Characterization of Zebrafish von Willebrand Factor Reveals Conservation of Domain Structure, Multimerization, and Intracellular Storage
Figure 1
Domain organization of human VWF and multispecies alignment of the VWF propeptide and ADAMTS13 cleavage sites and flanking sequences. Sequence alignment was performed using ClustalW2 followed by output using BOXSHADE (Section 2). (a) Domain organization of human VWF. Upper notations indicate known protein-protein interaction domains (Gp: glycoprotein). The solid triangle indicates the propeptide (PP) cleavage site, and the open triangle indicates the ADAMTS13 cleavage site. “B” indicates domains B1–B3. (b) Alignment of sequences surrounding the Arg-Ser (RS, indicated by the solid triangle) human propeptide cleavage site demonstrates a high degree of conservation. Note the extended RX(R/K)R motif present in all species except for medaka. The open triangle indicates the presence of an unconserved cysteine in medaka Vwf. (c) Alignment at the human ADAMTS13 cleavage site (YM, indicated by the solid triangle) and flanking sequences demonstrates conservation of the Tyr-Met residues in mammalian and avian species, but a Phe-Leu putative site in teleost fish. The invariant Leu (human residue 1603) is indicated by a white triangle. z: zebrafish; h: human; m: mouse; ca: canine; c: chicken; fu: fugu; st: stickleback; med: medaka.
