Fig. 5

Evolutionary history of animal trypsins. a Phylogeny of animal trypsins; clades are named after the orthologs from H. sapiens. Domain architectures for N. vectensis proteins are shown. Proteins with multiple trypsin domains are polyphyletic; in such cases, the domain architecture diagram points to a single trypsin domain and the position of the other trypsin domains is indicated by open/closed circles. Open stars indicate clades that descended from single genes present in the last common ancestor of animals. “N” indicates the position of human neurotrypsin (NP_003610.2). The trypsin-Death protein groups with trypsin-PDZ proteins but is not found on this tree. N. vectensis proteins characterized by in situ hybridization are indicated: arrows (this study), ^†[34], or *[12]. A tree file with branch support values is available on our Github site (https://github.com/josephryan/2019-Babonis_et_al_trypsins). b Comparison of the domain content of trypsins from N. vectensis and H. sapiens. The non-catalytic trypsins do not have associated domains and are not included. The tryptase/transmembrane trypsins are not represented in N. vectensis and are also not included. The “pancreatic” group includes granzyme, kallikrein, HGF, and elastase