Two forms of 1B236/myelin-associated glycoprotein, a cell adhesion molecule for postnatal neural development, are produced by alternative splicing.
The structures of two rat brain-specific 1B236 mRNAs, alternative splice products from a single gene regulated differently during postnatal brain development, were deduced from full-length cDNA clones. The 626- and 582-amino acid-long encoded proteins are indistinguishable from two forms of myelin-associated glycoprotein, a cell adhesion molecule involved in axonal-glial and glial-glial interactions in postnatal brain development, particularly in myelination. The two proteins share a single membrane-spanning domain and a glycosylated N terminus but differ in the structures of their C termini. The N terminus consists of five domains related in sequence to each other and to immunoglobulin-like molecules, especially the neural cell adhesion molecule N-CAM, suggesting a common structure for cell adhesion molecules.
D000375:Aging; D000595:Amino Acid Sequence; D000818:Animals; D000954:Antigens, Surface / Q000235:genetics*; D001483:Base Sequence; D001921:Brain / Q000254:growth & development*; D002448:Cell Adhesion; D015815:Cell Adhesion Molecules; D003001:Cloning, Molecular; D004247:DNA / Q000378:metabolism; D005796:Genes; D009185:Myelin Proteins / Q000235:genetics*; D018992:Myelin-Associated Glycoprotein; D012326:RNA Splicing; D012333:RNA, Messenger / Q000235:genetics*; D051381:Rats
D000954:Antigens, Surface; D015815:Cell Adhesion Molecules; D009185:Myelin Proteins; D018992:Myelin-Associated Glycoprotein; D012333:RNA, Messenger; D004247:DNA