Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of tubulin protein. Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate. Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of non-tubulin proteins such as MYLK. (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + H2O = (L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + L-glutamate Binds 1 zinc ion per subunit. Inhibited by RARRES1. Interacts with RARRES1, KIF11 AND MAPRE1. Colocalizes with gamma-tubulin in the centrioles and with glutamylated tubulin in the basal bodies of ciliated cells. Belongs to the peptidase M14 family. Was initially shown to catalyze the removal of carboxy-terminus tyrosine from alpha-tubulin (By similarity). However, later studies did not identified any detyrosinase or deglycylase activities from the carboxy-terminus of tubulin (By similarity). Was originally thought to have detyrosinating activity from C-terminal positions on tubulin.