Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling (PubMed:15284220, PubMed:19116766, PubMed:19223473,PubMed:9204896). Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1 (PubMed:15284220, PubMed:19116766, PubMed:19223473,PubMed:9204896). In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal (PubMed:15284220, PubMed:19116766, PubMed:19223473,PubMed:9204896). Involved in the regulation of lymphangiogenesis (PubMed:32908006). Interacts with TEK/TIE2, competing for the same binding site as ANGPT1 (PubMed:9204896, PubMed:12427764, PubMed:15284220, PubMed:19223473, PubMed:32908006). Interacts with ITGA5 (PubMed:32908006). The Fibrinogen C-terminal domain mediates interaction with the TEK/TIE2 receptor. The disease is caused by variants affecting the gene represented in this entry. Angiopoietin entry