|PROSITE documentation PDOC50234
VWFA domain profile
Von Willebrand factor (VWF) is a large, multimeric blood glycoprotein that is
required for normal hemostasis. Mutant forms are involved in the most common
inherited bleeding disorder (von Willebrand disease: VWD). VWF mediates the
adhesion of platelets to sites of vascular damage by binding to specific
platelet membrane glycoproteins and to constituents of exposed connective
tissue. It is also essential for the transport of the blood clotting factor
VWF is a large multidomain protein. Among those domains the type A domain is
known to be distributed in at least 22 human proteins, all of them being
extracellular. In VWF there is 3 repeats of the type A domain (A1,A2,A3) that
have been shown to bind other proteins like collagen and heparin. The 3D
structure of A1 and A3 has been published [3,4]. The domain adopts a classic
α/β "Rossmann" fold.
The following proteins have been found to contain a VWFA domain:
- Complement factors B, C2, CR3 and CR4.
- Collagen type VI.
- Collagen type VII.
- Collagen type XII.
- Collagen type XIV.
- Integrin α chains. In these proteins, the VWFA domain is known as a 'I-
- Human cartilage matrix protein. Major component of the extracellular matrix
of nonarticular cartilage. Binds to collagen.
- Mammalian calcium channel α-2/delta subunits.
- Cochlin. In human, defects in COCH are the cause of mucopolysaccharide
depositions in the channels of cochlear and vesicular nerves. These
depositions cause degeneration of dendritic fibers.
- Epithelial chloride channel protein. Voltage-gate chloride channel.
- Inter-α-trypsin inhibitor heavy chains H1, H2 and H4. They are involved
in a variety of immune phenomena.
- Mouse matrilin-2.
- Plasmodium berghei sporozoite surface protein 2.
- Caenorhabditis elegans unc-36 protein.
We developed a profile that spans the whole domain.
December 2001 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|VWFA, PS50234; VWFA domain profile (MATRIX)
|Sequences known to belong to this class detected by the profile:
|Other sequence(s) detected in Swiss-Prot:
|Matching PDB structures:
1AO3 1AOX 1ATZ 1AUQ ... [ALL]
||Voorberg J., Fontijn R., van Mourik J.A., Pannekoek H.
||Domains involved in multimer assembly of von willebrand factor (vWF): multimerization is independent of dimerization.
||EMBO J. 9:797-803(1990).
||Huizinga E.G., Martijn van der Plas R., Kroon J., Sixma J.J., Gros P.
||Crystal structure of the A3 domain of human von Willebrand factor: implications for collagen binding.
||Emsley J., Cruz M., Handin R., Liddington R.
||Crystal structure of the von Willebrand Factor A1 domain and implications for the binding of platelet glycoprotein Ib.
||J. Biol. Chem. 273:10396-10401(1998).
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