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Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
Gene References into Functions
PSGL1 and Siglec-5 are in close proximity at the leukocyte surface.SPSGL1 is a ligand for Siglec-5 and interacts with Siglec-5 ectodomain.Siglec-5 plays a role in PSGL1-mediated leukocyte rolling and the inflammatory response in general. PMID: 27892504
An unbiased screen revealed Hsp70 as a ligand for Siglec-5 and Siglec-14. Hsp70 stimulation through Siglec-5 delivers an anti-inflammatory signal, while stimulation through Siglec-14 is pro-inflammatory. PMID: 26459514
Data indicate that the Siglec-5/14 genotype influences neutrophil responses to group B Streptococcus. PMID: 24799499
we found that secretory IgA is taken up by M cells via the Dectin-1 receptor, with the possible involvement of Siglec-5 acting as a co-receptor. PMID: 24068891
These studies demonstrate the Siglec5 carbohydrate recognition domain alone is sufficient for binding sialylated carbohydrates and provide a foundation for further investigation of Siglec5 structure and function. PMID: 23321067
Siglec-5 expression protects T cells from HIV-1- and apoptosis-induced cell death and contributes to the different outcomes of HIV-1 infection in humans and chimpanzees. PMID: 22945238
Human Siglec-5 inhibitory receptor and immunoglobulin A (IgA) have separate binding sites in streptococcal beta protein. PMID: 21795693
Siglec-5 expression correlates with lack of proliferation in a subset of human cells, and is upregulated by activation of chimpanzee but not human lymphocytes. PMID: 20231688
expression of Siglec-5 on cells of the myelomonocytic lineage and alteration of its expression by inflammatory stimuli suggest a role for this protein in cell/cell interactions following microbial exposure. PMID: 12763136
Siglec-5 can be classified as an inhibitory receptor with the potential to mediate SHP-1 and/or SHP-2-dependent signaling in the absence of tyrosine phosphorylation. PMID: 15769739
Siglecs-5 did not interact with sulfate derivatives of LacNAc and sulfated oligosaccharides containing sialic acid. PMID: 16732727
The expression levels of Siglec-5 were high or detectable in bone marrow plasma from AML patients and serum from normal donors. PMID: 16828866
Siglec-14 and Siglec-5 appear to be the first glycan binding paired receptors. Near-complete sequence identity of the amino-terminal part of human Siglec-14 and Siglec-5 indicates partial gene conversion between SIGLEC14 and SIGLEC5. PMID: 17012248
Siglec-5 is identified as a receptor for alpha-1-acid glycoprotein (AGP) 1 in human neutrophils. PMID: 17675532
Structural implications of SIGLEC5-mediated sialoglycan recognition are reported. PMID: 18022638
Group B Streptococcus beta protein binding to Siglec-5 functions to impair leukocyte phagocytosis, oxidative burst, and extracellular trap production, promoting bacterial survival. PMID: 19596804
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Subcellular Location
Membrane; Single-pass type I membrane protein.
Protein Families
Immunoglobulin superfamily, SIGLEC (sialic acid binding Ig-like lectin) family
Tissue Specificity
Expressed by monocytic/myeloid lineage cells. Found at high levels in peripheral blood leukocytes, spleen, bone marrow and at lower levels in lymph node, lung, appendix, placenta, pancreas and thymus. Expressed by monocytes and neutrophils but absent from