Umekage T, Kato K
MRC Molecular Genetics Unit, Cambridge, UK.
FEBS Lett. 1991 Jul 29;286(1-2):147-51. doi: 10.1016/0014-5793(91)80961-2.
We have isolated a mouse brain cDNA clone encoding a protein of 200 amino acids (Mr 20,165) with partial homology with MARCKS (myristoylated alanine-rich C-kinase substrate). Two regions show similarity with MARCKS, one is the kinase C phosphorylation site domain which is supposed to bind calmodulin, and the other is the region near to the N-terminus, including the consensus sequence of myristoylation. It has a similar amino acid composition to MARCKS, but the content of alanine is not as high. It is distributed throughout the mouse brain, but the pattern is not identical with that of MARCKS. Both proteins may be members of a new protein family involved in coupling the protein kinase C and calmodulin signal transduction systems.
我们分离出了一个小鼠脑cDNA克隆,它编码一种由200个氨基酸组成(分子量为20,165)的蛋白质,该蛋白质与MARCKS(肉豆蔻酰化富含丙氨酸的蛋白激酶C底物)有部分同源性。有两个区域与MARCKS相似,一个是假定能结合钙调蛋白的蛋白激酶C磷酸化位点结构域,另一个是靠近N端的区域,包括肉豆蔻酰化共有序列。它的氨基酸组成与MARCKS相似,但丙氨酸含量没那么高。它分布于整个小鼠脑,但分布模式与MARCKS不同。这两种蛋白质可能是参与连接蛋白激酶C和钙调蛋白信号转导系统的新蛋白质家族的成员。