN COMPLEX WITH LIPID IV-A,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-26 AND ASN-114.
RX PubMed=17569869; DOI=10.1126/science.1139111;
RA Ohto U., Fukase K., Miyake K., Satow Y.;
RT "Crystal structures of human MD-2 and its complex with antiendotoxic lipid
RT IVa.";
RL Science 316:1632-1634(2007).
CC -!- FUNCTION: Binds bacterial lipopolysaccharide (LPS) (PubMed:17803912,
CC PubMed:17569869). Cooperates with TLR4 in the innate immune response to
CC bacterial lipopolysaccharide (LPS), and with TLR2 in the response to
CC cell wall components from Gram-positive and Gram-negative bacteria
CC (PubMed:11160242, PubMed:11593030). Enhances TLR4-dependent activation
CC of NF-kappa-B (PubMed:10359581). Cells expressing both LY96 and TLR4,
CC but not TLR4 alone, respond to LPS (PubMed:10359581).
CC {ECO:0000269|PubMed:10359581, ECO:0000269|PubMed:11160242,
CC ECO:0000269|PubMed:11593030, ECO:0000269|PubMed:17569869,
CC ECO:0000269|PubMed:17803912}.
CC -!- SUBUNIT: Heterogeneous homomer formed from homodimers; disulfide-linked
CC (PubMed:11593030, PubMed:12642668). Belongs to the lipopolysaccharide
CC (LPS) receptor, a multi-protein complex containing at least CD14, LY96
CC and TLR4 (PubMed:11274165). Binds to the extracellular domains of TLR2
CC and TLR4 (PubMed:10359581, PubMed:11593030, PubMed:17803912). Ligand
CC binding induces interaction with TLR4 and oligomerization of the
CC complex. {ECO:0000269|PubMed:10359581, ECO:0000269|PubMed:11274165,
CC ECO:0000269|PubMed:11593030, ECO:0000269|PubMed:17569869,
CC ECO:0000269|PubMed:17803912}.
CC -!- INTERACTION:
CC Q9Y6Y9; P80188: LCN2; NbExp=3; IntAct=EBI-1539247, EBI-11911016;
CC Q9Y6Y9; Q14696: MESD; NbExp=3; IntAct=EBI-1539247, EBI-6165891;
CC Q9Y6Y9; O00206: TLR4; NbExp=7; IntAct=EBI-1539247, EBI-528701;
CC Q9Y6Y9; O00206-1: TLR4; NbExp=5; IntAct=EBI-1539247, EBI-15745059;
CC Q9Y6Y9; P49278: DERP2; Xeno; NbExp=2; IntAct=EBI-1539247, EBI-15745025;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:10359581, ECO:0000269|PubMed:11593030,
CC ECO:0000305|PubMed:11274165}. Secreted {ECO:0000269|PubMed:11593030}.
CC Note=Retained in the extracellular space at the cell surface by
CC interaction with TLR4 (PubMed:10359581). {ECO:0000269|PubMed:10359581,
CC ECO:0000269|PubMed:11593030}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y6Y9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y6Y9-2; Sequence=VSP_055045;
CC -!- PTM: N-glycosylated; high-mannose. {ECO:0000269|PubMed:11593030,
CC ECO:0000269|PubMed:17569869}.
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DR EMBL; AB018549; BAA78717.1; -; mRNA.
DR EMBL; AF168121; AAF89635.1; -; mRNA.
DR EMBL; AB446498; BAG55275.1; -; mRNA.
DR EMBL; AC022868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020690; AAH20690.1; -; mRNA.
DR CCDS; CCDS56540.1; -. [Q9Y6Y9-2]
DR CCDS; CCDS6216.1; -. [Q9Y6Y9-1]
DR RefSeq; NP_001182726.1; NM_001195797.1. [Q9Y6Y9-2]
DR RefSeq; NP_056179.3; NM_015364.4. [Q9Y6Y9-1]
DR PDB; 2E56; X-ray; 2.00 A; A=17-160.
DR PDB; 2E59; X-ray; 2.21 A; A=17-160.
DR PDB; 2Z65; X-ray; 2.70 A; C/D=19-158.
DR PDB; 3FXI; X-ray; 3.10 A; C/D=19-160.
DR PDB; 3ULA; X-ray; 3.60 A; B/D=19-158.
