Regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Required for proper architecture of actin filaments and for cell movements during embryogenesis. Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. Participates in angiogenesis. May play a role in the polarity, proliferation and migration of endothelial cells. Selectively promotes FGF-induced MAPK activation through SRC. Interacts with SRC. Detected before the 1k-cell stage, suggesting that it is maternally supplied. At the sphere stage, stronger expression in the dorsal blastomeres. In the gastrula, expressed in the whole embryo, except in the evacuation zone. During segmentation and pharyngula period, expressed in many distinct domains, including the polster, telencephalon, trigeminal placodes, rhombomeres, trunk neurons, somites and axial vasculature. During the pharyngula period, additional expression observed in lateral line primordia and in intersegmental vessels. Up-regulated by fgf17 and fgf8. Phosphorylation at Tyr-103 is necessary for efficient binding to SRC and synergistically functioning with SRC to activate the downstream MAPK pathway. Belongs to the angiomotin family.