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J. Biol. Chem., Vol. 265, Issue 25, 15294-15299, Sep, 1990
MS Lan, SK Batra, WN Qi, RS Metzgar and MA Hollingsworth
A monospecific polyclonal antiserum against deglycosylated human pancreatic
tumor mucin was used to select human pancreatic mucin cDNA clones from a
lambda gt11 cDNA expression library developed from a human pancreatic tumor
cell line. The full-length 4.4-kilobase mucin cDNA sequence included a
72-base pair 5'-untranslated region and a 307- base pair 3'-untranslated
region. The predicted amino acid sequence for this cDNA revealed a protein
of 122,071 daltons containing 1,255 amino acid residues of which greater
than 60% were serine, threonine, proline, alanine, and glycine.
Approximately two-thirds of the protein sequence consisted of identical
20-amino acid tandem repeats which were flanked by degenerate tandem
repeats and nontandem repeat sequences on both the amino-terminal and
carboxyl-terminal ends. The amino acid sequence also contained five
putative N-linked glycosylation sites, a putative signal sequence and
transmembrane domain, and numerous serine and threonine residues (potential
O-linked glycosylation sites) outside and within the tandem repeat
position. The cDNA and deduced amino acid sequence of the pancreatic mucin
sequence was over 99% homologous with a mucin cDNA sequence derived from
breast tumor mucin, even though the native forms of these molecules are
quite distinct in size and degree of glycosylation.
Cloning and sequencing of a human pancreatic tumor mucin cDNA
Department of Microbiology and Immunology, Duke University Medical Center, Durham, North Carolina 27710.
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