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Q9JHF9 (LY96_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lymphocyte antigen 96

Short name=Ly-96
Alternative name(s):
ESOP-1
Protein MD-2
Gene names
Name:Ly96
Synonyms:Esop1, Md2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length160 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 MD2 and TLR4, but not TLR4 alone, respond to LPS By similarity.

Subunit structure

Heterogeneous homopolymer formed from homodimers; disulfide-linked. Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, LY96 and TLR4. Binds to the extracellular domains of TLR2 and TLR4. Ligand binding induces interaction with TLR4 and oligomerization of the complex By similarity. Ref.4

Subcellular location

Secretedextracellular space.

Tissue specificity

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Tlr4Q9QUK63EBI-1534566,EBI-1534575

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 160142Lymphocyte antigen 96
PRO_0000018620

Amino acid modifications

Glycosylation261N-linked (GlcNAc...) Ref.4
Glycosylation1141N-linked (GlcNAc...) Ref.4
Glycosylation1501N-linked (GlcNAc...) Ref.4
Disulfide bond25 ↔ 51 Ref.4
Disulfide bond37 ↔ 148 Ref.4
Disulfide bond95 ↔ 105 Ref.4

Secondary structure

........................ 160
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9JHF9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: E224D17E5D5429E2

FASTA16018,394
        10         20         30         40         50         60 
MLPFILFSTL LSPILTESEK QQWFCNSSDA IISYSYCDHL KFPISISSEP CIRLRGTNGF 

        70         80         90        100        110        120 
VHVEFIPRGN LKYLYFNLFI SVNSIELPKR KEVLCHGHDD DYSFCRALKG ETVNTSIPFS 

       130        140        150        160 
FEGILFPKGH YRCVAEAIAG DTEEKLFCLN FTIIHRRDVN 

« Hide

References

« Hide 'large scale' references
[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].
[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].
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. expand/collapse author list , 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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF168120 mRNA. Translation: AAF89634.1.
AB018550 mRNA. Translation: BAA93619.1.
AK019283 mRNA. Translation: BAB31645.1.
CCDSCCDS14832.1.
RefSeqNP_001153183.1. NM_001159711.1.
NP_058619.1. NM_016923.2.
XP_006495518.1. XM_006495455.1.
XP_006495519.1. XM_006495456.1.
UniGeneMm.116844.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z64X-ray2.84C21-155[»]
3VQ1X-ray2.70C/D17-160[»]
3VQ2X-ray2.48C/D17-160[»]
ProteinModelPortalQ9JHF9.
SMRQ9JHF9. Positions 21-155.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-38572N.
IntActQ9JHF9. 1 interaction.

Chemistry

ChEMBLCHEMBL3038514.

PTM databases

PhosphoSiteQ9JHF9.

Proteomic databases

PRIDEQ9JHF9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026881; ENSMUSP00000026881; ENSMUSG00000025779.
GeneID17087.
KEGGmmu:17087.
UCSCuc007ajz.2. mouse.

Organism-specific databases

CTD23643.
MGIMGI:1341909. Ly96.

Phylogenomic databases

eggNOGNOG46291.
GeneTreeENSGT00390000000742.
HOGENOMHOG000001152.
HOVERGENHBG032514.
InParanoidQ9JHF9.
KOK05400.
OMAIPRRDIK.
OrthoDBEOG7QG45N.
PhylomeDBQ9JHF9.
TreeFamTF335876.

Gene expression databases

ArrayExpressQ9JHF9.
BgeeQ9JHF9.
CleanExMM_LY96.
GenevestigatorQ9JHF9.

Family and domain databases

Gene3D2.60.40.770. 1 hit.
InterProIPR014756. Ig_E-set.
IPR003172. ML_dom.
[Graphical view]
PfamPF02221. E1_DerP2_DerF2. 1 hit.
[Graphical view]
SMARTSM00737. ML. 1 hit.
[Graphical view]
SUPFAMSSF81296. SSF81296. 1 hit.
ProtoNetSearch...

Other

ChiTaRSLY96. mouse.
EvolutionaryTraceQ9JHF9.
NextBio291228.
PROQ9JHF9.
SOURCESearch...

Entry information

Entry nameLY96_MOUSE
AccessionPrimary (citable) accession number: Q9JHF9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot