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

 LY96_MOUSE              Reviewed;         160 AA.
Q9JHF9;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
30-AUG-2017, entry version 129.
RecName: Full=Lymphocyte antigen 96;
Short=Ly-96;
AltName: Full=ESOP-1 {ECO:0000303|PubMed:10891475};
AltName: Full=Protein MD-2;
Flags: Precursor;
Name=Ly96; Synonyms=Esop1, Md2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT,
AND INTERACTION WITH TLR4.
TISSUE=Kidney;
PubMed=10725698; DOI=10.4049/jimmunol.164.7.3471;
Akashi S., Shimazu R., Ogata H., Nagai Y., Takeda K., Kimoto M.,
Miyake K.;
"Cell surface expression and lipopolysaccaride signaling via the Toll-
like receptor 4-MD-2 complex on mouse peritoneal macrophages.";
J. Immunol. 164:3471-3475(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-126.
PubMed=20133493; DOI=10.1093/intimm/dxq005;
Tsukamoto H., Fukudome K., Takao S., Tsuneyoshi N., Kimoto M.;
"Lipopolysaccharide-binding protein-mediated Toll-like receptor 4
dimerization enables rapid signal transduction against
lipopolysaccharide stimulation on membrane-associated CD14-expressing
cells.";
Int. Immunol. 22:271-280(2010).
[5]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=24380872; DOI=10.1093/intimm/dxt071;
Tanimura N., Saitoh S., Ohto U., Akashi-Takamura S., Fujimoto Y.,
Fukase K., Shimizu T., Miyake K.;
"The attenuated inflammation of MPL is due to the lack of CD14-
dependent tight dimerization of the TLR4/MD2 complex at the plasma
membrane.";
Int. Immunol. 26:307-314(2014).
[6]
X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) OF 21-155 IN COMPLEX WITH TLR4,
GLYCOSYLATION AT ASN-26; ASN-114 AND ASN-150, AND DISULFIDE BONDS.
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).
[7]
X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 17-160 IN COMPLEX WITH TLR4
AND LIPID X, DISULFIDE BONDS, AND INTERACTION WITH TLR4.
PubMed=22532668; DOI=10.1073/pnas.1201193109;
Ohto U., Fukase K., Miyake K., Shimizu T.;
"Structural basis of species-specific endotoxin sensing by innate
immune receptor TLR4/MD-2.";
Proc. Natl. Acad. Sci. U.S.A. 109:7421-7426(2012).
-!- FUNCTION: Binds bacterial lipopolysaccharide (LPS)
(PubMed:22532668). 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. Enhances TLR4-dependent activation of NF-kappa-
B. Cells expressing both LY96 and TLR4, but not TLR4 alone,
respond to LPS (PubMed:10725698). {ECO:0000250|UniProtKB:Q9Y6Y9,
ECO:0000269|PubMed:10725698, ECO:0000269|PubMed:20133493,
ECO:0000269|PubMed:24380872}.
-!- SUBUNIT: Heterogeneous homopolymer formed from homodimers;
disulfide-linked (By similarity). Belongs to the
lipopolysaccharide (LPS) receptor, a multi-protein complex
containing at least CD14, LY96 and TLR4 (PubMed:10725698,
PubMed:20133493, PubMed:24380872). Binds to the extracellular
domain of TLR4 (PubMed:10725698, PubMed:20133493, PubMed:24380872,
PubMed:17803912, PubMed:22532668). Binds to the extracellular
domain of TLR2 (By similarity). Ligand binding induces interaction
with TLR4 and oligomerization of the complex (PubMed:20133493,
PubMed:24380872, PubMed:22532668). {ECO:0000250|UniProtKB:Q9Y6Y9,
ECO:0000269|PubMed:10725698, ECO:0000269|PubMed:17803912,
ECO:0000269|PubMed:20133493, ECO:0000269|PubMed:22532668,
ECO:0000269|PubMed:24380872}.
-!- INTERACTION:
Q9QUK6:Tlr4; NbExp=3; IntAct=EBI-1534566, EBI-1534575;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space
{ECO:0000269|PubMed:10725698, ECO:0000269|PubMed:20133493,
ECO:0000305|PubMed:24380872}. Secreted
{ECO:0000269|PubMed:10891475}. Note=Retained in the extracellular
space at the cell surface by interaction with TLR4.
{ECO:0000269|PubMed:10725698, ECO:0000269|PubMed:20133493,
ECO:0000305|PubMed:24380872}.
-!- TISSUE SPECIFICITY: Highly expressed in spleen, bone marrow,
thymus, liver, kidney, ovary and decidua. Detected at lower levels
in testis, small intestine and skin.
{ECO:0000269|PubMed:10891475}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:17803912}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF168120; AAF89634.1; -; mRNA.
EMBL; AB018550; BAA93619.1; -; mRNA.
EMBL; AK019283; BAB31645.1; -; mRNA.
CCDS; CCDS14832.1; -.
RefSeq; NP_001153183.1; NM_001159711.1.
RefSeq; NP_058619.1; NM_016923.2.
UniGene; Mm.116844; -.
PDB; 2Z64; X-ray; 2.84 A; C=21-155.
PDB; 3VQ1; X-ray; 2.70 A; C/D=17-160.
PDB; 3VQ2; X-ray; 2.48 A; C/D=17-160.
