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This gene encodes a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. The encoded glycoprotein is a small type II membrane receptor with an extracellular C-type lectin-like domain fold and a cytoplasmic domain with an immunoreceptor tyrosine-based activation motif. It functions as a pattern-recognition receptor that recognizes a variety of beta-1,3-linked and beta-1,6-linked glucans from fungi and plants, and in this way plays a role in innate immune response. Al

The protein encoded by this gene is a member of the keratin gene family. The type II cytokeratins consist of basic or neutral proteins which are arranged in pairs of heterotypic keratin chains coexpressed during differentiation of simple and stratified epithelial tissues. This type II cytokeratin is specifically expressed in the simple epithelia lining the cavities of the internal organs and in the gland ducts and blood vessels. The genes encoding the type II cytokeratins are clustered in a

CYP3A proteins are P450 monooxygenases and in animals, P450 enzymes serve two major functions: biosynthesis of steroids, fatty acids and bile acids, and the metabolism of endogenous and exogenous substrates. A wide variety of exogenous substrates are metabolized by P450 enzymes, including toxins and drugs. The four major families involved in drug metabolism are CYP1, 2, 3 and 4. The hepatic CYP3A1 protein is detected throughout ciliated and nonciliated cells in seven-day-old rats, and i

CYP3A proteins are P450 monooxygenases and in animals, P450 enzymes serve two major functions: biosynthesis of steroids, fatty acids and bile acids, and the metabolism of endogenous and exogenous substrates. A wide variety of exogenous substrates are metabolized by P450 enzymes, including toxins and drugs. The four major families involved in drug metabolism are CYP1, 2, 3 and 4. The hepatic CYP3A1 protein is detected throughout ciliated and nonciliated cells in seven-day-old rats, and i

This gene encodes a glycoprotein with an approximate molecular weight of 76.5 kDa. It is thought to have been created as a result of an ancient gene duplication event that led to generation of homologous C and N-terminal domains each of which binds one ion of ferric iron. The function of this protein is to transport iron from the intestine, reticuloendothelial system, and liver parenchymal cells to all proliferating cells in the body. This protein may also have a physiologic role as granulocy

This gene encodes a member of the natural killer cell receptor C-type lectin family. The encoded protein inhibits osteoclast formation and contains a transmembrane domain near the N-terminus as well as the C-type lectin-like extracellular domain. Several alternatively spliced transcript variants have been identified, but the full-length nature of every transcript has not been defined.