Molecular characterization of a new immunoglobulin superfamily protein with potential roles in opioid binding and cell contact.
The EMBO JournalPublished 1 February 1989Open access
Peter R. Schofield, Keith McFarland, J. S. Hayflick, J N Wilcox, T. M. Cho, Suzanne Roy
Citations126
SJR quartileQ1
SJR score4.82
SNIP1.93
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Abstract
A purified opioid-binding protein has been characterized by cDNA cloning. The cDNA sequence predicts an extracellularly located glycoprotein of 345 amino acids. This protein does not possess a membrane-spanning domain but contains a C-terminal hydrophobic sequence characteristic of membrane attachment by a phosphatidylinositol linkage. It displays homology to the immunoglobulin protein superfamily, featuring three domains that resemble disulfide-bonded constant regions. More specifically, the protein is most homologous to a subfamily of proteins which includes the neural cell adhesion molecule (NCAM) and myelin-associated glycoprotein (MAG) and one subgroup of the tyrosine kinase growth factor receptors comprising the platelet-derived growth factor receptor (PDGF R), the colony-stimulating factor 1 receptor (CSF-1 R) and the c-kit protooncogene. These sequence homologies suggest that the protein could be involved in either cell recognition and adhesion, peptidergic ligand binding or both.
Keywords
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