Molecular characterization of a new immunoglobulin superfamily protein with 
potential roles in opioid binding and cell contact

Schofield, Peter R.; McFarland, K. C.; Hayflick, Joel S.; Wilcox, J. N.; Cho, T. N.; Roy, S.; Lee, N. M.; Loh, H. H.; Seeburg, Peter H.

doi:10.1002/j.1460-2075.1989.tb03402.x

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Molecular characterization of a new immunoglobulin superfamily protein with potential roles in opioid binding and cell contact

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Seeburg, Peter H.
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Schofield, P. R., McFarland, K. C., Hayflick, J. S., Wilcox, J. N., Cho, T. N., Roy, S., et al. (1989). Molecular characterization of a new immunoglobulin superfamily protein with potential roles in opioid binding and cell contact. EMBO Journal, 8(2), 489-495. doi:10.1002/j.1460-2075.1989.tb03402.x.

Cite as: https://hdl.handle.net/21.11116/0000-0000-8ECC-B

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.