title: The glycopeptide domain of the rat vasopressin precursor.
abstract: The vasopressin precursor is composed of 3 domains, namely vasopressin, MSEL-neurophysin and a glycopeptide. Processing occurs during axonal transport from hypothalamus to neurohypophysis from which the 3 fragments can be isolated. The glycopeptide fragment of the rat vasopressin precursor has been purified and sequenced. Despite the fact that rat MSEL-neurophysin is shortened (93 residues instead of 95 for other mammals), rat glycopeptide has 39 residues, as do the other mammalian glycopeptides, suggesting a similar processing. Fifteen substitutions are however observed when compared to ox glycopeptide. The C-terminal part of MSEL-neurophysin (residues 77-93) and the glycopeptide are encoded by the same exon and the homologies when compared with their bovine counterparts are 58% and 62% respectively. In contrast, the central part of rat MSEL-neurophysin (residues 10-76), which is encoded by a separate exon, displays 96% of homology; vasopressin and the N-terminal part of MSEL-neurophysin (residues 1-9), encoded by a third exon, are nearly invariant.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D006020:Glycopeptides / Q000302:isolation & purification*; D006801:Humans; D011498:Protein Precursors / Q000032:analysis*; D051381:Rats; D013045:Species Specificity; D014667:Vasopressins / Q000032:analysis*
chemical_list: D006020:Glycopeptides; D011498:Protein Precursors; D014667:Vasopressins