ID   LY96_BOVIN              Reviewed;         160 AA.
AC   P58754;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Lymphocyte antigen 96;
DE            Short=Ly-96;
DE   AltName: Full=Protein MD-2 {ECO:0000303|PubMed:17559944};
DE   Flags: Precursor;
GN   Name=LY96; Synonyms=MD2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lymph node;
RA   Guionaud C.T., Dubey C., Zumkehr J.R., Sonstegard T.S., Jungi T.W.;
RT   "Role of bovine TLR2, TLR4 and CD14 in the recognition of bacterial
RT   constituents.";
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=17559944; DOI=10.1016/j.vetimm.2007.04.017;
RA   Sauter K.S., Brcic M., Franchini M., Jungi T.W.;
RT   "Stable transduction of bovine TLR4 and bovine MD-2 into LPS-nonresponsive
RT   cells and soluble CD14 promote the ability to respond to LPS.";
RL   Vet. Immunol. Immunopathol. 118:92-104(2007).
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 (By similarity). Enhances TLR4-
CC       dependent activation of NF-kappa-B. Cells expressing both LY96 and
CC       TLR4, but not TLR4 alone, respond to LPS.
CC       {ECO:0000250|UniProtKB:Q9Y6Y9, ECO:0000269|PubMed:17559944}.
CC   -!- SUBUNIT: Heterogeneous homomer formed from homodimers; disulfide-linked
CC       (By similarity). Belongs to the lipopolysaccharide (LPS) receptor, a
CC       multi-protein complex containing at least CD14, LY96 and TLR4
CC       (PubMed:17559944). Binds to the extracellular domains of TLR2 and TLR4.
CC       Ligand binding induces interaction with TLR4 and oligomerization of the
CC       complex (By similarity). {ECO:0000250|UniProtKB:Q9Y6Y9,
CC       ECO:0000269|PubMed:17559944}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:17559944}. Secreted {ECO:0000250|UniProtKB:Q9Y6Y9}.
CC       Note=Retained in the extracellular space at the cell surface by
CC       interaction with TLR4. {ECO:0000305|PubMed:17559944}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9Y6Y9}.
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DR   EMBL; AF368418; AAL16721.1; -; mRNA.
DR   AlphaFoldDB; P58754; -.
DR   SMR; P58754; -.
DR   InParanoid; P58754; -.
DR   Proteomes; UP000009136; Unplaced.
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   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Immunity; Inflammatory response;
KW   Innate immunity; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..160
FT                   /note="Lymphocyte antigen 96"
FT                   /id="PRO_0000018617"
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        114
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"
SQ   SEQUENCE   160 AA;  18484 MW;  D97760E5FE93B352 CRC64;
     MFPFMLFSTL FSSIFTEPRE KMWICNSSDA SLWYNYCDDM KFPISVKVEP CVTIKGTKGK
     LHLYYIARRD IQKLYLNLHI SIKSMTLPMR KEVICREYGG DYSFCGALKG ETVNTTIPFS
     FQGIRFSPGQ YHCVVEAISG NSEEMLFCLN FTIIHYSSLN