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Lymphocyte antigen 96 (Ly-96) (ESOP-1) (Protein MD-2)

 LY96_HUMAN              Reviewed;         160 AA.
Q9Y6Y9; B3Y6A5; E5RJJ7;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
25-OCT-2017, entry version 154.
RecName: Full=Lymphocyte antigen 96;
Short=Ly-96;
AltName: Full=ESOP-1 {ECO:0000303|PubMed:10891475};
AltName: Full=Protein MD-2 {ECO:0000303|PubMed:10359581};
Flags: Precursor;
Name=LY96; Synonyms=ESOP1, MD2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-56, FUNCTION,
INTERACTION WITH TLR4, AND SUBCELLULAR LOCATION.
TISSUE=Uterus;
PubMed=10359581; DOI=10.1084/jem.189.11.1777;
Shimazu R., Akashi S., Ogata H., Nagai Y., Fukudome K., Miyake K.,
Kimoto M.;
"MD-2, a molecule that confers lipopolysaccharide responsiveness on
Toll-like receptor 4.";
J. Exp. Med. 189:1777-1782(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-56.
PubMed=10891475;
Kato K., Morrison A.M., Nakano T., Tashiro K., Honjo T.;
"ESOP-1, a secreted protein expressed in the hematopoietic, nervous,
and reproductive systems of embryonic and adult mice.";
Blood 96:362-364(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF CYS-95, AND
VARIANT GLY-56.
PubMed=11435474; DOI=10.1084/jem.194.1.79;
Schromm A.B., Lien E., Henneke P., Chow J.C., Yoshimura A., Heine H.,
Latz E., Monks B.G., Schwartz D.A., Miyake K., Golenbock D.T.;
"Molecular genetic analysis of an endotoxin nonresponder mutant cell
line. A point mutation in a conserved region of MD-2 abolishes
endotoxin-induced signaling.";
J. Exp. Med. 194:79-88(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-56.
PubMed=18810425; DOI=10.1007/s00251-008-0332-0;
Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T.,
Kimura A.;
"Natural selection in the TLR-related genes in the course of primate
evolution.";
Immunogenetics 60:727-735(2008).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLY-56.
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=11274165; DOI=10.1074/jbc.M009164200;
da Silva Correia J., Soldau K., Christen U., Tobias P.S.,
Ulevitch R.J.;
"Lipopolysaccharide is in close proximity to each of the proteins in
its membrane receptor complex. transfer from CD14 to TLR4 and MD-2.";
J. Biol. Chem. 276:21129-21135(2001).
[8]
INTERACTION WITH TLR2 AND TLR4, AND FUNCTION.
PubMed=11160242; DOI=10.4049/jimmunol.166.3.1938;
Dziarski R., Wang Q., Miyake K., Kirschning C.J., Gupta D.;
"MD-2 enables Toll-like receptor 2 (TLR2)-mediated responses to
lipopolysaccharide and enhances TLR2-mediated responses to Gram-
positive and Gram-negative bacteria and their cell wall components.";
J. Immunol. 166:1938-1944(2001).
[9]
DISULFIDE BONDS, GLYCOSYLATION, SUBCELLULAR LOCATION, FUNCTION, AND
INTERACTION WITH TLR4.
PubMed=11593030; DOI=10.1073/pnas.211445098;
Visintin A., Mazzoni A., Spitzer J.A., Segal D.M.;
"Secreted MD-2 is a large polymeric protein that efficiently confers
lipopolysaccharide sensitivity to Toll-like receptor 4.";
Proc. Natl. Acad. Sci. U.S.A. 98:12156-12161(2001).
[10]
INTERCHAIN DISULFIDE BOND.
PubMed=12642668; DOI=10.1073/pnas.0630495100;
Mullen G.E.D., Kennedy M.N., Visintin A., Mazzoni A., Leifer C.A.,
Davies D.R., Segal D.M.;
"The role of disulfide bonds in the assembly and function of MD-2.";
Proc. Natl. Acad. Sci. U.S.A. 100:3919-3924(2003).
