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IFITM3 is a multi-pass membrane protein that belongs to the IFITM (interferon inducible transmembrane) family of proteins. IFITM proteins are induced by type I and type II interferons and contain multiple interferon (IFN)-stimulated response elements (ISREs) in their promoter regions. IFITM proteins play important roles in many cellular processes and their expression requires the presence of the chromatin remodeling SWI/SNF-like BAF complexes. Cellular processes involving IFITM proteins incl

The TEK receptor tyrosine kinase is expressed almost exclusively in endothelial cells in mice, rats, and humans. This receptor possesses a unique extracellular domain containing 2 immunoglobulin-like loops separated by 3 epidermal growth factor-like repeats that are connected to 3 fibronectin type III-like repeats. The ligand for the receptor is angiopoietin-1. Defects in TEK are associated with inherited venous malformations; the TEK signaling pathway appears to be critical for endothelial ce

Mucin is a high M.W. (1,000 kDa) glycoprotein, expressed by mucus cells of the gastric epithelium and by goblet cells of the fetal, precancerous and cancerous colon, but not by those of the normal colon. It also appears in other epithelial tissues, which are embryologically derived from the foregut (epigastric and bronchial epithelium) and in Müller ducts (mucus cells of the endocervix and urethral epithelium near the prostatic utriculus). The expression of MUC5AC has been fre

GPCR2037 is a G protein-coupled receptor that undergoes weak activation by Galanin and is most abundant in the central nervous system (CNS), where it appears to be critical for development. During embryonal development the expression of GPCR2037 is widespread in the nervous system (dorsal thalamus, striatum, locus coeruleus and hindbrain nuclei). GPCR2037 in the CNS of 7- and 15-day-old mouse embryos can localize to the habenular complex. Low levels of GPCR2037 are detectable in testis, live

The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronecti

MST1R/Ron, a HGF Receptor/MET-type protein kinase, mediates the biological activities of macrophage-stimulating protein (MSP), a multifunctional cytokine that regulates cell adhesion, motility, growth, and survival. The protein is a membrane-spanning, disulfide-linked heterodimer, which results from cleavage of a glycosylated precursor into 35-kD (alpha) and 150-kD (beta) subunits. Ligand binding results in tyrosine phosphorylation of the beta chain. In knockout studies, MST1R/RON (-/-) mice