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rdf:type |
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lifeskim:mentions |
umls-concept:C0002345,
umls-concept:C0017428,
umls-concept:C0026682,
umls-concept:C0029246,
umls-concept:C0086418,
umls-concept:C0376315,
umls-concept:C0678594,
umls-concept:C0681842,
umls-concept:C1417495,
umls-concept:C1749467,
umls-concept:C1883633
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pubmed:issue |
3
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pubmed:dateCreated |
1999-11-23
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pubmed:databankReference |
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pubmed:abstractText |
The MUC3 gene encodes a large, glycosylated mucin produced by intestinal epithelial cells to form a protective barrier against the external environment. Recently published cDNA sequences for the carboxyl-terminal region of MUC3 polypeptide indicated that rodent Muc3 possesses two epidermal growth factor (EGF)-like domains, and putative transmembrane and cytoplasmic domains, whereas the sequence of human MUC3 predicted termination after the first EGF-like domain. Here we describe the complete genomic sequence encompassing the carboxyl terminal region of human MUC3, revealing the boundaries of 11 exons. RT-PCR and cDNA library cloning experiments indicate that the gene is alternatively spliced, yielding a major membrane-bound form as well as multiple soluble forms. Thus, this work indicates that both membrane-bound and soluble MUC3 mucin proteins are produced by alternative splicing of a single gene. A potentially important polymorphism involving a Tyr residue with a proposed role in signalling is described as well.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 1999 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
263
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
728-36
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:10512748-3' Untranslated Regions,
pubmed-meshheading:10512748-Alternative Splicing,
pubmed-meshheading:10512748-Amino Acid Sequence,
pubmed-meshheading:10512748-Animals,
pubmed-meshheading:10512748-Base Sequence,
pubmed-meshheading:10512748-Cell Membrane,
pubmed-meshheading:10512748-Conserved Sequence,
pubmed-meshheading:10512748-Cytoplasm,
pubmed-meshheading:10512748-Epidermal Growth Factor,
pubmed-meshheading:10512748-Exons,
pubmed-meshheading:10512748-Humans,
pubmed-meshheading:10512748-Mice,
pubmed-meshheading:10512748-Molecular Sequence Data,
pubmed-meshheading:10512748-Mucin-3,
pubmed-meshheading:10512748-Mucins,
pubmed-meshheading:10512748-Neoplasm Proteins,
pubmed-meshheading:10512748-Rats,
pubmed-meshheading:10512748-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:10512748-Sequence Alignment,
pubmed-meshheading:10512748-Sequence Homology, Amino Acid
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pubmed:year |
1999
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pubmed:articleTitle |
Genomic organization and structure of the 3' region of human MUC3: alternative splicing predicts membrane-bound and soluble forms of the mucin.
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pubmed:affiliation |
Department of Medicine, University of California, San Francisco, California 94143, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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