DR PDB; 4G8A; X-ray; 2.40 A; C/D=17-160.
DR PDBsum; 2E56; -.
DR PDBsum; 2E59; -.
DR PDBsum; 2Z65; -.
DR PDBsum; 3FXI; -.
DR PDBsum; 3ULA; -.
DR PDBsum; 4G8A; -.
DR AlphaFoldDB; Q9Y6Y9; -.
DR SMR; Q9Y6Y9; -.
DR BioGRID; 117170; 8.
DR ComplexPortal; CPX-2545; LY96-TLR4 toll-like receptor complex.
DR DIP; DIP-38571N; -.
DR IntAct; Q9Y6Y9; 10.
DR STRING; 9606.ENSP00000284818; -.
DR BindingDB; Q9Y6Y9; -.
DR ChEMBL; CHEMBL2375202; -.
DR DrugBank; DB02767; (R)-3-hydroxytetradecanoic acid.
DR DrugBank; DB03017; Lauric acid.
DR DrugBank; DB00295; Morphine.
DR DrugBank; DB08231; Myristic acid.
DR GuidetoPHARMACOLOGY; 2890; -.
DR GlyGen; Q9Y6Y9; 2 sites.
DR iPTMnet; Q9Y6Y9; -.
DR PhosphoSitePlus; Q9Y6Y9; -.
DR BioMuta; LY96; -.
DR DMDM; 296434574; -.
DR jPOST; Q9Y6Y9; -.
DR MassIVE; Q9Y6Y9; -.
DR MaxQB; Q9Y6Y9; -.
DR PaxDb; Q9Y6Y9; -.
DR PeptideAtlas; Q9Y6Y9; -.
DR PRIDE; Q9Y6Y9; -.
DR ProteomicsDB; 16624; -.
DR ProteomicsDB; 86830; -. [Q9Y6Y9-1]
DR Antibodypedia; 12334; 485 antibodies from 38 providers.
DR DNASU; 23643; -.
DR Ensembl; ENST00000284818.7; ENSP00000284818.2; ENSG00000154589.7. [Q9Y6Y9-1]
DR Ensembl; ENST00000518893.1; ENSP00000430533.1; ENSG00000154589.7. [Q9Y6Y9-2]
DR GeneID; 23643; -.
DR KEGG; hsa:23643; -.
DR MANE-Select; ENST00000284818.7; ENSP00000284818.2; NM_015364.5; NP_056179.4.
DR UCSC; uc003yad.4; human. [Q9Y6Y9-1]
DR CTD; 23643; -.
DR DisGeNET; 23643; -.
DR GeneCards; LY96; -.
DR HGNC; HGNC:17156; LY96.
DR HPA; ENSG00000154589; Low tissue specificity.
DR MIM; 605243; gene.
DR neXtProt; NX_Q9Y6Y9; -.
DR OpenTargets; ENSG00000154589; -.
DR PharmGKB; PA134924906; -.
DR VEuPathDB; HostDB:ENSG00000154589; -.
DR eggNOG; ENOG502SD7W; Eukaryota.
DR GeneTree; ENSGT00390000000742; -.
DR HOGENOM; CLU_141711_0_0_1; -.
DR InParanoid; Q9Y6Y9; -.
DR OMA; YTYCDNM; -.
DR OrthoDB; 1320082at2759; -.
DR PhylomeDB; Q9Y6Y9; -.
DR TreeFam; TF335876; -.
DR PathwayCommons; Q9Y6Y9; -.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-140534; Caspase activation via Death Receptors in the presence of ligand.
DR Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-HSA-166058; MyD88:MAL(TIRAP) cascade initiated on plasma membrane.
DR Reactome; R-HSA-166166; MyD88-independent TLR4 cascade.
DR Reactome; R-HSA-2562578; TRIF-mediated programmed cell death.
DR Reactome; R-HSA-5602498; MyD88 deficiency (TLR2/4).
DR Reactome; R-HSA-5603041; IRAK4 deficiency (TLR2/4).
DR Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
DR Reactome; R-HSA-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
DR Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
DR Reactome; R-HSA-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR Reactome; R-HSA-9707616; Heme signaling.
DR Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR SignaLink; Q9Y6Y9; -.
DR SIGNOR; Q9Y6Y9; -.
DR BioGRID-ORCS; 23643; 15 hits in 1008 CRISPR screens.