[11]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 19-158 IN COMPLEX WITH TLR4
AND LIPOPOLYSACCHARIDE ANALOG, AND SUBUNIT.
PubMed=17803912; DOI=10.1016/j.cell.2007.08.002;
Kim H.M., Park B.S., Kim J.-I., Kim S.E., Lee J., Oh S.C.,
Enkhbayar P., Matsushima N., Lee H., Yoo O.J., Lee J.-O.;
"Crystal structure of the TLR4-MD-2 complex with bound endotoxin
antagonist Eritoran.";
Cell 130:906-917(2007).
[12]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-160 IN COMPLEX WITH LIPID
IV-A, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-26 AND ASN-114.
PubMed=17569869; DOI=10.1126/science.1139111;
Ohto U., Fukase K., Miyake K., Satow Y.;
"Crystal structures of human MD-2 and its complex with antiendotoxic
lipid IVa.";
Science 316:1632-1634(2007).
-!- FUNCTION: Binds bacterial lipopolysaccharide (LPS)
(PubMed:17803912, PubMed:17569869). Cooperates with TLR4 in the
innate immune response to bacterial lipopolysaccharide (LPS), and
with TLR2 in the response to cell wall components from Gram-
positive and Gram-negative bacteria (PubMed:11160242,
PubMed:11593030). Enhances TLR4-dependent activation of NF-kappa-B
(PubMed:10359581). Cells expressing both LY96 and TLR4, but not
TLR4 alone, respond to LPS (PubMed:10359581).
{ECO:0000269|PubMed:10359581, ECO:0000269|PubMed:11160242,
ECO:0000269|PubMed:11593030, ECO:0000269|PubMed:17569869,
ECO:0000269|PubMed:17803912}.
-!- SUBUNIT: Heterogeneous homopolymer formed from homodimers;
disulfide-linked (PubMed:11593030, PubMed:12642668). Belongs to
the lipopolysaccharide (LPS) receptor, a multi-protein complex
containing at least CD14, LY96 and TLR4 (PubMed:11274165). Binds
to the extracellular domains of TLR2 and TLR4 (PubMed:10359581,
PubMed:11593030, PubMed:17803912). Ligand binding induces
interaction with TLR4 and oligomerization of the complex.
{ECO:0000269|PubMed:10359581, ECO:0000269|PubMed:11274165,
ECO:0000269|PubMed:11593030, ECO:0000269|PubMed:17569869,
ECO:0000269|PubMed:17803912}.
-!- INTERACTION:
P49278:DERP2 (xeno); NbExp=2; IntAct=EBI-1539247, EBI-15745025;
O00206:TLR4; NbExp=5; IntAct=EBI-1539247, EBI-528701;
O00206-1:TLR4; NbExp=5; IntAct=EBI-1539247, EBI-15745059;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space
{ECO:0000269|PubMed:10359581, ECO:0000269|PubMed:11593030,
ECO:0000305|PubMed:11274165}. Secreted
{ECO:0000269|PubMed:11593030}. Note=Retained in the extracellular
space at the cell surface by interaction with TLR4
(PubMed:10359581). {ECO:0000269|PubMed:10359581,
ECO:0000269|PubMed:11593030}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y6Y9-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y6Y9-2; Sequence=VSP_055045;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- PTM: N-glycosylated; high-mannose. {ECO:0000269|PubMed:11593030,
ECO:0000269|PubMed:17569869}.
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EMBL; AB018549; BAA78717.1; -; mRNA.
EMBL; AF168121; AAF89635.1; -; mRNA.
EMBL; AB446498; BAG55275.1; -; mRNA.
EMBL; AC022868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC087672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC020690; AAH20690.1; -; mRNA.
