UniProt functional annotation for Q9Y6Y9



	UniProt functional annotation for Q9Y6Y9

UniProt code: Q9Y6Y9.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Binds bacterial lipopolysaccharide (LPS) (PubMed:17803912, PubMed:17569869). 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 (PubMed:11160242, PubMed:11593030). Enhances TLR4-dependent activation of NF-kappa-B (PubMed:10359581). Cells expressing both LY96 and TLR4, but not TLR4 alone, respond to LPS (PubMed:10359581). {ECO:0000269|PubMed:10359581, ECO:0000269|PubMed:11160242, ECO:0000269|PubMed:11593030, ECO:0000269|PubMed:17569869, ECO:0000269|PubMed:17803912}.

Subunit: Heterogeneous homomer formed from homodimers; disulfide-linked (PubMed:11593030, PubMed:12642668). Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, LY96 and TLR4 (PubMed:11274165). Binds to the extracellular domains of TLR2 and TLR4 (PubMed:10359581, PubMed:11593030, PubMed:17803912). Ligand binding induces interaction with TLR4 and oligomerization of the complex. {ECO:0000269|PubMed:10359581, ECO:0000269|PubMed:11274165, ECO:0000269|PubMed:11593030, ECO:0000269|PubMed:17569869, ECO:0000269|PubMed:17803912}.

Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:10359581, ECO:0000269|PubMed:11593030, ECO:0000305|PubMed:11274165}. Secreted {ECO:0000269|PubMed:11593030}. Note=Retained in the extracellular space at the cell surface by interaction with TLR4 (PubMed:10359581). {ECO:0000269|PubMed:10359581, ECO:0000269|PubMed:11593030}.

Ptm: N-glycosylated; high-mannose. {ECO:0000269|PubMed:11593030, ECO:0000269|PubMed:17569869}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Binds bacterial lipopolysaccharide (LPS) (PubMed:17803912, PubMed:17569869). 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 (PubMed:11160242, PubMed:11593030). Enhances TLR4-dependent activation of NF-kappa-B (PubMed:10359581). Cells expressing both LY96 and TLR4, but not TLR4 alone, respond to LPS (PubMed:10359581). {ECO:0000269\|PubMed:10359581, ECO:0000269\|PubMed:11160242, ECO:0000269\|PubMed:11593030, ECO:0000269\|PubMed:17569869, ECO:0000269\|PubMed:17803912}.


Subunit:		Heterogeneous homomer formed from homodimers; disulfide-linked (PubMed:11593030, PubMed:12642668). Belongs to the lipopolysaccharide (LPS) receptor, a multi-protein complex containing at least CD14, LY96 and TLR4 (PubMed:11274165). Binds to the extracellular domains of TLR2 and TLR4 (PubMed:10359581, PubMed:11593030, PubMed:17803912). Ligand binding induces interaction with TLR4 and oligomerization of the complex. {ECO:0000269\|PubMed:10359581, ECO:0000269\|PubMed:11274165, ECO:0000269\|PubMed:11593030, ECO:0000269\|PubMed:17569869, ECO:0000269\|PubMed:17803912}.
Subcellular location:		Secreted, extracellular space {ECO:0000269\|PubMed:10359581, ECO:0000269\|PubMed:11593030, ECO:0000305\|PubMed:11274165}. Secreted {ECO:0000269\|PubMed:11593030}. Note=Retained in the extracellular space at the cell surface by interaction with TLR4 (PubMed:10359581). {ECO:0000269\|PubMed:10359581, ECO:0000269\|PubMed:11593030}.
Ptm:		N-glycosylated; high-mannose. {ECO:0000269\|PubMed:11593030, ECO:0000269\|PubMed:17569869}.