Morén A, Ichijo H, Miyazono K
Ludwig Institute for Cancer Research, Uppsala, Sweden.
Biochem Biophys Res Commun. 1992 Nov 30;189(1):356-62. doi: 10.1016/0006-291x(92)91566-9.
Full-length cDNAs for the transforming growth factor-beta (TGF-beta) type III receptors were isolated from porcine uterus and human placenta cDNA libraries. The human TGF-beta type III receptor coding region encodes a protein of 849 amino acids with a single transmembrane domain and a short stretch of the intracellular domain. Potential glycosaminoglycan attachment sites were found in the extracellular domain. The overall amino acid sequence identities with those of the porcine and rat TGF-beta type III receptors were 83% and 81%, respectively. A high degree of sequence conservation was observed in the transmembrane and intracellular domains, which also have sequence similarity with human endoglin. In addition, two portions with 29 and 52 amino acids in the extracellular domain were found to be substantially similar with human endoglin.
从猪子宫和人胎盘cDNA文库中分离出转化生长因子-β（TGF-β）Ⅲ型受体的全长cDNA。人TGF-βⅢ型受体编码区编码一种含849个氨基酸的蛋白质，具有一个单一跨膜结构域和一段短的胞内结构域。在胞外结构域发现了潜在的糖胺聚糖附着位点。与人TGF-βⅢ型受体的氨基酸序列总体一致性分别为83%和81%。在跨膜和胞内结构域观察到高度的序列保守性，这些结构域与人内皮糖蛋白也有序列相似性。此外，在胞外结构域发现两个分别含29和52个氨基酸的部分与人内皮糖蛋白基本相似。
