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J. Biol. Chem., Vol. 262, Issue 11, 5308-5312, 04, 1987
MF Gillen, D Banville, RG Rutledge, S Narang, VL Seligy, JF Whitfield and JP MacManus
RNA from a rat liver tumor (Morris hepatoma 5123tc) was used to construct
cDNAs together comprising the complete coding sequence of rat oncomodulin
mRNA. Information obtained from these cDNAs as well as from primer
extension analysis gave a deduced length for the complete oncomodulin mRNA
of approximately 680 nucleotides (excluding the poly(A) tail) including a
5'-untranslated region of 97 +/- 2 nucleotides, a 324-nucleotide-coding
sequence and a 259-nucleotide 3'- noncoding region. Comparison of the
oncomodulin cDNA sequence with those coding for other members of the
calcium-binding protein family shows little homology with the exception of
a recently reported parvalbumin cDNA where the oncomodulin and parvalbumin
nucleotide sequences are 59% identical in the protein-coding region. RNA
blot analysis of poly(A+) RNA from normal adult rat liver gave no evidence
of oncomodulin expression in this tissue. A single RNA species was
detected, however, in RNA extracts from the hepatoma and from rat and human
placentas. A probe prepared from one of the rat oncomodulin cDNAs
hybridized with a single DNA species in restriction digests of hepatoma and
normal DNA from rat and sequences in DNA of humans and other mammals. A
38-nucleotide sequence spanning the 5'-untranslated region and the first
seven codons of the oncomodulin cDNA, was far less homologous than was the
same region of a parvalbumin cDNA, to a chicken calmodulin cDNA sequence
coding for the first calcium-binding domain. The oncomodulin gene appears
to have diverged more from that of calmodulin than has the parvalbumin
gene.
A complete complementary DNA for the oncodevelopmental calcium-binding protein, oncomodulin
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