Pancreatic ribonuclease | |||||||||
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Identifiers | |||||||||
Symbol | RNaseA | ||||||||
Pfam | PF00074 | ||||||||
InterPro | IPR001427 | ||||||||
SMART | SM00092 | ||||||||
PROSITE | PDOC00118 | ||||||||
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Pancreatic ribonucleasea are pyrimidine-specific endonucleases found in high quantity in the pancreas of certain mammals and of some reptiles.[1]
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;[2] liver-type ribonucleases;[3] angiogenin, which induces vascularisation of normal and malignant tissues; eosinophil cationic protein,[4] 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 disulfide bonds and three amino acid residues involved in the catalytic activity.
Human genes encoding proteins containing this domain include:
This article incorporates text from the public domain Pfam and InterPro IPR001427