Other Proteins

Coronavirus N protein is required for coronavirus RNA synthesis, and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is a most abundant protein of coronavirus. N protein packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. Because of the conservation of N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.

Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.

Natural cytotoxicity triggering receptor 2 (NCR2), also known as Natural killer cell p44-related protein (NKp44), or CD336, is a member of the natural cytotoxicity receptor (NCR) family, which composed of one Ig-like extracellular domain, a transmembrane segment, and a cytoplasmic domain. It is a novel transmembrane glycoprotein belonging to the Immunoglobulin superfamily characterized by a single extracellular V-type domain. The cytoplasmic domain of NKp44 also contains a sequence that matches the immunoreceptor tyrosine-based inhibitory motif (ITIM) consensus. This Cytotoxicity-activating receptor that may contribute to the increased efficiency of activated natural killer (NK) cells to mediate tumor cell lysis. NKp44 is selectively expressed by IL-2-activated NK cells and may contribute to the increased efficiency of activated NK cells to mediate tumor cell lysis. Tumor cell recognition of the mutated NKp44 proteins was significantly reduced and correlated with their lower recognitio

MHC class I polypeptide-related sequence B; also known as MICB; is a heavily glycosylated protein serving as a ligand for the type I I receptor NKG2D. MICB shares 85% amino acid identity with MICA; a closely related protein; both of which contain three extracellular immunoglobulin-like domains; but without capacity to bind peptide or interact with beta-2-microglobulin. acting as a stress-induced self-antigen; binding of MICB to the NKG2D receptor activates the cytolytic response of natural killer (NK) cells; CD8+αβ T cells; and γδ T cells on which the receptor is expressed. MICA/B are minimally expressed on normal cells; but are frequently expressed on epithelial tumors and can be induced by bacterial and viral infections. MICA/B recognition thus is involved in tumor surveillance; viral infections; and autoimmune diseases.

Hepatitis A virus cellular receptor 2 (HAVCR2); formerly known as T cell immunoglobulin and mucin domain-3 (TIM-3); is a transmembrane glycoprotein expressed on the surface of terminally differentiated Th1 cells but not on Th2 cells. It was the first surface molecule that specifically identifies Th1 cells in both mice and human. Recently; identification of Galectin-9 as a ligand for TIM-3 has established the TIM-3-Galectin-9 pathway as an important regulator of Th1 immunity and tolerance induction. Engagement of Tim-3 by its ligand galectin-9 negatively regulates IFN-gamma secretion and influences the ability to induce T cell tolerance in both mice and man. It suggests a novel paradigm in which dysregulation of the TIM-3-galectin-9 pathway could underlie chronic autoimmune disease states; such as multiple sclerosis. Recent work has explored the role of TIM-3 in systemic lupus erythematosus (SLE); and their results indicate that TIM-3 may represent a novel target for the treatment of SL

Cerebral Dopamine Neurotrophic Factor (CDNF), also known as ARMETL1 (ARMET-like protein 1), is a secreted protein with eight conserved cysteine residues, predicting a unique protein fold and defining a new, evolutionarily conserved protein family. CDNF is a novel neurotrophic factor with strong trophic activity on dopaminergic neurons comparable to that of glial cell line-derived neurotrophic factor (GDNF). CDNF/ARMETL1 is a evolutionary conserved protein which can protect and restore the function of dopaminergic neurons in the rat model of Parkinson's disease, suggesting that CDNF might be beneficial for the treatment of Parkinson's disease. CDNF is widely expressed in neurons in several brain regions including cerebral cortex, hippocampus, substantia nigra, striatum and cerebellum. Human CDNF is glycosylated and secreted from transiently transfected cells. CDNF promotes the survival, growth, and function of dopamine-specific neurons and is expressed in brain regions that undergo coca

Interleukin-8 (IL-8) belongs to the neutrophil-specific CXC family of chemokines. It is one of the initial cytokines released from a variety of cell types; including T cells; endothelial cells and fibroblasts; in response to an inflammatory stimulus and acts by recruiting neutrophils; T-cells and basophils to the site of inflammation. Elevated Interleukin-8 levels are associated with the onset of a variety of disease states.

Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. They are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. Serpin E1 is a secreted protein which belongs to the Serpin family. Serpin E1 acts as 'bait' for tissue plasminogen activator, urokinase, and protein C. Its rapid interaction with TPA may function as a major control point in the regulation of fibrinolysis. Defects in SERPINE1 are characterized by abnormal bleeding due to Serpin E1 defect in the plasma. High concentrations of Serpin E1 have been associated with thrombophilia which is an autosomal dominant disorder in which affected individuals are prone to develop serious spontaneous thrombosis.

Inter-Cellular Adhesion Molecule 1 (ICAM1) is a type of intercellular adhesion molecule continuously present in low concentrations in the membranes of leukocytes and endothelial cells. As an endothelial and leukocyte-associated transmembrane protein, ICAM1 is well known for its importance in stabilizing cell-cell interactions and facilitating leukocyte endothelial transmigration. The presence of heavy glycosylation and other structural characteristics lend ICAM1 binding sites for a number of immune-associated ligands. Notably, ICAM-1 binds to macrophage adhesion ligand-1 (Mac-1; ITGB2 / ITGAM), leukocyte function associated antigen-1 (LFA-1/integrin), and fibrinogen.ICAM-1 expressed by respiratory epithelial cells is also the binding site for rhinovirus, the causative agent of most common colds.