Angiomotin (IPR009114)

Short name: Angiomotin

Overlapping homologous superfamilies


Family relationships



Angiogenesis, the process whereby new blood vessels are formed by a mechanism of sprouting from existing vessels, has recently been the subject of intense research. Angiostatin, a proteolytically generated fragment of plasminogen consisting of the first four kringle domains, is a potent angiogenesis 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 [PMID: 11257124]. This protein has been named angiomotin.

Angiomotin was identified via a yeast two-hybrid screen for proteins that interact with angiostatin. It is a 72kDa cell-surface associated protein expressed in endothelium and other tissues where angiogenesis occurs, such as placenta and tumours. It appears that angiomotin stimulates angiogenesis by increasing cell motility and that binding of angiostatin inhibits this process [PMID: 11257132]. Two paralogues of angiomotin have recently been cloned and their amino acid sequences determined. Together with angiomotin, these proteins form a novel family bearing little sequence similarity to other known proteins. Sequence analysis has revealed putative coiled-coil and PDZ-binding domains [PMID: 12406577].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.