Pancreatic ribonucleases (EC 3.1.27.5) are pyrimidine-specific endonucleases
present in high quantity in the pancreas of a number of mammalian taxa and of
a few reptiles [1,2]. As shown in the following schematic representation of
the sequence of pancreatic RNases there are four conserved disulfide bonds and
three amino acid residues involved in the catalytic activity.
Angiogenin, which induces vascularization of normal and malignant tissues.
It abolishes protein synthesis by specifically hydrolyzing cellular tRNAs.
Eosinophil cationic protein (ECP) [5], a cytotoxin and helminthotoxin with
ribonuclease activity.
Frog liver ribonuclease and frog sialic acid-binding lectin [6].
The signature pattern we developed for these proteins includes five conserved
residues: a cysteine involved in a disulfide bond, a lysine involved in the
catalytic activity and three other residues important for substrate binding.
Striking sequence similarity among sialic acid-binding lectin, pancreatic ribonucleases, and angiogenin: possible structural and functional relationships.
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see prosite_license.html.