We report the complete primary structure of chicken embryo vinculin. The amino acid sequence was derived from the nucleotide sequence of five overlapping cDNA clones isolated from a λgt11 phage library. Chicken embryo vinculin contains 1066 amino acids, has a calculated M(r) of 116,990, a calculated pI of 5.9, and a hydropathy index of -4.22. A search of the National Biomedical Research Foundation protein sequence data base found no proteins with significant homology to vinculin. A striking feature of the linear sequence is a proline-rich region extending between residues 837 and 879. This region contains 45% proline and 19% aspartic plus glutamic acids; it is also the longest hydrophilic stretch in the molecule. The proline-rich region separates an amino-terminal domain with a calculated pI of 5.4 from a carboxyl-terminal domain with a calculated pI of 9.7. This feature suggests a structural basis for the specific interaction of vinculin with acidic phospholipids and a mechanism for the shuttling of vinculin between cytoplasm and membrane-associated junctional plaque.
|Original language||English (US)|
|Number of pages||5|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|State||Published - 1988|
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