Villin sequence and peptide map identify six homologous domains

Proc Natl Acad Sci U S A. 1988 Jul;85(14):4986-90. doi: 10.1073/pnas.85.14.4986.

Abstract

Site-specific proteases and antisera to the amino terminus of villin have been used to show that villin is organized into seven protease-resistant domains. Six are contained in the amino-terminal Mr 87,000 villin core, a Ca2+-regulated actin-severing fragment, whereas the carboxyl-terminal domain includes the villin "headpiece," a fragment involved in bundling of actin filaments. Ca2+ inhibits proteolytic cleavage between domains in the amino-terminal half of villin. The protein sequence of villin deduced from a single cDNA clone contains a conserved sequence that is repeated six times and is found in each domain of the villin core. The conserved repeats are found in other actin-severing proteins but not in the villin headpiece. Our results suggest that actin-severing proteins are organized around a common Mr 14,000-17,000 domain.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Calcium / pharmacology
  • Calcium-Binding Proteins
  • Carrier Proteins* / genetics
  • Carrier Proteins* / metabolism
  • Chickens
  • Chymotrypsin / metabolism
  • DNA / genetics
  • Electrophoresis, Polyacrylamide Gel
  • Gelsolin
  • Immunoassay
  • Microfilament Proteins* / genetics
  • Microfilament Proteins* / metabolism
  • Molecular Sequence Data
  • Molecular Weight
  • Peptide Fragments / metabolism
  • Repetitive Sequences, Nucleic Acid
  • Sequence Homology, Nucleic Acid
  • Serine Endopeptidases / metabolism
  • Trypsin / metabolism

Substances

  • Calcium-Binding Proteins
  • Carrier Proteins
  • Gelsolin
  • Microfilament Proteins
  • Peptide Fragments
  • villin
  • DNA
  • Serine Endopeptidases
  • Chymotrypsin
  • glutamyl endopeptidase
  • Trypsin
  • Calcium

Associated data

  • GENBANK/J03781
  • PIR/UNKNOWN