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.
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.


CONCLUSIONS
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.
Lang
Tiange
T
Department of Medical Biochemistry, Goteborg University, Goteborg, Sweden. tiange.lang@medkem.gu.se
Hansson
Gunnar C
GC
Samuelsson
Tore
T
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens / Q000235:genetics*; D019295:Computational Biology / Q000379:methods; D019143:Evolution, Molecular; D005091:Exons; D005544:Forecasting; D016678:Genome; D006801:Humans; D008562:Membrane Glycoproteins / Q000235:genetics; D008969:Molecular Sequence Data; D055271:Mucin 5AC; D055262:Mucin-2; D055257:Mucin-5B; D055272:Mucin-6; D009077:Mucins / Q000235:genetics*; D005810:Multigene Family; D010059:Ovomucin / Q000235:genetics*; D010802:Phylogeny; D017434:Protein Structure, Tertiary / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D020080:Tandem Repeat Sequences; D014714:Vertebrates / Q000235:genetics; D015027:Zebrafish / Q000235:genetics; D029961:Zebrafish Proteins / Q000235:genetics
C429552:MUC13 protein, human; C524625:MUC2 protein, human; C524678:MUC5AC protein, human; C524578:MUC5B protein, human; C524734:MUC6 protein, human; D008562:Membrane Glycoproteins; D055271:Mucin 5AC; D055262:Mucin-2; D055257:Mucin-5B; D055272:Mucin-6; D009077:Mucins; D029961:Zebrafish Proteins; C482644:heg1 protein, zebrafish; D010059:Ovomucin