Pathways & interactions
Ribonuclease A-like domain superfamily (IPR036816)
Short name: RNaseA-like_dom_sf
- Pancreatic ribonuclease (IPR001427)
- Ribonuclease A-domain (IPR023412)
- Probable inactive ribonuclease-like protein 13 (IPR029739)
- Probable inactive ribonuclease-like protein 12 (IPR029740)
- Inactive ribonuclease-like protein 9 (IPR029741)
- Inactive ribonuclease-like protein 10 (IPR029742)
- Ribonuclease 11 (IPR029743)
- Epididymal secretory protein E3-alpha (IPR029747)
- Epididymal secretory protein E3-beta (IPR029748)
Pancreatic ribonucleases (RNaseA) are pyrimidine-specific endonucleases found in high quantity in the pancreas of certain mammals and of some reptiles [PMID: 3940901]. Specifically, the enzymes are involved in endonucleolytic cleavage of 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cyclic phosphate intermediates. Ribonuclease can unwind the DNA helix by complexing with single-stranded DNA; the complex arises by an extended multi-site cation-anion interaction between lysine and arginine residues of the enzyme and phosphate groups of the nucleotides. Other proteins belonging to the pancreatic RNAse family include: bovine seminal vesicle and brain ribonucleases; kidney non-secretory ribonucleases [PMID: 2734298]; liver-type ribonucleases [PMID: 2611266]; angiogenin, which induces vascularisation of normal and malignant tissues; eosinophil cationic protein [PMID: 2473157], a cytotoxin and helminthotoxin with ribonuclease activity; and frog liver ribonuclease and frog sialic acid-binding lectin. The sequence of pancreatic RNases contains four conserved disulphide bonds and three amino acid residues involved in the catalytic activity.
This entry represents a domain superfamily found in Ribonuclease A. Its structure is an alpha+beta fold with long curved beta sheet and three helices.