Dahms N M, Lobel P, Breitmeyer J, Chirgwin J M, Kornfeld S
Cell. 1987 Jul 17;50(2):181-92. doi: 10.1016/0092-8674(87)90214-5.
We have isolated cDNA clones encoding the entire sequence of the bovine 46 kd cation-dependent mannose 6-phosphate (CD Man-6-P) receptor. Translation of CD Man-6-P receptor mRNA in Xenopus laevis oocytes results in a protein that binds specifically to phosphomannan-Sepharose, thus demonstrating that our cDNA clones encode a functional receptor. The deduced 279 amino acid sequence reveals a single polypeptide chain that contains a putative signal sequence and a transmembrane domain. Trypsin digestion of microsomal membranes containing the receptor and the location of the five potential N-linked glycosylation sites indicate that the receptor is a transmembrane protein with an extracytoplasmic amino terminus. This extracytoplasmic domain is homologous to the approximately 145 amino acid long repeating domains present in the 215 kd cation-independent Man-6-P receptor.
我们已经分离出编码牛46kd阳离子依赖性甘露糖6-磷酸（CD Man-6-P）受体完整序列的cDNA克隆。在非洲爪蟾卵母细胞中翻译CD Man-6-P受体mRNA会产生一种能与磷酸甘露聚糖-琼脂糖特异性结合的蛋白质，从而证明我们的cDNA克隆编码一种功能性受体。推导的279个氨基酸序列显示出一条单一的多肽链，其中包含一个假定的信号序列和一个跨膜结构域。对含有该受体的微粒体膜进行胰蛋白酶消化以及五个潜在N-连接糖基化位点的定位表明，该受体是一种胞外氨基末端的跨膜蛋白。这个胞外结构域与215kd阳离子非依赖性Man-6-P受体中存在的约145个氨基酸长的重复结构域同源。
