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Glycobiology Advance Access originally published online on March 24, 2004
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Glycobiology vol 14 no 6 pp. 521-527, 2004
Glycobiology vol. 14 no. 6 © Oxford University Press 2004; all rights reserved.

Bioinformatic identification of polymerizing and transmembrane mucins in the puffer fish Fugu rubripes

Tiange Lang2, Marina Alexandersson3, Gunnar C. Hansson1,2 and Tore Samuelsson2

2 Department of Medical Biochemistry, Göteborg University, Gothenburg, Sweden; and 3 FCC, Fraunhofer-Chalmers Research Centre for Industrial Mathematics, Chalmers Science Park, Gothenburg, Sweden

Received on November 24, 2003; revised on January 20, 2004; accepted on February 23, 2004

Mucins are large glycoproteins characterized by mucin domains that show little sequence conservation and are rich in the amino acids Ser, Thr, and Pro. To effectively predict mucins from genomic and protein sequences obtained from genome projects, we developed a strategy based on the amino acid compositional bias characteristic of the mucin domains. This strategy is combined with an analysis of other features commonly found in mucins. Our method has now been used to predict mucins in the puffer fish Fugu rubripes that were previously not identified or annotated. At least three gel-forming mucins were found with the same general domain structure as the human MUC2 mucin. In addition one transmembrane mucin was identified with SEA and EGF domains as found in the mammalian transmembrane mucins. These results suggest that the number of gel-forming mucins has been conserved during evolution of the vertebrates, whereas the family of transmembrane mucins has been markedly expanded in the higher vertebrates.

1 To whom correspondence should be addressed; e-mail: gunnar.hansson{at}medkem.gu.se


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 Proc. Natl. Acad. Sci. USAHome page
T. Lang, G. C. Hansson, and T. Samuelsson
Gel-forming mucins appeared early in metazoan evolution
PNAS, October 9, 2007; 104(41): 16209 - 16214.
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