cDNA-derived sequence of chicken embryo vinculin

M. D. Coutu, S. W. Craig

Research output: Contribution to journalArticlepeer-review

Abstract

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 languageEnglish (US)
Pages (from-to)8535-8539
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume85
Issue number22
DOIs
StatePublished - 1988

ASJC Scopus subject areas

  • General

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