Ringwald M, Schuh R, Vestweber D, Eistetter H, Lottspeich F, Engel J, Dölz R, Jähnig F, Epplen J, Mayer S
Friedrich-Miescher-Laboratorium, der Max-Planck-Gesellschaft, Tübingen, FRG.
EMBO J. 1987 Dec 1;6(12):3647-53. doi: 10.1002/j.1460-2075.1987.tb02697.x.
We have determined the amino acid sequence of the Ca2+-dependent cell adhesion molecule uvomorulin as it appears on the cell surface. The extracellular part of the molecule exhibits three internally repeated domains of 112 residues which are most likely generated by gene duplication. Each of the repeated domains contains two highly conserved units which could represent putative Ca2+-binding sites. Secondary structure predictions suggest that the putative Ca2+-binding units are located in external loops at the surface of the protein. The protein sequence exhibits a single membrane-spanning region and a cytoplasmic domain. Sequence comparison reveals extensive homology to the chicken L-CAM. Both uvomorulin and L-CAM are identical in 65% of their entire amino acid sequence suggesting a common origin for both CAMs.
我们已经确定了细胞表面出现的钙离子依赖性细胞黏附分子桥粒芯蛋白的氨基酸序列。该分子的细胞外部分呈现出三个由112个残基组成的内部重复结构域，很可能是通过基因复制产生的。每个重复结构域包含两个高度保守的单元，可能代表假定的钙离子结合位点。二级结构预测表明，假定的钙离子结合单元位于蛋白质表面的外部环中。该蛋白质序列具有一个单一的跨膜区域和一个细胞质结构域。序列比较显示与鸡的L-CAM有广泛的同源性。桥粒芯蛋白和L-CAM在其整个氨基酸序列中有65%是相同的，这表明这两种细胞黏附分子有共同的起源。
