Structure update - Up to date with human thyroglobulin

The coding region of the human thyrogloblulin (TG) mRNA has been resequence d, and comparison with the TG sequence originally published in 1987 showed many variations. All of the variations were validated in 20-40 other allele s. and this resulted in the revision of 41 nucleotide positions. This revie w presents the revised wild-type human TG sequence, including all known exo n/exon boundaries and additional data on the TG mRNA population, concerning alternative splicing and variability of the polyadertylation cleavage site . The amino acid sequence derived shows one additional, 12 changed, and 10 polymorphic residues, Protein characteristics, such as acceptor and donor t yrosine residues, N-glycosylation sites, cysteine-rich repeats, the propose d receptor domain, and antigenic epitopes, are included, and their relation ship to the revised sequence is discussed. Furthermore, all reported TG mut ations causing dyshormonogenesis in humans and animals are designated in th e nucleotide and amino acid sequences. This up-to-date profile of the human TG molecule presents the features of importance for its complex role in th yroid hormonogenesis, and is the basis for future studies on the structure- function relationship.