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Q9JHF9

- LY96_MOUSE

UniProt

Q9JHF9 - LY96_MOUSE

Protein

Lymphocyte antigen 96

Gene

Ly96

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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.By similarity

    GO - Molecular functioni

    1. lipopolysaccharide receptor activity Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. detection of lipopolysaccharide Source: UniProtKB
    2. inflammatory response Source: UniProtKB-KW
    3. innate immune response Source: UniProtKB-KW
    4. positive regulation of lipopolysaccharide-mediated signaling pathway Source: MGI

    Keywords - Biological processi

    Immunity, Inflammatory response, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_196636. TRIF-mediated programmed cell death.
    REACT_198539. TRAF6 mediated induction of TAK1 complex.
    REACT_225463. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
    REACT_226192. IKK complex recruitment mediated by RIP1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lymphocyte antigen 96
    Short name:
    Ly-96
    Alternative name(s):
    ESOP-1
    Protein MD-2
    Gene namesi
    Name:Ly96
    Synonyms:Esop1, Md2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1341909. Ly96.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB-SubCell
    2. lipopolysaccharide receptor complex Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    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 ↔ 511 Publication
    Glycosylationi26 – 261N-linked (GlcNAc...)1 Publication
    Disulfide bondi37 ↔ 1481 Publication
    Disulfide bondi95 ↔ 1051 Publication
    Glycosylationi114 – 1141N-linked (GlcNAc...)1 Publication
    Glycosylationi150 – 1501N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    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.

    Gene expression databases

    ArrayExpressiQ9JHF9.
    BgeeiQ9JHF9.
    CleanExiMM_LY96.
    GenevestigatoriQ9JHF9.

    Interactioni

    Subunit structurei

    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.By similarity

    Binary interactionsi

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

    Protein-protein interaction databases

    DIPiDIP-38572N.
    IntActiQ9JHF9. 1 interaction.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Z64X-ray2.84C21-155[»]
    3VQ1X-ray2.70C/D17-160[»]
    3VQ2X-ray2.48C/D17-160[»]
    ProteinModelPortaliQ9JHF9.
    SMRiQ9JHF9. Positions 21-155.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9JHF9.

    Family & Domainsi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG46291.
    GeneTreeiENSGT00390000000742.
    HOGENOMiHOG000001152.
    HOVERGENiHBG032514.
    InParanoidiQ9JHF9.
    KOiK05400.
    OMAiIPRRDIK.
    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

    MLPFILFSTL LSPILTESEK QQWFCNSSDA IISYSYCDHL KFPISISSEP    50
    CIRLRGTNGF VHVEFIPRGN LKYLYFNLFI SVNSIELPKR KEVLCHGHDD 100
    DYSFCRALKG ETVNTSIPFS FEGILFPKGH YRCVAEAIAG DTEEKLFCLN 150
    FTIIHRRDVN 160
    Length:160
    Mass (Da):18,394
    Last modified:October 1, 2000 - v1
    Checksum:iE224D17E5D5429E2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_006495518.1. XM_006495455.1.
    XP_006495519.1. XM_006495456.1.
    UniGeneiMm.116844.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF168120 mRNA. Translation: AAF89634.1 .
    AB018550 mRNA. Translation: BAA93619.1 .
    AK019283 mRNA. Translation: BAB31645.1 .
    CCDSi CCDS14832.1.
    RefSeqi NP_001153183.1. NM_001159711.1.
    NP_058619.1. NM_016923.2.
    XP_006495518.1. XM_006495455.1.
    XP_006495519.1. XM_006495456.1.
    UniGenei Mm.116844.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Z64 X-ray 2.84 C 21-155 [» ]
    3VQ1 X-ray 2.70 C/D 17-160 [» ]
    3VQ2 X-ray 2.48 C/D 17-160 [» ]
    ProteinModelPortali Q9JHF9.
    SMRi Q9JHF9. Positions 21-155.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-38572N.
    IntActi Q9JHF9. 1 interaction.

    Chemistry

    ChEMBLi CHEMBL3038514.

    PTM databases

    PhosphoSitei Q9JHF9.

    Proteomic databases

    PRIDEi Q9JHF9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000026881 ; ENSMUSP00000026881 ; ENSMUSG00000025779 .
    GeneIDi 17087.
    KEGGi mmu:17087.
    UCSCi uc007ajz.2. mouse.

    Organism-specific databases

    CTDi 23643.
    MGIi MGI:1341909. Ly96.

    Phylogenomic databases

    eggNOGi NOG46291.
    GeneTreei ENSGT00390000000742.
    HOGENOMi HOG000001152.
    HOVERGENi HBG032514.
    InParanoidi Q9JHF9.
    KOi K05400.
    OMAi IPRRDIK.
    OrthoDBi EOG7QG45N.
    PhylomeDBi Q9JHF9.
    TreeFami TF335876.

    Enzyme and pathway databases

    Reactomei REACT_196636. TRIF-mediated programmed cell death.
    REACT_198539. TRAF6 mediated induction of TAK1 complex.
    REACT_225463. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
    REACT_226192. IKK complex recruitment mediated by RIP1.

    Miscellaneous databases

    ChiTaRSi LY96. mouse.
    EvolutionaryTracei Q9JHF9.
    NextBioi 291228.
    PROi Q9JHF9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9JHF9.
    Bgeei Q9JHF9.
    CleanExi MM_LY96.
    Genevestigatori Q9JHF9.

    Family and domain databases

    Gene3Di 2.60.40.770. 1 hit.
    InterProi IPR014756. Ig_E-set.
    IPR003172. ML_dom.
    [Graphical view ]
    Pfami PF02221. E1_DerP2_DerF2. 1 hit.
    [Graphical view ]
    SMARTi SM00737. ML. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81296. SSF81296. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    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: October 1, 2014
    This is version 105 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

    External Data

    Dasty 3