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(Received for publication, July 2, 1996, and in revised form, December 13, 1996)
From the Department of Biotechnology, Faculty of Engineering,
Okayama University, Tsushima-Naka, Okayama 700, Japan and
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 Fc
Volume 272, Number 11,
Issue of March 14, 1997
pp. 7320-7327
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
Core Research for Evolutional Science and Technology,
Japan Science and Technology Corporation, Japan
2
receptor, and a human Fc
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.
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