DR ChiTaRS; LY96; human.
DR EvolutionaryTrace; Q9Y6Y9; -.
DR GeneWiki; Lymphocyte_antigen_96; -.
DR GenomeRNAi; 23643; -.
DR Pharos; Q9Y6Y9; Tchem.
DR PRO; PR:Q9Y6Y9; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9Y6Y9; protein.
DR Bgee; ENSG00000154589; Expressed in monocyte and 172 other tissues.
DR Genevisible; Q9Y6Y9; HS.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0046696; C:lipopolysaccharide receptor complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IPI:ComplexPortal.
DR GO; GO:0015026; F:coreceptor activity; TAS:ProtInc.
DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:InterPro.
DR GO; GO:0001875; F:lipopolysaccharide immune receptor activity; IDA:UniProtKB.
DR GO; GO:0035662; F:Toll-like receptor 4 binding; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0032497; P:detection of lipopolysaccharide; IDA:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IC:ComplexPortal.
DR GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISS:UniProtKB.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IDA:ComplexPortal.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR039217; LY96.
DR InterPro; IPR003172; ML_dom.
DR PANTHER; PTHR15218; PTHR15218; 1.
DR SMART; SM00737; ML; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein; Immunity;
KW Inflammatory response; Innate immunity; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..160
FT /note="Lymphocyte antigen 96"
FT /id="PRO_0000018619"
FT REGION 119..123
FT /note="Interaction with lipopolysaccharide"
FT /evidence="ECO:0000269|PubMed:17569869,
FT ECO:0000269|PubMed:17803912, ECO:0007744|PDB:2E56,
FT ECO:0007744|PDB:2E59, ECO:0007744|PDB:4G8A"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17569869,
FT ECO:0007744|PDB:2E56, ECO:0007744|PDB:2E59"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17569869,
FT ECO:0007744|PDB:2E56, ECO:0007744|PDB:2E59"
FT DISULFID 25..51
FT /evidence="ECO:0000269|PubMed:17569869,
FT ECO:0000269|PubMed:17803912, ECO:0007744|PDB:2E56,
FT ECO:0007744|PDB:2E59, ECO:0007744|PDB:2Z65"
FT DISULFID 37..148
FT /evidence="ECO:0000269|PubMed:17569869,
FT ECO:0000269|PubMed:17803912, ECO:0007744|PDB:2E56,
FT ECO:0007744|PDB:2E59, ECO:0007744|PDB:2Z65"
FT DISULFID 95..105
FT /evidence="ECO:0000269|PubMed:17569869,
FT ECO:0000269|PubMed:17803912, ECO:0007744|PDB:2E56,
FT ECO:0007744|PDB:2E59, ECO:0007744|PDB:2Z65"
FT VAR_SEQ 38..68
FT /note="DKMQYPISINVNPCIELKRSKGLLHIFYIPR -> G (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055045"
FT VARIANT 56
FT /note="R -> G (in dbSNP:rs6472812)"
FT /evidence="ECO:0000269|PubMed:10359581,
FT ECO:0000269|PubMed:10891475, ECO:0000269|PubMed:11435474,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:18810425"
FT /id="VAR_050030"
FT VARIANT 157
FT /note="P -> S (in dbSNP:rs11466004)"
FT /id="VAR_024532"
FT MUTAGEN 95
FT /note="C->Y: Abolishes LPS-response."
FT /evidence="ECO:0000269|PubMed:11435474"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:2E56"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:2E56"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:4G8A"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:2E56"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:2E56"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:2E56"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:2E56"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:2E56"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:2E56"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:2E56"
FT STRAND 129..139
FT /evidence="ECO:0007829|PDB:2E56"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:2E56"
FT STRAND 144..155
FT /evidence="ECO:0007829|PDB:2E56"
SQ SEQUENCE 160 AA; 18546 MW; 0F92AFF583637C6B CRC64;
MLPFLFFSTL FSSIFTEAQK QYWVCNSSDA SISYTYCDKM QYPISINVNP CIELKRSKGL
LHIFYIPRRD LKQLYFNLYI TVNTMNLPKR KEVICRGSDD DYSFCRALKG ETVNTTISFS
FKGIKFSKGK YKCVVEAISG SPEEMLFCLE FVILHQPNSN