CCDS; CCDS56540.1; -. [Q9Y6Y9-2]
CCDS; CCDS6216.1; -. [Q9Y6Y9-1]
RefSeq; NP_001182726.1; NM_001195797.1. [Q9Y6Y9-2]
RefSeq; NP_056179.3; NM_015364.4.
UniGene; Hs.726603; -.
PDB; 1T2Z; Model; -; A=19-160.
PDB; 2E56; X-ray; 2.00 A; A=17-160.
PDB; 2E59; X-ray; 2.21 A; A=17-160.
PDB; 2Z65; X-ray; 2.70 A; C/D=19-158.
PDB; 3FXI; X-ray; 3.10 A; C/D=19-160.
PDB; 3ULA; X-ray; 3.60 A; B/D=19-158.
PDB; 4G8A; X-ray; 2.40 A; C/D=17-160.
PDBsum; 1T2Z; -.
PDBsum; 2E56; -.
PDBsum; 2E59; -.
PDBsum; 2Z65; -.
PDBsum; 3FXI; -.
PDBsum; 3ULA; -.
PDBsum; 4G8A; -.
ProteinModelPortal; Q9Y6Y9; -.
SMR; Q9Y6Y9; -.
BioGrid; 117170; 4.
DIP; DIP-38571N; -.
IntAct; Q9Y6Y9; 7.
STRING; 9606.ENSP00000284818; -.
ChEMBL; CHEMBL2375202; -.
DrugBank; DB02767; 3-Hydroxy-Myristic Acid.
DrugBank; DB03017; Lauric Acid.
DrugBank; DB08231; MYRISTIC ACID.
GuidetoPHARMACOLOGY; 2890; -.
iPTMnet; Q9Y6Y9; -.
PhosphoSitePlus; Q9Y6Y9; -.
BioMuta; LY96; -.
DMDM; 296434574; -.
PaxDb; Q9Y6Y9; -.
PeptideAtlas; Q9Y6Y9; -.
PRIDE; Q9Y6Y9; -.
Ensembl; ENST00000284818; ENSP00000284818; ENSG00000154589. [Q9Y6Y9-1]
Ensembl; ENST00000518893; ENSP00000430533; ENSG00000154589. [Q9Y6Y9-2]
GeneID; 23643; -.
KEGG; hsa:23643; -.
UCSC; uc003yad.4; human. [Q9Y6Y9-1]
CTD; 23643; -.
DisGeNET; 23643; -.
EuPathDB; HostDB:ENSG00000154589.6; -.
GeneCards; LY96; -.
HGNC; HGNC:17156; LY96.
HPA; HPA053060; -.
MIM; 605243; gene.
neXtProt; NX_Q9Y6Y9; -.
OpenTargets; ENSG00000154589; -.
PharmGKB; PA134924906; -.
eggNOG; ENOG410J4Q5; Eukaryota.
eggNOG; ENOG411154R; LUCA.
GeneTree; ENSGT00390000000742; -.
HOGENOM; HOG000001152; -.
HOVERGEN; HBG032514; -.
InParanoid; Q9Y6Y9; -.
KO; K05400; -.
OMA; YIPRRDI; -.
OrthoDB; EOG091G0T85; -.
PhylomeDB; Q9Y6Y9; -.
TreeFam; TF335876; -.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-140534; Ligand-dependent caspase activation.
Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
Reactome; R-HSA-166058; MyD88:Mal cascade initiated on plasma membrane.
Reactome; R-HSA-166166; MyD88-independent TLR3/TLR4 cascade.
Reactome; R-HSA-2562578; TRIF-mediated programmed cell death.
Reactome; R-HSA-5602498; MyD88 deficiency (TLR2/4).
Reactome; R-HSA-5603041; IRAK4 deficiency (TLR2/4).
Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-HSA-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
Reactome; R-HSA-937072; TRAF6 mediated induction of TAK1 complex.
Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
SIGNOR; Q9Y6Y9; -.
EvolutionaryTrace; Q9Y6Y9; -.
GeneWiki; Lymphocyte_antigen_96; -.
