TY - JOUR
T1 - Cloning of cDNA Encoding Rat Phospholipase C-β4, a New Member of the Phospholipase C
AU - Kim, M. J.
AU - Bahk, Y. Y.
AU - Min, D. S.
AU - Lee, S. J.
AU - Ryu, S. H.
AU - Suh, P. G.
PY - 1993/7/30
Y1 - 1993/7/30
N2 - Phospholipase C-β4(PLC-β4), a new member of phospholipase C isozyme, was purified from bovine cerebellum. The cDNA encoding rat PLC-β4 has been cloned from a cDNA library prepared from rat brain. The predicted open reading frame encodes a protein of 1,176 amino acids with a calculated molecular weight of 134,552. The deduced amino acid sequence exhibits 39, 36, and 36% identity with the sequences of rat PLC-β1, human PLC-β2, and rat PLC-β3, respectively. The amino acid sequence of PLC-β4, especially, shows higher identity (50%) with norpA PLC sequence from Drosophila melanogaster than those of other PLC-β subtypes, suggesting that the PLC-β4 might be a mammalian PLC equivalent of norpA PLC implicated in photosignal transduction in Drosophila.
AB - Phospholipase C-β4(PLC-β4), a new member of phospholipase C isozyme, was purified from bovine cerebellum. The cDNA encoding rat PLC-β4 has been cloned from a cDNA library prepared from rat brain. The predicted open reading frame encodes a protein of 1,176 amino acids with a calculated molecular weight of 134,552. The deduced amino acid sequence exhibits 39, 36, and 36% identity with the sequences of rat PLC-β1, human PLC-β2, and rat PLC-β3, respectively. The amino acid sequence of PLC-β4, especially, shows higher identity (50%) with norpA PLC sequence from Drosophila melanogaster than those of other PLC-β subtypes, suggesting that the PLC-β4 might be a mammalian PLC equivalent of norpA PLC implicated in photosignal transduction in Drosophila.
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U2 - 10.1006/bbrc.1993.1879
DO - 10.1006/bbrc.1993.1879
M3 - Article
C2 - 7688223
AN - SCOPUS:0027312968
SN - 0006-291X
VL - 194
SP - 706
EP - 712
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -