Premium
Molecular cloning of human myelin‐associated glycoprotein
Author(s) -
Spagnol G.,
Williams M.,
Srinivasan J.,
Golier J.,
Bauer D.,
Lebo R. V.,
Latov N.
Publication year - 1989
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490240203
Subject(s) - peptide sequence , nucleic acid sequence , complementary dna , biology , microbiology and biotechnology , homology (biology) , amino acid , open reading frame , molecular cloning , glycoprotein , gene isoform , gene , genetics , biochemistry
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 library, 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).