GenomeRNAi; 23643; -.
PRO; PR:Q9Y6Y9; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000154589; -.
CleanEx; HS_LY96; -.
Genevisible; Q9Y6Y9; HS.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
GO; GO:0046696; C:lipopolysaccharide receptor complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0015026; F:coreceptor activity; TAS:ProtInc.
GO; GO:0001875; F:lipopolysaccharide receptor activity; IDA:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
GO; GO:0032497; P:detection of lipopolysaccharide; IDA:UniProtKB.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0070266; P:necroptotic process; TAS:Reactome.
GO; GO:0034128; P:negative regulation of MyD88-independent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI.
GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISS:UniProtKB.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR003172; ML_dom.
Pfam; PF02221; E1_DerP2_DerF2; 1.
SMART; SM00737; ML; 1.
SUPFAM; SSF81296; SSF81296; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
Glycoprotein; Immunity; Inflammatory response; Innate immunity;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 160 Lymphocyte antigen 96.
/FTId=PRO_0000018619.
REGION 119 123 Interaction with lipopolysaccharide.
{ECO:0000244|PDB:2E56,
ECO:0000244|PDB:2E59,
ECO:0000244|PDB:4G8A,
ECO:0000269|PubMed:17569869,
ECO:0000269|PubMed:17803912}.
CARBOHYD 26 26 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:2E56,
ECO:0000244|PDB:2E59,
ECO:0000269|PubMed:17569869}.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:2E56,
ECO:0000244|PDB:2E59,
ECO:0000269|PubMed:17569869}.
DISULFID 25 51 {ECO:0000244|PDB:2E56,
ECO:0000244|PDB:2E59,
ECO:0000244|PDB:2Z65,
ECO:0000269|PubMed:17569869,
ECO:0000269|PubMed:17803912}.
DISULFID 37 148 {ECO:0000244|PDB:2E56,
ECO:0000244|PDB:2E59,
ECO:0000244|PDB:2Z65,
ECO:0000269|PubMed:17569869,
ECO:0000269|PubMed:17803912}.
DISULFID 95 105 {ECO:0000244|PDB:2E56,
ECO:0000244|PDB:2E59,
ECO:0000244|PDB:2Z65,
ECO:0000269|PubMed:17569869,
ECO:0000269|PubMed:17803912}.
VAR_SEQ 38 68 DKMQYPISINVNPCIELKRSKGLLHIFYIPR -> G (in
isoform 2). {ECO:0000305}.
/FTId=VSP_055045.
VARIANT 56 56 R -> G (in dbSNP:rs6472812).
{ECO:0000269|PubMed:10359581,
ECO:0000269|PubMed:10891475,
ECO:0000269|PubMed:11435474,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:18810425}.
/FTId=VAR_050030.
VARIANT 157 157 P -> S (in dbSNP:rs11466004).
/FTId=VAR_024532.
MUTAGEN 95 95 C->Y: Abolishes LPS-response.
{ECO:0000269|PubMed:11435474}.
STRAND 22 26 {ECO:0000244|PDB:2E56}.
STRAND 28 36 {ECO:0000244|PDB:2E56}.
STRAND 38 40 {ECO:0000244|PDB:4G8A}.
STRAND 45 50 {ECO:0000244|PDB:2E56}.
STRAND 57 65 {ECO:0000244|PDB:2E56}.
STRAND 75 82 {ECO:0000244|PDB:2E56}.
STRAND 90 93 {ECO:0000244|PDB:2E56}.
STRAND 97 101 {ECO:0000244|PDB:2E56}.
HELIX 103 106 {ECO:0000244|PDB:2E56}.
STRAND 113 121 {ECO:0000244|PDB:2E56}.
STRAND 129 139 {ECO:0000244|PDB:2E56}.
TURN 140 143 {ECO:0000244|PDB:2E56}.
STRAND 144 155 {ECO:0000244|PDB:2E56}.
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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