Hovens C M, Stacker S A, Andres A C, Harpur A G, Ziemiecki A, Wilks A F
Ludwig Institute for Cancer Research, Royal Melbourne Hospital, Victoria, Australia.
Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):11818-22. doi: 10.1073/pnas.89.24.11818.
By using the polymerase chain reaction with degenerate oligonucleotides based on highly conserved motifs held in common between all members of the protein tyrosine kinase (PTK) family, a PTK-related sequence was isolated from murine peritoneal macrophage cDNA. Full-length clones have been isolated that encompass the entire coding region of the mRNA, and the predicted amino acid sequence indicates that the protein encoded has the structure of a growth factor receptor PTK (RTK). We have dubbed this molecule RYK (for related to tyrosine kinase). The RYK-encoded protein bears a transmembrane domain, with a relatively small (183 amino acid) extracellular domain, containing five potential N-linked glycosylation sites. The intracellular domain of RYK is unique among the broader family of RTKs and has several unusual sequence idiosyncrasies in some of the most highly conserved elements of the PTK domain. These sequence differences call into question the potential catalytic activity of the RYK protein.
通过使用基于蛋白质酪氨酸激酶（PTK）家族所有成员共有的高度保守基序的简并寡核苷酸进行聚合酶链反应，从鼠腹膜巨噬细胞cDNA中分离出一个与PTK相关的序列。已分离出包含mRNA整个编码区的全长克隆，预测的氨基酸序列表明所编码的蛋白质具有生长因子受体PTK（RTK）的结构。我们将该分子命名为RYK（与酪氨酸激酶相关）。RYK编码的蛋白质带有一个跨膜结构域，其细胞外结构域相对较小（183个氨基酸），包含五个潜在的N-连接糖基化位点。RYK的细胞内结构域在更广泛的RTK家族中是独特的，并且在PTK结构域的一些高度保守元件中具有几个不寻常的序列特性。这些序列差异使人对RYK蛋白的潜在催化活性产生疑问。
