A. Roglic et al., CDNA CLONING OF A NOVEL G-PROTEIN-COUPLED RECEPTOR WITH A LARGE EXTRACELLULAR LOOP STRUCTURE, Biochimica et biophysica acta, N. Gene structure and expression, 1305(1-2), 1996, pp. 39-43
A cDNA designated as AZ3B has been isolated from a differentiated HL-6
0 cell cDNA library with a probe derived from the N-formyl peptide rec
eptor gene. The 1.97-kb cDNA encodes a novel G protein-coupled recepto
r (GPCR) with 482 amino acids. In addition to the predicted 7 transmem
brane domains common to all GPCRs, the protein encoded by AZ3B contain
s a large extracellular loop of similar to 172 amino acids between the
fourth and the fifth transmembrane domains, a feature unique among th
e hundreds of GPCRs identified to date. High sequence homology exists
between the AZ3B protein and a number of chemoattractant receptors in
the amino-terminal 170 residues and the carboxyl-terminal 150 residues
. Northern and flow cytometric analyses suggested that the AZ3B messag
e and protein are widely expressed in several differentiated hematopoi
etic cell lines, in the lung, placenta, heart, and endothelial cells.
We postulate that the AZ3B protein defines a distinct group of recepto
rs within the GPCR superfamily.