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Protein

Lymphocyte antigen 96

Gene

Ly96

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity3 Publications

GO - Molecular functioni

GO - Biological processi

  • cellular response to lipopolysaccharide Source: UniProtKB
  • detection of lipopolysaccharide Source: UniProtKB
  • inflammatory response Source: UniProtKB-KW
  • innate immune response Source: UniProtKB-KW
  • lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  • positive regulation of lipopolysaccharide-mediated signaling pathway Source: MGI
  • positive regulation of tumor necrosis factor production Source: UniProtKB
  • response to lipopolysaccharide Source: MGI
  • toll-like receptor 4 signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

ReactomeiR-MMU-166016. Toll Like Receptor 4 (TLR4) Cascade.
R-MMU-166166. MyD88-independent TLR3/TLR4 cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Lymphocyte antigen 96
Short name:
Ly-96
Alternative name(s):
ESOP-11 Publication
Protein MD-2
Gene namesi
Name:Ly96
Synonyms:Esop1, Md2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1341909. Ly96.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi126 – 1261F → A: Abolishes dimerization of the TLR4 complex and stimulation of TNF production in response to bacterial lipopolysaccharide. 1 Publication

Chemistry

ChEMBLiCHEMBL3038514.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Chaini19 – 160142Lymphocyte antigen 96PRO_0000018620Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ 51Combined sources2 Publications
Glycosylationi26 – 261N-linked (GlcNAc...)Combined sources1 Publication
Disulfide bondi37 ↔ 148Combined sources2 Publications
Disulfide bondi95 ↔ 105Combined sources2 Publications
Glycosylationi114 – 1141N-linked (GlcNAc...)1 Publication
Glycosylationi150 – 1501N-linked (GlcNAc...)1 Publication

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9JHF9.
PaxDbiQ9JHF9.
PRIDEiQ9JHF9.

PTM databases

PhosphoSiteiQ9JHF9.

Expressioni

Tissue specificityi

Highly expressed in spleen, bone marrow, thymus, liver, kidney, ovary and decidua. Detected at lower levels in testis, small intestine and skin.1 Publication

Gene expression databases

BgeeiQ9JHF9.
CleanExiMM_LY96.
ExpressionAtlasiQ9JHF9. baseline and differential.
GenevisibleiQ9JHF9. MM.

Interactioni

Subunit structurei

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).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Tlr4Q9QUK63EBI-1534566,EBI-1534575

Protein-protein interaction databases

DIPiDIP-38572N.
IntActiQ9JHF9. 1 interaction.
STRINGi10090.ENSMUSP00000026881.

Structurei

Secondary structure

1
160
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 264Combined sources
Beta strandi31 – 377Combined sources
Beta strandi44 – 507Combined sources
Beta strandi57 – 659Combined sources
Beta strandi74 – 829Combined sources
Beta strandi90 – 945Combined sources
Beta strandi97 – 993Combined sources
Helixi103 – 1064Combined sources
Beta strandi113 – 1219Combined sources
Beta strandi128 – 13912Combined sources
Turni140 – 1423Combined sources
Beta strandi145 – 15410Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z64X-ray2.84C21-155[»]
3VQ1X-ray2.70C/D17-160[»]
3VQ2X-ray2.48C/D17-160[»]
5IJBX-ray2.91C/D22-157[»]
5IJCX-ray2.57C/D21-156[»]
5IJDX-ray2.70C/D20-156[»]
ProteinModelPortaliQ9JHF9.
SMRiQ9JHF9. Positions 21-155.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JHF9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni119 – 1235Interaction with lipopolysaccharideBy similarity1 Publication

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J4Q5. Eukaryota.
ENOG411154R. LUCA.
GeneTreeiENSGT00390000000742.
HOGENOMiHOG000001152.
HOVERGENiHBG032514.
InParanoidiQ9JHF9.
KOiK05400.
OMAiIFTEAQK.
OrthoDBiEOG7QG45N.
PhylomeDBiQ9JHF9.
TreeFamiTF335876.

Family and domain databases

Gene3Di2.60.40.770. 1 hit.
InterProiIPR014756. Ig_E-set.
IPR003172. ML_dom.
[Graphical view]
PfamiPF02221. E1_DerP2_DerF2. 1 hit.
[Graphical view]
SMARTiSM00737. ML. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JHF9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPFILFSTL LSPILTESEK QQWFCNSSDA IISYSYCDHL KFPISISSEP
60 70 80 90 100
CIRLRGTNGF VHVEFIPRGN LKYLYFNLFI SVNSIELPKR KEVLCHGHDD
110 120 130 140 150
DYSFCRALKG ETVNTSIPFS FEGILFPKGH YRCVAEAIAG DTEEKLFCLN
160
FTIIHRRDVN
Length:160
Mass (Da):18,394
Last modified:October 1, 2000 - v1
Checksum:iE224D17E5D5429E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF168120 mRNA. Translation: AAF89634.1.
AB018550 mRNA. Translation: BAA93619.1.
AK019283 mRNA. Translation: BAB31645.1.
CCDSiCCDS14832.1.
RefSeqiNP_001153183.1. NM_001159711.1.
NP_058619.1. NM_016923.2.
XP_006495519.1. XM_006495456.2.
UniGeneiMm.116844.

Genome annotation databases

EnsembliENSMUST00000026881; ENSMUSP00000026881; ENSMUSG00000025779.
GeneIDi17087.
KEGGimmu:17087.
UCSCiuc007ajz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF168120 mRNA. Translation: AAF89634.1.
AB018550 mRNA. Translation: BAA93619.1.
AK019283 mRNA. Translation: BAB31645.1.
CCDSiCCDS14832.1.
RefSeqiNP_001153183.1. NM_001159711.1.
NP_058619.1. NM_016923.2.
XP_006495519.1. XM_006495456.2.
UniGeneiMm.116844.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z64X-ray2.84C21-155[»]
3VQ1X-ray2.70C/D17-160[»]
3VQ2X-ray2.48C/D17-160[»]
5IJBX-ray2.91C/D22-157[»]
5IJCX-ray2.57C/D21-156[»]
5IJDX-ray2.70C/D20-156[»]
ProteinModelPortaliQ9JHF9.
SMRiQ9JHF9. Positions 21-155.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-38572N.
IntActiQ9JHF9. 1 interaction.
STRINGi10090.ENSMUSP00000026881.

Chemistry

ChEMBLiCHEMBL3038514.

PTM databases

PhosphoSiteiQ9JHF9.

Proteomic databases

MaxQBiQ9JHF9.
PaxDbiQ9JHF9.
PRIDEiQ9JHF9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026881; ENSMUSP00000026881; ENSMUSG00000025779.
GeneIDi17087.
KEGGimmu:17087.
UCSCiuc007ajz.2. mouse.

Organism-specific databases

CTDi23643.
MGIiMGI:1341909. Ly96.

Phylogenomic databases

eggNOGiENOG410J4Q5. Eukaryota.
ENOG411154R. LUCA.
GeneTreeiENSGT00390000000742.
HOGENOMiHOG000001152.
HOVERGENiHBG032514.
InParanoidiQ9JHF9.
KOiK05400.
OMAiIFTEAQK.
OrthoDBiEOG7QG45N.
PhylomeDBiQ9JHF9.
TreeFamiTF335876.

Enzyme and pathway databases

ReactomeiR-MMU-166016. Toll Like Receptor 4 (TLR4) Cascade.
R-MMU-166166. MyD88-independent TLR3/TLR4 cascade.

Miscellaneous databases

EvolutionaryTraceiQ9JHF9.
PROiQ9JHF9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JHF9.
CleanExiMM_LY96.
ExpressionAtlasiQ9JHF9. baseline and differential.
GenevisibleiQ9JHF9. MM.

Family and domain databases

Gene3Di2.60.40.770. 1 hit.
InterProiIPR014756. Ig_E-set.
IPR003172. ML_dom.
[Graphical view]
PfamiPF02221. E1_DerP2_DerF2. 1 hit.
[Graphical view]
SMARTiSM00737. ML. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ESOP-1, a secreted protein expressed in the hematopoietic, nervous, and reproductive systems of embryonic and adult mice."
    Kato K., Morrison A.M., Nakano T., Tashiro K., Honjo T.
    Blood 96:362-364(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Cell surface expression and lipopolysaccaride signaling via the Toll-like receptor 4-MD-2 complex on mouse peritoneal macrophages."
    Akashi S., Shimazu R., Ogata H., Nagai Y., Takeda K., Kimoto M., Miyake K.
    J. Immunol. 164:3471-3475(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH TLR4.
    Tissue: Kidney.
  3. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  4. "Lipopolysaccharide-binding protein-mediated Toll-like receptor 4 dimerization enables rapid signal transduction against lipopolysaccharide stimulation on membrane-associated CD14-expressing cells."
    Tsukamoto H., Fukudome K., Takao S., Tsuneyoshi N., Kimoto M.
    Int. Immunol. 22:271-280(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-126.
  5. "The attenuated inflammation of MPL is due to the lack of CD14-dependent tight dimerization of the TLR4/MD2 complex at the plasma membrane."
    Tanimura N., Saitoh S., Ohto U., Akashi-Takamura S., Fujimoto Y., Fukase K., Shimizu T., Miyake K.
    Int. Immunol. 26:307-314(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  6. "Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran."
    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.
    Cell 130:906-917(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) OF 21-155 IN COMPLEX WITH TLR4, GLYCOSYLATION AT ASN-26; ASN-114 AND ASN-150, DISULFIDE BONDS.
  7. "Structural basis of species-specific endotoxin sensing by innate immune receptor TLR4/MD-2."
    Ohto U., Fukase K., Miyake K., Shimizu T.
    Proc. Natl. Acad. Sci. U.S.A. 109:7421-7426(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 17-160 IN COMPLEX WITH TLR4 AND LIPID X, DISULFIDE BONDS, INTERACTION WITH TLR4.

Entry informationi

Entry nameiLY96_MOUSE
AccessioniPrimary (citable) accession number: Q9JHF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.