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An inventory of mucin genes in the chicken genome shows that the mucin domain of Muc13 is encoded by multiple exons and that ovomucin is part of a locus of related gel-forming mucins.

Journal article
Authors Tiange Lang
Gunnar C. Hansson
Tore Samuelsson
Published in BMC genomics
Volume 7
Pages 197
ISSN 1471-2164
Publication year 2006
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 197
Language en
Links dx.doi.org/10.1186/1471-2164-7-197
Keywords Amino Acid Sequence, Animals, Chickens, genetics, Computational Biology, methods, Evolution, Molecular, Exons, Forecasting, Genome, Humans, Membrane Glycoproteins, genetics, Molecular Sequence Data, Mucins, genetics, Multigene Family, Ovomucin, genetics, Phylogeny, Protein Structure, Tertiary, genetics, Sequence Homology, Amino Acid, Tandem Repeat Sequences, Vertebrates, genetics, Zebrafish, genetics, Zebrafish Proteins, genetics
Subject categories Medical and Health Sciences

Abstract

BACKGROUND: Mucins are large glycoproteins that cover epithelial surfaces of the body. All mucins contain at least one PTS domain, a region rich in proline, threonine and serine. Mucins are also characterized by von Willebrand D (VWD) domains or SEA domains. We have developed computational methods to identify mucin genes and proteins based on these properties of the proteins. Using such methods we are able to characterize different organisms where genome sequence is available with respect to their mucin repertoire. RESULTS: We have here made a comprehensive analysis of potential mucins encoded by the chicken (Gallus gallus) genome. Three transmembrane mucins (Muc4, Muc13, and Muc16) and four gel-forming mucins (Muc6, Muc2, Muc5ac, and Muc5b) were identified. The gel-forming mucins are encoded within a locus similar to the corresponding human mucins. However, the chicken has an additional gene inserted between Muc2 and Muc5ac that encodes the the alpha-subunit of ovomucin, a protein similar to Muc2, but it is lacking a PTS domain. We also show that the beta-subunit of ovomucin is the orthologue of human MUC6. The transmembrane Muc13 gene is in chicken as well as in mammals adjacent to the HEG (heart of glass) gene. HEG has PTS, EGF and transmembrane domains like Muc13, suggesting that these two proteins are evolutionary related. Unlike previously known mucins, the PTS domain of Muc13 is encoded by multiple exons, where each exon encodes a repeat unit of the PTS domain. CONCLUSION: We report new mucin homologues in chicken and this information will aid in understanding the evolution of mucins in vertebrates. The fact that ovomucin, a protein not found in mammals, was located in the same locus as other gel-forming mucins provides strong support that these proteins are evolutionary related. Furthermore, a relationship of HEG and the transmembrane Muc13 is suggested on the basis of their biochemical properties and their presence in the same locus. Finally, our finding that the chicken Muc13 is distributed between multiple exons raises the interesting possibility that the length of the PTS domain could be controlled by alternative splicing.

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