V-set and immunoglobulin domain-containing protein 4(VSIG4) is a transmembrane protein contains a signal peptide, a V-type Ig-like domain, a C2-type Ig-like domain, several potential O-glycosylation sites, and an intracellular domain with 2 potential phosphorylation sites and is structurally related to the B7 family of immune regulatory proteins. This protein is also a receptor for the complement component 3 fragments C3b and iC3b.The main function is strong negative regulator of T-cell proliferation and IL2 production and it is also potent inhibitor of the alternative complement pathway convertases. It abundantly expressed in several fetal tissues such as adult tissues, highest expression in lung and placenta and it also expressed in resting macrophages.
VSIG4 (V-set and immunoglobulin domain containing 4); also known as complement receptor of the immunoglobulin superfamily (CRIg) and Z39Ig; is a type I transmembrane glycoprotein. It is a B7 family-related protein and an Ig superfamily member. In contrast to the B7 family members which contain two IgG domains; VSIG4 contains one complete V-type Ig domain and a truncated C-type Ig domain. VSIG4 is exclusively expressed on tissue resident macrophages and binds to multimers of C3b and iC3b that are covalently attached to particle surfaces. No VSIG4 expression appears to be present in T and B cells. VSIG4 functions as a negative regulator of T cell activation; and may be involved in the maintenance of peripheral T cell tolerance; and is also identified as a potent suppressor of established inflammation. Mouse VSIG4 is synthesized as a 280 amino acid precursor that contains a signal sequence; an V-type Ig domain (aa 36-115); one potential N-linked glycosylation site; and a single transmembrane domain. The V-type Ig domain of mouse VSIG4 shares 86% and 80% aa sequence identity with the V-type Ig domains of rat and human VSIG4; respectively.
V-Set and Immunoglobulin Domain-Containing Protein 4 (VSIG4) is a 45-50 kDa macrophage-specific transmembrane glycoprotein that belongs to the B7 family-related protein and an Ig superfamily member. In contrast to the B7 family members which contain two IgG domains; VSIG4 contains one complete V-type Ig domain and a truncated C-type I g domain. VSIG4 is abundantly expressed in several fetal tissues. In adult tissues; the highest expression of VSIG4 is in lung and placenta. It is also expressed in resting macrophages. No VSIG4 expression appears to be present in T and B cells. The specific expression of VSIG4 on resting macrophages in tissue suggests that this inhibitory ligand may be important for the maintenance of T cell unresponsiveness in healthy tissues. VSIG4 functions as a negative regulator of T cell activation; and may be involved in the maintenance of peripheral T cell tolerance; and is also identified as a potent suppressor of established inflammation. VSIG4 is a phagocytic receptor; strong negative regulator of T-cell proliferation and IL2 production. It is a potent inhibitor of the alternative complement pathway convertases. Human VSIG4 is 399 amino acids (aa) in length. It is a type I transmembrane (TM) glycoprotein that contains a 264 aa extracellular domain (ECD) (aa 20 - 283) and a 95 aa cytoplasmic region.
V-set and immunoglobulin domain-containing protein 8(VSIG8) is a single-pass type I membrane protein.The human VSIG8 cDNA encodes 414 amino acids (aa) including a 21 aa signal sequence; a 242 aa extracellular domain (ECD) containing 2 Ig-like V-type (immunoglobulin-like) domains; a 21 aa transmembrane domain and a 130 aa cytoplasmic domain.The funtion of VSIG8 is not clear.
Visinin-Like Protein 1 (VILIP) is a a member of the Visinin/Recoverin subfamily of neuronal calcium sensor proteins. VILIP is strongly expressed in the Granule Cells of the Cerebellum where it associates with membranes in a Calcium-dependent manner and modulates intracellular signaling pathways of the central nervous system by directly or indirectly regulating the activity of Adenylyl Cyclase. It has been shown that VILIP regulates the inhibition of rhodopsin phosphorylation in a Calcium-dependent manner in vitro.
V-set and transmembrane domain-containing protein 1 is a single-pass membrane protein. VSTM1 Contains 1 Ig-like V-type domain, in humans is encoded by the VSTM1 gene. It expressed on myeloid (neutrophils, eosinophils and monocytes) but not on lymphoid cells. It behaves as a cytokine, promoting IL17A secretion by CD4+ T-cells, and differentiation and activation of IL17 producing helper T-cells (TH17). Inhibitory immune receptor involved in the regulation of phagocytes.
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