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A more recent version of this article appeared on October 1, 2002
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Submitted on May 7, 2002
Revised on June 25, 2002
Accepted on July 10, 2002
1 Howard Hughes Medical Institute, Center for Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139
* Corresponding author. E-mail address: rohynes{at}mit.edu.
The von Willebrand A (VWA) domain is a well-studied domain involved in cell adhesion, in extracellular matrix proteins and in integrin receptors. A number of human diseases arise from mutations in VWA domains. We have analyzed the phylogenetic distribution of this domain and the relationships among close to 500 proteins containing this domain. Although the majority of VWA-containing proteins are extracellular, the most ancient ones present in all eukaryotes are all intracellular proteins involved in functions such as transcription, DNA repair, ribosomal and membrane transport and the proteasome. A common feature appears to be involvement in multiprotein complexes. Subsequent evolution involved deployment of VWA domains by metazoa in extracellular proteins involved in cell adhesion such as integrin ß subunits (all metazoa). Nematodes and chordates separately expanded their complements of extracellular matrix proteins containing VWA domains whereas plants expanded their intracellular complement. Chordates developed VWA-containing integrin 
subunits, collagens and other ECM proteins (e.g. matrilins, cochlin/vitrin, von Willebrand factor). Consideration of the known properties of VWA domains in integrins and ECM proteins allows insights into their involvement in protein-protein interactions and the roles of bound divalent cations and conformational changes. These allow inferences about similar functions in novel situations such as protease regulators (e.g. complement, trypsin inhibitors) and intracellular proteins (e.g. helicases, chelatases and copines).
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