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Vol. 13, Issue 10, 3369-3387, October 2002
Howard Hughes Medical Institute, Center for Cancer Research,
Massachusetts Institute of Technology, Cambridge, Massachusetts 02139
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 ~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 seems 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 
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 extracellular matrix proteins
(e.g., matrilins, cochlin/vitrin, and von Willebrand factor).
Consideration of the known properties of VWA domains in
integrins and extracellular matrix 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 factors and trypsin inhibitors) and
intracellular proteins (e.g., helicases, chelatases, and copines).
Online version of this article contains supplemental material.
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