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 4 (VSIG4) is a type I transmembrane glycoprotein that is a B7 family-related protein and an Ig superfamily member. Mouse VSIG4 is synthesized as a 280 amino acid (aa) precursor that contains a signal sequence, an IgV-type immunological domain (aa 36-115),one potential N-linked glycosylation site, and a single transmembrane domain. The IgV domain of mouse VSIG4 shares 86% and 80% aa sequence identity with the IgV domains of rat and human VSIG4, respectively. VSIG4 functions as a negative regulator of mouse as well as human T cell activation, and may be involved in the maintenance of peripheral T cell tolerance and/or unresponsiveness. VSIG4 acts as a macrophage complement receptor by binding complement fragments C3b and iC3b. VSIG4 binding to C3b inhibits complement activation through the alternative pathway, making it a potent suppressor of established inflammation.
V-set and immunoglobulin domain-containing protein 8(VSIG8) is a single-pass type I membrane protein.The mouse VSIG8 cDNA encodes 417 amino acids (aa) including a 21 aa signal sequence, a 241 aa extracellular domain (ECD) containing 2 Ig-like V-type (immunoglobulin-like) domains, a 21 aa transmembrane domain and a 134 aa cytoplasmic domain. The function of VSIG8 is not clear.
Von Willebrand Factor (VWF) is a multimeric glycoprotein involved in hemostasis in blood, binds receptors on the surface of platelets and in connective tissue, thereby mediating the adhesion of platelets to sites of vascular injury. From studies it appears that VWF protein uncoils under these circumstances, decelerating passing platelets. VWF protein is deficient or defective in von Willebrand disease (VWD) and is involved in a large number of other diseases, including thrombosis, thrombotic thrombocytopenic purpura, Stroke, Heyde's syndrome, possibly hemolytic-uremic syndrome and so on.
WIF1, also known as WIF-1 and wnt inhibitory factor 1, is a secreted protein which binds WNT proteins and inhibits their activities. It contains a WNT inhibitory factor (WIF) domain and 5 epidermal growth factor (EGF)-like domains. WNT proteins are extracellular signaling molecules involved in the control of embryonic development. WIF1 may be involved in mesoderm segmentation and can be detected in fish, amphibia and mammals. WIF-1 is a recurrent target in human salivary gland oncogenesis. Downregulation of WIF1 takes part in the development and progression of pleomorphic adenomas. WIF1 also is a tumor suppressor, and has been found to be epigenetically silenced in various cancers, specifically in nonfunctioning pituitary tumors. WIF1 are expected to have molecular function (protein tyrosine kinase activity) and to localize in various compartments (extracellular space, extracellular region).
This antimicrobial gene encodes a member of the chemokine superfamily. Chemokines function in inflammatory and immunological responses, inducing leukocyte migration and activation. The encoded protein is a member of the C-chemokine subfamily, retaining only two of four cysteines conserved in other chemokines, and is thoμght to be specifically chemotactic for T cells. This gene and a closely related family member are located on the long arm of chromosome 1.
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