Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function (PubMed:29146868). Acts as an angiogenesis inhibitor: inhibits migration, proliferation and network formation by endothelial cells as well as angiogenesis (PubMed:19204325). This inhibitory effect is selective to endothelial cells as it does not affect the migration of smooth muscle cells or fibroblasts (By similarity). C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-L-tyrosyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + L-tyrosine Interacts with SVBP; interaction enhances VASH1 tyrosine carboxypeptidase activity. Mainly localizes in the cytoplasm. Some fraction is secreted via a non-canonical secretion system; interaction with SVBP promotes secretion. Expressed at low level in proliferating endothelial cells at the sprouting front but highly expressed in nonproliferating endothelial cells in the termination zone. Ubiquitinated in vitro. Belongs to the transglutaminase-like superfamily. Vasohibin family.