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XB-ART-17617
Glycoconj J 1996 Oct 01;135:735-40. doi: 10.1007/bf00702337.
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Alternative splicing of repetitive units is responsible for the polydispersities of integumentary mucin B.1 (FIM-B.1) from Xenopus laevis.

Joba W , Hoffmann W .


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Frog integumentary mucin B.1 (FIM-B.1) represents a polymorphic extracellular mosaic protein which contains tandemly arranged serine/threonine-rich modules as well as cysteine-rich domains. The latter are probably important for oligomerization of FIM-B.1 and have also been found in many proteins of the complement cascade as well as regions homologous to von Willebrand factor. The repetitive modules are targets for extensive O-glycosylation. Previous cDNA cloning experiments clearly established polydispersities within the same individual, which originate from deletions/insertions in the repetitive domain. Here, we analyse part of the corresponding genomic region. Each repetitive unit as well as the cysteine-rich domain is encoded by an individual class 1-1 exon typical of shuffled modules. Alternative splicing of these multiple cassettes creates the polydisperse FIM-B.1 transcripts.

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Species referenced: Xenopus laevis
Genes referenced: muc19

References [+] :
Baltimore, Gene conversion: some implications for immunoglobulin genes. 1981, Pubmed