Abstract
We have cloned from murine macrophages a cDNA coding for a new protein of the scavenger receptor family whose mRNA is increased very strongly by adherence and moderately by exposure to tumor necrosis factor and interferon-gamma. The nucleotidic sequence extends for 2168 bases and encodes a protein of 559 amino acids with six potential glycosylation sites. The first 100 NH2-terminal amino acids represent a single scavenger receptor cysteine-rich domain, whereas the COOH-terminal end of the molecule is compatible either with a transmembrane hydrophobic peptide followed by a very short intracytoplasmic sequence or a signal sequence for an anchoring via a glycophosphatidylinositol. The protein is highly homologous to most of the very recently identified human MAC-2-binding protein and murine cyclophilin C-associated protein.
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