Kornblihtt A R, Umezawa K, Vibe-Pedersen K, Baralle F E
EMBO J. 1985 Jul;4(7):1755-9. doi: 10.1002/j.1460-2075.1985.tb03847.x.
Cellular and plasma fibronectins are heterodimers consisting of similar but not identical polypeptides. The differences between fibronectin subunits are due in part to the variability of internal primary sequences. This results from alternative splicing in at least two regions (ED and IIICS) of the pre-mRNA. The complete primary structure of human fibronectin, including most of the internal variations, has been determined by sequencing a series of overlapping cDNA clones. In total, they covered 7692 nucleotides and represented the mRNA sequence coding from the amino terminus of the mature protein to the poly(A) tail. The deduced amino acid sequence of fibronectin has been analysed in terms of the arrangement of internal homologies and the different binding domains.
细胞纤连蛋白和血浆纤连蛋白是由相似但不相同的多肽组成的异二聚体。纤连蛋白亚基之间的差异部分归因于内部一级序列的变异性。这是由前体mRNA至少两个区域(ED和IIICS)的可变剪接导致的。通过对一系列重叠的cDNA克隆进行测序,已确定了人纤连蛋白的完整一级结构,包括大部分内部变异。它们总共覆盖了7692个核苷酸,代表了从成熟蛋白的氨基末端到聚腺苷酸尾的mRNA序列。已根据内部同源性的排列和不同的结合域对纤连蛋白推导的氨基酸序列进行了分析。