Perez J L, Shen X, Finkernagel S, Sciorra L, Jenkins N A, Gilbert D J, Copeland N G, Wong T W
Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854.
Oncogene. 1994 Jan;9(1):211-9.
We have cloned a novel receptor tyrosine kinase that has an unusual ectodomain. The extracellular sequence consists of 416 amino acids and has none of the structural motifs that have been found in other receptor tyrosine kinases. The 150 amino acids in the amino terminus of the receptor is homologous to a putative phospholipid-binding sequence that is found also in other cell adhesion molecules such as the neuronal A5 antigen and coagulation factors V and VIII. The kinase domain has a short cytoplasmic tail and contains a short insert between subdomains I and II. The structure of this receptor kinase suggests that it belongs to a new family of receptors involved in cell-cell interactions. The cell adhesion kinase (Cak) is expressed at low levels in most adult tissues and expression is highest in the brain and lung. Using fluorescence in situ hybridization and interspecific backcross mapping, the Cak gene was localized to human chromosome 6 and mouse chromosome 17.
我们克隆了一种具有异常胞外域的新型受体酪氨酸激酶。其胞外序列由416个氨基酸组成，且没有在其他受体酪氨酸激酶中发现的结构基序。该受体氨基末端的150个氨基酸与一个假定的磷脂结合序列同源，此序列也存在于其他细胞黏附分子中，如神经元A5抗原以及凝血因子V和VIII。激酶结构域有一个短的胞质尾巴，并且在亚结构域I和II之间包含一个短插入序列。这种受体激酶的结构表明它属于参与细胞间相互作用的新受体家族。细胞黏附激酶（Cak）在大多数成年组织中低水平表达，在脑和肺中的表达最高。利用荧光原位杂交和种间回交图谱分析，Cak基因被定位到人类6号染色体和小鼠17号染色体上。
