| Function | Part of the innate immune responses against microbial infection. Specifically recognizes a set of N-terminally truncated immunoglobulins that are produced via cleavage by proteases from a range of pathogenic bacteria and fungi, including L.pneumophila, M.hyorhinis, S.pneumoniae, S.aureus and C.albicans. Recognizes epitopes that are in part in the variable region of the immunoglobulin light chains, but requires also the constant region for signaling. Binds to a subset of cleaved IgM, IgG3 and IgG4 molecules, but does not bind cleaved IgA1. Binding of N-terminally truncated immunoglobulins mediates activation of neutrophils. In monocytes, activation leads to the release of CSF2, CF3, IL6, CXCL8 and CCL3 and down-regulates responses to bacterial lipopolysaccharide (LPS), possibly via down-regulation of TLR4 expression and reduced signaling via TLR4. In eosinophils, activation by ligand binding leads to the release of RNASE2, IL4 and leukotriene C4. Does not bind class I MHC antigens. |
| Protein Name | Leukocyte Immunoglobulin-Like Receptor Subfamily A Member 2Cd85 Antigen-Like Family Member HImmunoglobulin-Like Transcript 1Ilt-1Leukocyte Immunoglobulin-Like Receptor 7Lir-7Cd Antigen Cd85h |
| Database Links | Reactome: R-HSA-198933 |
| Cellular Localisation | Cell MembraneSingle-Pass Type I Membrane ProteinIsoform 4: Secreted |
| Alternative Protein Names | Leukocyte Immunoglobulin-Like Receptor Subfamily A Member 2 proteinCd85 Antigen-Like Family Member H proteinImmunoglobulin-Like Transcript 1 proteinIlt-1 proteinLeukocyte Immunoglobulin-Like Receptor 7 proteinLir-7 proteinCd Antigen Cd85h proteinLILRA2 proteinILT1 proteinLIR7 protein |
Information sourced from Uniprot.org
