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Primary structure of human fibronectin: differential splicing may generate at least 10 polypeptides from a single gene.
Author(s) -
Kornblihtt A.R.,
Umezawa K.,
VibePedersen K.,
Baralle F.E.
Publication year - 1985
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1985.tb03847.x
Subject(s) - rna splicing , protein primary structure , alternative splicing , gene , biology , fibronectin , complementary dna , sequence (biology) , coding region , genetics , messenger rna , microbiology and biotechnology , peptide sequence , rna , extracellular matrix
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.