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Database: UniProt
Entry: Q9Y6Y9
LinkDB: Q9Y6Y9
Original site: Q9Y6Y9 
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   29-SEP-2021, entry version 182.
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; 1T2Z; Model; -; A=19-160.
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; 1T2Z; -.
DR   PDBsum; 2E56; -.
DR   PDBsum; 2E59; -.
DR   PDBsum; 2Z65; -.
DR   PDBsum; 3FXI; -.
DR   PDBsum; 3ULA; -.
DR   PDBsum; 4G8A; -.
DR   SMR; Q9Y6Y9; -.
DR   BioGRID; 117170; 8.
DR   DIP; DIP-38571N; -.
DR   IntAct; Q9Y6Y9; 8.
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   PaxDb; Q9Y6Y9; -.
DR   PeptideAtlas; Q9Y6Y9; -.
DR   PRIDE; Q9Y6Y9; -.
DR   ProteomicsDB; 16624; -.
DR   ProteomicsDB; 86830; -. [Q9Y6Y9-1]
DR   Antibodypedia; 12334; 483 antibodies.
DR   DNASU; 23643; -.
DR   Ensembl; ENST00000284818; ENSP00000284818; ENSG00000154589. [Q9Y6Y9-1]
DR   Ensembl; ENST00000518893; ENSP00000430533; ENSG00000154589. [Q9Y6Y9-2]
DR   GeneID; 23643; -.
DR   KEGG; hsa:23643; -.
DR   UCSC; uc003yad.4; human. [Q9Y6Y9-1]
DR   CTD; 23643; -.
DR   DisGeNET; 23643; -.
DR   GeneCards; LY96; -.
DR   HGNC; HGNC:17156; LY96.
DR   HPA; ENSG00000154589; Tissue enhanced (blood).
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; EVICRGY; -.
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   SIGNOR; Q9Y6Y9; -.
DR   BioGRID-ORCS; 23643; 8 hits in 946 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 212 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: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; IEA:UniProtKB-KW.
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   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
//
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