Molecular cloning of murine p68, a Ca2+-binding protein of the lipocortin family
- 1 October 1988
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 177 (1), 21-27
- https://doi.org/10.1111/j.1432-1033.1988.tb14340.x
Abstract
A plasmid cDNa library prepared from a T-lymphocyte clone of murine strain B10.A origin was screened by cross-species DNA hybridization using a partial human p68 cDNA clone, identified as containing coding sequences for previously determined amino-acid sequences. The longest p68 cDNA insert from this library and a full-length cDNA insert from a second similar library were fully sequenced. A comparison of the derived amino-acid sequence with that of human p68 revealed extensive homology (95% overall). Homology at the nucleotide level was 89% in the open reading frame and 85% and 50% in the 5'' (33 nucleotides) and 3'' (347 nucleotides) non-coding regions respectively. Eight segments of internal homology were observed, each containing a highly conserved consensus region of 17 amino acids correlating with that described for several membrane associated calcium-binding proteins [Geisow, M. J., Fritsche, U., Hexham, J.M. and Johnson, T. (1986) Nature (Lond.) 320, 636-638]. These results provide further evidence that p68 is a member of the same gene family as p32,p36 and lipocortin I and demonstrate an unusually high level of inter-species sequence conservation of p68 between mouse and human.This publication has 46 references indexed in Scilit:
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