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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.
R-MMU-5686938. Regulation of TLR by endogenous ligand.

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)DescriptionActionsGraphical viewLength
Mutagenesisi126F → A: Abolishes dimerization of the TLR4 complex and stimulation of TNF production in response to bacterial lipopolysaccharide. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3038514.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000001862019 – 160Lymphocyte antigen 96Add BLAST142

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi25 ↔ 51Combined sources2 Publications
Glycosylationi26N-linked (GlcNAc...)Combined sources1 Publication1
Disulfide bondi37 ↔ 148Combined sources2 Publications
Disulfide bondi95 ↔ 105Combined sources2 Publications
Glycosylationi114N-linked (GlcNAc...)1 Publication1
Glycosylationi150N-linked (GlcNAc...)1 Publication1

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9JHF9.
PaxDbiQ9JHF9.
PRIDEiQ9JHF9.

PTM databases

PhosphoSitePlusiQ9JHF9.

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

BgeeiENSMUSG00000025779.
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 interactor.
STRINGi10090.ENSMUSP00000026881.

Structurei

Secondary structure

1160
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 26Combined sources4
Beta strandi31 – 37Combined sources7
Beta strandi44 – 50Combined sources7
Beta strandi57 – 65Combined sources9
Beta strandi74 – 82Combined sources9
Beta strandi90 – 94Combined sources5
Beta strandi97 – 99Combined sources3
Helixi103 – 106Combined sources4
Beta strandi113 – 121Combined sources9
Beta strandi128 – 139Combined sources12
Turni140 – 142Combined sources3
Beta strandi145 – 154Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Z64X-ray2.84C21-155[»]
3VQ1X-ray2.70C/D17-160[»]
3VQ2X-ray2.48C/D17-160[»]
5IJBX-ray2.91C/D19-160[»]
5IJCX-ray2.57C/D19-160[»]
5IJDX-ray2.70C/D19-160[»]
ProteinModelPortaliQ9JHF9.
SMRiQ9JHF9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JHF9.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni119 – 123Interaction with lipopolysaccharideBy similarity1 Publication5

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J4Q5. Eukaryota.
ENOG411154R. LUCA.
GeneTreeiENSGT00390000000742.
HOGENOMiHOG000001152.
HOVERGENiHBG032514.
InParanoidiQ9JHF9.
KOiK05400.
OMAiIFTEAQK.
OrthoDBiEOG091G0T85.
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.
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.
UniGeneiMm.116844.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Z64X-ray2.84C21-155[»]
3VQ1X-ray2.70C/D17-160[»]
3VQ2X-ray2.48C/D17-160[»]
5IJBX-ray2.91C/D19-160[»]
5IJCX-ray2.57C/D19-160[»]
5IJDX-ray2.70C/D19-160[»]
ProteinModelPortaliQ9JHF9.
SMRiQ9JHF9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

ChEMBLiCHEMBL3038514.

PTM databases

PhosphoSitePlusiQ9JHF9.

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.
OrthoDBiEOG091G0T85.
PhylomeDBiQ9JHF9.
TreeFamiTF335876.

Enzyme and pathway databases

ReactomeiR-MMU-166016. Toll Like Receptor 4 (TLR4) Cascade.
R-MMU-166166. MyD88-independent TLR3/TLR4 cascade.
R-MMU-5686938. Regulation of TLR by endogenous ligand.

Miscellaneous databases

EvolutionaryTraceiQ9JHF9.
PROiQ9JHF9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000025779.
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...

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: November 2, 2016
This is version 124 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.