cDNA-derived sequence of chicken embryo vinculin

M. D. Coutu, S. W. Craig

Research output: Contribution to journalArticle

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
StatePublished - 1988

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Vinculin
Chickens
Embryonic Structures
Complementary DNA
Proline
Glutamates
Bacteriophages
Biomedical Research
Amino Acid Sequence
Phospholipids
Cytoplasm
Proteins
Clone Cells
Databases
Amino Acids
Membranes

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

cDNA-derived sequence of chicken embryo vinculin. / Coutu, M. D.; Craig, S. W.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 85, No. 22, 1988, p. 8535-8539.

Research output: Contribution to journalArticle

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