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Molecular characterization of a new immunoglobulin superfamily protein with potential roles in opioid binding and cell contact.
Author(s) -
Schofield P. R.,
McFarland K. C.,
Hayflick J. S.,
Wilcox J. N.,
Cho T. M.,
Roy S.,
Lee N. M.,
Loh H. H.,
Seeburg P. H.
Publication year - 1989
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1989.tb03402.x
Subject(s) - biology , immunoglobulin superfamily , immunoglobulin domain , peptide sequence , microbiology and biotechnology , complementary dna , biochemistry , neural cell adhesion molecule , cell adhesion molecule , receptor , cell adhesion , cell , gene
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.