ID   LY96_CRIGR              Reviewed;         160 AA.
AC   P58755;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Lymphocyte antigen 96;
DE            Short=Ly-96;
DE   AltName: Full=Protein MD-2;
DE   Flags: Precursor;
GN   Name=LY96; Synonyms=MD2;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND VARIANT TYR-95.
RC   TISSUE=Ovarian carcinoma;
RX   PubMed=11435474; DOI=10.1084/jem.194.1.79;
RA   Schromm A.B., Lien E., Henneke P., Chow J.C., Yoshimura A., Heine H.,
RA   Latz E., Monks B.G., Schwartz D.A., Miyake K., Golenbock D.T.;
RT   "Molecular genetic analysis of an endotoxin nonresponder mutant cell line.
RT   A point mutation in a conserved region of MD-2 abolishes endotoxin-induced
RT   signaling.";
RL   J. Exp. Med. 194:79-88(2001).
CC   -!- FUNCTION: Binds bacterial lipopolysaccharide (LPS). Cooperates with
CC       TLR4 in the innate immune response to bacterial lipopolysaccharide
CC       (LPS), and with TLR2 in the response to cell wall components from Gram-
CC       positive and Gram-negative bacteria. Enhances TLR4-dependent activation
CC       of NF-kappa-B. Cells expressing both LY96 and TLR4, but not TLR4 alone,
CC       respond to LPS. {ECO:0000250|UniProtKB:Q9Y6Y9,
CC       ECO:0000269|PubMed:11435474}.
CC   -!- SUBUNIT: Heterogeneous homomer formed from homodimers; disulfide-
CC       linked. Belongs to the lipopolysaccharide (LPS) receptor, a multi-
CC       protein complex containing at least CD14, LY96 and TLR4. Binds to the
CC       extracellular domains of TLR2 and TLR4. Ligand binding induces
CC       interaction with TLR4 and oligomerization of the complex.
CC       {ECO:0000250|UniProtKB:Q9Y6Y9}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000250|UniProtKB:Q9Y6Y9}. Secreted
CC       {ECO:0000250|UniProtKB:Q9Y6Y9}. Note=Retained in the extracellular
CC       space at the cell surface by interaction with TLR4.
CC       {ECO:0000250|UniProtKB:Q9Y6Y9}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9Y6Y9}.
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DR   EMBL; AF325501; AAK57984.1; -; mRNA.
DR   RefSeq; NP_001233702.1; NM_001246773.1.
DR   AlphaFoldDB; P58755; -.
DR   SMR; P58755; -.
DR   STRING; 10029.NP_001233702.1; -.
DR   GeneID; 100689342; -.
DR   KEGG; cge:100689342; -.
DR   CTD; 23643; -.
DR   eggNOG; ENOG502SD7W; Eukaryota.
DR   OMA; YTYCDNM; -.
DR   OrthoDB; 1320082at2759; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0046696; C:lipopolysaccharide receptor complex; ISS:UniProtKB.
DR   GO; GO:0001530; F:lipopolysaccharide binding; IEA:InterPro.
DR   GO; GO:0001875; F:lipopolysaccharide immune receptor activity; ISS:UniProtKB.
DR   GO; GO:0035662; F:Toll-like receptor 4 binding; IEA:InterPro.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR   GO; GO:0032497; P:detection of lipopolysaccharide; ISS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:UniProtKB.
DR   GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR039217; LY96.
DR   InterPro; IPR003172; ML_dom.
DR   PANTHER; PTHR15218; PTHR15218; 1.
DR   Pfam; PF02221; E1_DerP2_DerF2; 1.
DR   SMART; SM00737; ML; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Immunity; Inflammatory response;
KW   Innate immunity; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..160
FT                   /note="Lymphocyte antigen 96"
FT                   /id="PRO_0000018618"
FT   REGION          119..123
FT                   /note="Interaction with lipopolysaccharide"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6Y9"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        25..51
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6Y9"
FT   DISULFID        37..148
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6Y9"
FT   DISULFID        95..105
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6Y9"
FT   VARIANT         95
FT                   /note="C -> Y (in endotoxin nonresponder)"
FT                   /evidence="ECO:0000269|PubMed:11435474"
SQ   SEQUENCE   160 AA;  18357 MW;  0E533B1AA5B46DD6 CRC64;
     MLPFILFSTL LPLIFTESEQ QLWFCNSSDA TFSYSYCDSM KFPFSITAEP CITLKGTNGF
     LHIKFIPRRD LKKLYFNLSI NVNSIEVPTR KEIICHGYDD NYSFCKALKG ETVNTVVPFS
     FKGILFPKGQ YRCVAEAIVG DNEEKLFCLN FTIIHHPNVN