Type A modules: interacting domains found in several non-fibrillar collagens and in other extracellular matrix proteins

Matrix. 1993 Jul;13(4):297-306. doi: 10.1016/s0934-8832(11)80025-9.


A 200-amino acid long motif first recognized in von Willebrand Factor (type A module) has been found in components of the extracellular matrix, hemostasis, cellular adhesion, and immune defense mechanisms. At present the extracellular matrix is the predominant site of expression of type A modules since at least four non-fibrillar collagens and two non-collagenous proteins contain a variable number of modules ranging from one to twelve. The modules conform to a consensus motif made of short conserved subregions separated by stretches of variable length. The proteins that incorporate type A modules participate in numerous biological events such as cell adhesion, migration, homing, pattern formation, and signal transduction after interaction with a large array of ligands.

Publication types

  • Comparative Study
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cell Adhesion
  • Chickens
  • Collagen / chemistry
  • Collagen / genetics
  • Collagen / metabolism*
  • Exons
  • Extracellular Matrix / metabolism
  • Extracellular Matrix Proteins / chemistry
  • Extracellular Matrix Proteins / genetics
  • Extracellular Matrix Proteins / metabolism*
  • Humans
  • Molecular Sequence Data
  • Protein Conformation
  • Receptors, Cell Surface / metabolism
  • Sequence Homology, Amino Acid
  • von Willebrand Factor / metabolism*


  • Extracellular Matrix Proteins
  • Receptors, Cell Surface
  • von Willebrand Factor
  • Collagen