Programmed Cell Death 1 Ligand 2 (PDCD1LG2) is a member of the BTN/MOG family. PDCD1LG2 contains one Ig-like C2-type domain and one Ig-like V-type domain. PDCD1LG2 is highly expressed in the heart, placenta, pancreas, lung and liver; it is weakly expressed in the spleen, lymph nodes, and thymus. PDCD1LG2 is involved in the costimulatory signal, essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. PDCD1LG2 interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production.
PVRIG (poliovirus receptor related immunoglobulin domain-containing protein), also known as CD112 receptor (CD112R), is an approximately 34 kDa single transmembrane protein in the poliovirus receptor-like protein (PVR) family. The extracellular domain sequence of human and mouse PVRIG have approximately 65% similarity. PVRIG functions as a cell surface receptor for Nectin-2/CD112, a cell surface protein that is widely expressed on antigen-presenting cells and tumor cells. Disrupting the PVRIG/Nectin-2 interaction enhances human T cell response, suggesting PVRIG is a novel checkpoint for human T cells. PVRIG may act as a coinhibitory receptor that suppresses T-cell receptor-mediated signals.
Human Siglec-15 is a transmembrane glycoprotein in the Siglec family. Siglecs are type I transmembrane proteins where the NH3+-terminus is in the extracellular space and the COO--terminus is cytosolic. Each Siglec contains an N-terminal V-type immunoglobulin domain (Ig domain) which acts as the binding receptor for sialic acid. These lectins are placed into the group of I-type lectins because the lectin domain is an immunoglobulin fold. All Siglecs are extended from the cell surface by C2-type Ig domains which have no binding activity. Siglecs differ in the number of these C2-type domains. Human Siglec-15 consists of a 244 amino acid (aa) extracellular domain (ECD) with two Ig-like domains, a 21 aa transmembrane segment, and a 44 aa cytoplasmic domain. Siglec-15 function is important for osteoclast formation and TRANCE/RANK Ligand signaling in osteoclasts.
Siglec-15 is a transmembrane glycoprotein in the Siglec family. Siglecs are type I transmembrane proteins where the NH3+-terminus is in the extracellular space and the COO--terminus is cytosolic. Each Siglec contains an N-terminal V-type immunoglobulin domain (Ig domain) which acts as the binding receptor for sialic acid. These lectins are placed into the group of I-type lectins because the lectin domain is an immunoglobulin fold. All Siglecs are extended from the cell surface by C2-type Ig domains which have no binding activity. Siglecs differ in the number of these C2-type domains. Siglec-15 function is important for osteoclast formation and TRANCE/RANK Ligand signaling in osteoclasts.
Sialic acid-binding Ig-like lectin 5 is a protein that in Cynomolgus is encoded by the SIGLEC5 gene, Cynomolgus SIGLEC5 cDNA encodes 551 amino acids (aa) that include a 16 aa signal sequence, a 439aa extracellular domain (ECD) with three Ig-like domains, a transmembrane region and a cytoplasma tail. No Siglec has been shown to recognized any cell surface ligand other than sialic acids, suggesting that interactions with glycans containing this carbohydrate are important in mediating the biological functions of Siglecs. Siglec5 to 11 share a high degree of sequence similarity with CD33/Siglec3 both in their extracellular and intracellular regions. 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.
Signal Regulatory Protein α (SIRPα) is a monomeric approximately 90 kD type I transmembrane glycoprotein. The 504 amino acid human SIRPα contains two Ig-like C1-type domains and one Ig-like V-type domain. SIRPα can express in various tissues, mainly on brain and myeloid cells, including macrophages, neutrophils, dendritic and Langerhans cells. It also can detect in neurons, smooth muscle and endothelial cells. SIRPA is an immunoglobulin-like cell surface receptor for CD47. SIRPα acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPα shows adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. SIRPα engagement generally produces a negative regulatory signal; it may mediate negative regulation of phagocytosis, mast cell activation and dendritic cell activation
Thymic stromal lymphopoietin (TSLP) is a protein belonging to the cytokine family, contains 140 amino acids. It is known to play an important role in the maturation of T cell populations through activation of antigen presenting cells. TSLP induces the release of T-cell-attracting chemokines from monocytes and, in particular, enhances the maturation of CD11c+ dendritic cells. It can induce allergic inflammation by directly activating mast cells. TSLP is produced mainly by non-hematopoietic cells such as fibroblasts, epithelial cells and different types of stromal or stromal-like cells. These cells are located in regions where TSLP activity is required.
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