Protein Domain : Angiomotin IPR009114

Type	Family
Description	Angiogenesis, the process whereby new blood vessels are formed by a mechanism of sprouting from existing vessels, has recently been the subjectof intense research. Angiostatin, a proteolytically generated fragment of plasminogen consisting of the first four kringle domains, is a potentangiogenesis inhibitor. Whilst this protein has been known for some time, until recently its mechanism of action was unknown. A functional angiostatin-binding protein has been described that inhibits endothelial cell motility and proliferation, key stages in angiogenesis []. This protein has beennamed angiomotin. Angiomotin was identified via a yeast two-hybrid screen for proteins that interact with angiostatin. It is a 72kDa cell-surface associated proteinexpressed in endothelium and other tissues where angiogenesis occurs, such as placenta and tumours. It appears that angiomotin stimulates angiogenesisby increasing cell motility and that binding of angiostatin inhibits this process []. Two paralogues of angiomotin have recently been cloned andtheir amino acid sequences determined. Together with angiomotin, these proteins form a novel family bearing little sequence similarity to otherknown proteins. Sequence analysis has revealed putative coiled-coil and PDZ-binding domains [].
Short Name	Angiomotin