VSIR (V-Set Immunoregulatory Receptor) is a Protein Coding gene. Diseases associated with VSIR include Ichthyosis, Congenital, Autosomal Recessive 6 and Monckeberg Arteriosclerosis. Among its related pathways are Cell adhesion molecules (CAMs) and NF-kappaB Signaling. An important paralog of this gene is VSIG8.
This gene encodes the nuclear hormone receptor for vitamin D3. This receptor also functions as a receptor for the secondary bile acid lithocholic acid. The receptor belongs to the family of trans-acting transcriptional regulatory factors and shows sequence similarity to the steroid and thyroid hormone receptors. Downstream targets of this nuclear hormone receptor are principally involved in mineral metabolism though the receptor regulates a variety of other metabolic pathways, such as those involved in the immune response and cancer. Mutations in this gene are associated with type II vitamin D-resistant rickets. A single nucleotide polymorphism in the initiation codon results in an alternate translation start site three codons downstream. Alternative splicing results in multiple transcript variants encoding different proteins.
Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.
Vitronectin, also known as VTN, is a member of the pexin family. It is an abundant glycoprotein found in serum the extracellular matrix and promotes cell adhesion and spreading. Vitronectin is a secreted protein and exists in either a single chain form or a cleaved, two chain form held together by a disulfide bond. Vitronectin is a plasma glycoprotein implicated as a regulator of diverse physiological process, including blood coagulation, fibrinolysis, pericellular proteolysis, complement dependent immune responses, and cell attachment and spreading. Because of its ability to bind platelet glycoproteins and mediate platelet adhesion and aggregation at sites of vascular injury, vitronectin has become an important mediator in the pathogenesis of coronary atherosclerosis. As a multifunctional protein with a multiple binding domain, Vitronectin interacts with a variety of plasma and cell proteins. Vitronectin binds multiple ligands, including the soluble vitronectin receptor. It may be an independent predictor of adverse cardiovascular outcomes following acute stenting. Accordingly, Vitronectin is suggested to be involved in hemostasis, cell migration, as well as tumor malignancy.
VWF (Von Willebrand factor) is a multimeric plasma glycoprotein that promotes adhesion of platelets to sites of vascular injury. Mature circulating VWF is made up of disulfide-bonded multimers that are in a complex with factor VIII. VWF is stored in secretory Weibel-Palade bodies in endothelial cells. It is synthesized as a large precursor protein and undergoes extensive posttranslational modifications including dimerization in the endoplasmic reticulum followed by cleavage of the pro-peptide and multimerization in the Golgi apparatus. VWF is important in hemostasis, and genetic defects in the structure and modification of VWF can cause von Willebrand disease (VWD), the most common congenital bleeding disorder in humans. Alternatively, increased levels of VWF have been shown to be involved in acute coronary thrombosis and are a clinical risk marker for atherosclerosis.
VPAC1 is the receptor for vasoactive intestinal peptides. This small neuropeptide is involved in regulating smooth muscle relaxation, the water and ion flux of the lung and intestinal epithelium, promoting neuron growth and survival, and regulating immune function. The activity of VPAC1 is regulated by G protein. VPAC1 interacts with citrulline nucleotide binding protein-related membrane receptors to activate adenate cyclase.
Human VIPR2 (Vasoactive Intestinal Polypeptide Receptor 2), also known as VPAC2, is a 60-70 kDa seven transmembrane glycoprotein receptor, which belongs to the G protein-coupled receptor 2 family of proteins. In its first extracellular region hormone receptor domain (aa 49-114) contains a mature chain, which has three N-linked glycosylation sites and a "Cilia targeting signal", which is composed of and Arg -Composition of Asp-Tyr-Arg sequence. Human VIPR2 has relatively high homology with mouse and rat VIPR2. VIPR2 is mainly expressed in skeletal muscle, CD4+ T cells, smooth muscle cells, dendritic cells, liver precursor cells, single cells, synthetic cells and selective neurons. VIPR2 couples with CAMP-mediated signal transduction pathways, and binds VIP and pituitary adenase activating polypeptide (PACAP).
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