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Searching the Evolutionary Origin of Epithelial Mucus Protein Components-Mucins and FCGBP

Journal article
Authors Tiange Lang
Sofia Klasson
Erik Larsson
Malin E V Johansson
Gunnar C. Hansson
Tore Samuelsson
Published in Molecular Biology and Evolution
Volume 33
Issue 8
Pages 1921-1936
ISSN 0737-4038
Publication year 2016
Published at Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 1921-1936
Language en
Keywords mucin, mucus, bioinformatics, evolution, von Willebrand D domain, von-willebrand-factor, gel-forming mucins, gliding motility, genome, surface, expression, sequence, layers, transcriptomics, identification, Biochemistry & Molecular Biology, Evolutionary Biology, Genetics &, Heredity
Subject categories Medical Genetics, Cell and Molecular Biology


The gel-forming mucins are large glycosylated proteins that are essential components of the mucus layers covering epithelial cells. Using novel methods of identifying mucins based on profile hidden Markov models, we have found a large number of such proteins in Metazoa, aiding in their classification and allowing evolutionary studies. Most vertebrates have 5-6 gel-forming mucin genes and the genomic arrangement of these genes is well conserved throughout vertebrates. An exception is the frog Xenopus tropicalis with an expanded repertoire of at least 26 mucins of this type. Furthermore, we found that the ovomucin protein, originally identified in chicken, is characteristic of reptiles, birds, and amphibians. Muc6 is absent in teleost fish, but we now show that it is present in animals such as ghost sharks, demonstrating an early origin in vertebrate evolution. Public RNA-Seq data were analyzed with respect tomucins in zebrafish, frog, and chicken, thus allowing comparison in regard of tissue and developmental specificity. Analyses of invertebrate proteins reveal that gel-forming-mucin type of proteins is widely distributed also in this group. Their presence in Cnidaria, Porifera, and in Ctenophora (comb jellies) shows that these proteins were present early in metazoan evolution. Finally, we examined the evolution of the FCGBP protein, abundant in mucus and related to gel-forming mucins in terms of structure and localization. We demonstrate that FCGBP, ubiquitous in vertebrates, has a conserved N-terminal domain. Interestingly, this domain is also present as an N-terminal sequence in a number of bacterial proteins.

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