Molecular cloning of human myelin-associated glycoprotein

✍ Scribed by Dr. G. Spagnol; M. Williams; J. Srinivasan; J. Golier; D. Bauer; R. V. Lebo; N. Latov

• Publisher: John Wiley and Sons
• Year: 1989
• Tongue: English
• Weight: 548 KB
• Volume: 24
• Category: Article
• ISSN: 0360-4012
• DOI: 10.1002/jnr.490240203

✦ Synopsis

The nucleotide sequence for human myelin-associated glycoprotein (MAG) and its deduced amino acid sequence, obtained by analysis of two overlapping cDNA clones isolated from a human brain cDNA li- brary, is presented and compared to that reported for rat MAG.

The sequence provides an open reading frame of 1,878 nucleotides encoding a peptide of 626 amino acids with a calculated molecular weight of 69.1 kD. It is 89% homologous in nucleotide sequence to the large isoform of rat MAG, with 95% homology in the amino acid sequence. It contains 9 potential glycosylation sites, one more than in rat, and shares other key features with rat MAG, including 5 immunoglobulin-like regions of internal homology, an RGD sequence, and potential phosphorylation sites. Its structure appears to be highly conserved in evolution, possibly suggesting a close interdependence between its structure and function. The human gene is located on the proximal long arm of chromosome 19 (19q12 + q13.2).