PDB; 5IJB; X-ray; 2.91 A; C/D=19-160.
PDB; 5IJC; X-ray; 2.57 A; C/D=19-160.
PDB; 5IJD; X-ray; 2.70 A; C/D=19-160.
PDBsum; 2Z64; -.
PDBsum; 3VQ1; -.
PDBsum; 3VQ2; -.
PDBsum; 5IJB; -.
PDBsum; 5IJC; -.
PDBsum; 5IJD; -.
ProteinModelPortal; Q9JHF9; -.
SMR; Q9JHF9; -.
DIP; DIP-38572N; -.
IntAct; Q9JHF9; 1.
STRING; 10090.ENSMUSP00000026881; -.
ChEMBL; CHEMBL2384895; -.
PhosphoSitePlus; Q9JHF9; -.
MaxQB; Q9JHF9; -.
PaxDb; Q9JHF9; -.
PRIDE; Q9JHF9; -.
Ensembl; ENSMUST00000026881; ENSMUSP00000026881; ENSMUSG00000025779.
GeneID; 17087; -.
KEGG; mmu:17087; -.
UCSC; uc007ajz.2; mouse.
CTD; 23643; -.
MGI; MGI:1341909; Ly96.
eggNOG; ENOG410J4Q5; Eukaryota.
eggNOG; ENOG411154R; LUCA.
GeneTree; ENSGT00390000000742; -.
HOGENOM; HOG000001152; -.
HOVERGEN; HBG032514; -.
InParanoid; Q9JHF9; -.
KO; K05400; -.
OMA; YIPRRDI; -.
OrthoDB; EOG091G0T85; -.
PhylomeDB; Q9JHF9; -.
TreeFam; TF335876; -.
Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade.
Reactome; R-MMU-166166; MyD88-independent TLR3/TLR4 cascade.
Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
EvolutionaryTrace; Q9JHF9; -.
PRO; PR:Q9JHF9; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000025779; -.
CleanEx; MM_LY96; -.
ExpressionAtlas; Q9JHF9; baseline and differential.
Genevisible; Q9JHF9; MM.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
GO; GO:0046696; C:lipopolysaccharide receptor complex; IDA:UniProtKB.
GO; GO:0001875; F:lipopolysaccharide receptor activity; ISS:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB.
GO; GO:0032497; P:detection of lipopolysaccharide; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IDA:MGI.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IMP:UniProtKB.
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; Complete proteome; Disulfide bond; Glycoprotein;
Immunity; Inflammatory response; Innate immunity; Reference proteome;
Secreted; Signal.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 160 Lymphocyte antigen 96.
/FTId=PRO_0000018620.
REGION 119 123 Interaction with lipopolysaccharide.
{ECO:0000250|UniProtKB:Q9Y6Y9,
ECO:0000269|PubMed:22532668}.
CARBOHYD 26 26 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:2Z64,
ECO:0000269|PubMed:17803912}.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17803912}.
CARBOHYD 150 150 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17803912}.
DISULFID 25 51 {ECO:0000244|PDB:2Z64,
ECO:0000244|PDB:3VQ1,
ECO:0000244|PDB:3VQ2,
ECO:0000269|PubMed:17803912,
ECO:0000269|PubMed:22532668}.
DISULFID 37 148 {ECO:0000244|PDB:2Z64,
ECO:0000244|PDB:3VQ1,
ECO:0000244|PDB:3VQ2,
ECO:0000269|PubMed:17803912,
ECO:0000269|PubMed:22532668}.
DISULFID 95 105 {ECO:0000244|PDB:2Z64,
ECO:0000244|PDB:3VQ1,
ECO:0000244|PDB:3VQ2,
ECO:0000269|PubMed:17803912,
ECO:0000269|PubMed:22532668}.
MUTAGEN 126 126 F->A: Abolishes dimerization of the TLR4
complex and stimulation of TNF production
in response to bacterial
lipopolysaccharide.
{ECO:0000269|PubMed:24380872}.
STRAND 23 26 {ECO:0000244|PDB:3VQ2}.
STRAND 31 37 {ECO:0000244|PDB:3VQ2}.
STRAND 44 50 {ECO:0000244|PDB:3VQ2}.
STRAND 57 65 {ECO:0000244|PDB:3VQ2}.
STRAND 74 82 {ECO:0000244|PDB:3VQ2}.
STRAND 90 94 {ECO:0000244|PDB:3VQ2}.
STRAND 97 99 {ECO:0000244|PDB:3VQ2}.
HELIX 103 106 {ECO:0000244|PDB:3VQ2}.
STRAND 113 121 {ECO:0000244|PDB:3VQ2}.
STRAND 128 139 {ECO:0000244|PDB:3VQ2}.
TURN 140 142 {ECO:0000244|PDB:3VQ2}.
STRAND 145 154 {ECO:0000244|PDB:3VQ2}.
SEQUENCE 160 AA; 18394 MW; E224D17E5D5429E2 CRC64;
MLPFILFSTL LSPILTESEK QQWFCNSSDA IISYSYCDHL KFPISISSEP CIRLRGTNGF
VHVEFIPRGN LKYLYFNLFI SVNSIELPKR KEVLCHGHDD DYSFCRALKG ETVNTSIPFS
FEGILFPKGH YRCVAEAIAG DTEEKLFCLN FTIIHRRDVN


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