Molecular Cloning of a Novel Murine Cell-surface Glycoprotein Homologous to Killer Cell Inhibitory Receptors

• DOI: 10.1074/jbc.272.11.7320
• Publication Date: 2002-07-26T15:13:47Z
• Authors: Keiko Hayami; Daisuke Fukuta; Yasuhiro Nishikawa; Yumi Yamashita; Masanori Inui; Yukiya Ohyama; Masaki Hikida; Hitoshi Ohmori; Toshiyuki Takai
• Keywords: DNA, Complementary; Membrane Glycoproteins; Base Sequence; Sequence Homology, Amino Acid; Molecular Sequence Data; Receptors, Fc; 3. Good health; Killer Cells, Natural; Mice; 03 medical and health sciences; 0302 clinical medicine; Animals; Humans; Cattle; Amino Acid Sequence; Cloning, Molecular; Sequence Alignment

We have isolated a cDNA clone encoding a novel murine cell-surface glycoprotein. This polypeptide is predicted to be composed of a signal peptide of 23 amino acids, an extracellular region of 620 amino acids that contains six immunoglobulin-like domains with five potential N-glycosylation sites, a transmembrane sequence of 20 amino acids, and a cytoplasmic tail of 178 amino acids with four sets of sequences similar to the immunoreceptor tyrosine-based inhibition motif. The relative molecular mass of the mature polypeptide is calculated to be 90,520 Da. The polypeptide, designated as p91, shows striking homologies to human killer cell inhibitory receptors, a murine gp49B1 protein, a bovine Fcgamma2 receptor, and a human Fcalpha receptor. The mRNA of p91 was especially abundant in murine macrophages. Western blot analysis using p91-specific anti-peptide sera detected a 130-kDa polypeptide in macrophages. Surface biotinylation and immunoprecipitation analysis verified the surface expression of the translation products on COS-1 cells transfected with the p91 cDNA, but the cells failed to show any Fc binding activity.