Summary: Pancreatic ribonuclease
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Pancreatic ribonuclease Edit Wikipedia article
Structure of RNase A
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / EGO|
Pancreatic ribonucleasea (EC 188.8.131.52, RNase, RNase I, RNase A, pancreatic RNase, ribonuclease I, endoribonuclease I, ribonucleic phosphatase, alkaline ribonuclease, ribonuclease, gene S glycoproteins, Ceratitis capitata alkaline ribonuclease, SLSG glycoproteins, gene S locus-specific glycoproteins, S-genotype-asssocd. glycoproteins, ribonucleate 3'-pyrimidino-oligonucleotidohydrolase) are pyrimidine-specific endonucleases found in high quantity in the pancreas of certain mammals and of some reptiles.
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 ribonuclease superfamily include: bovine seminal vesicle and brain ribonucleases; kidney non-secretory ribonucleases; liver-type ribonucleases; angiogenin, which induces vascularisation of normal and malignant tissues; eosinophil cationic protein, a cytotoxin and helminthotoxin with ribonuclease activity; and frog liver ribonuclease and frog sialic acid-binding lectin. The sequence of pancreatic ribonucleases contains four conserved disulfide bonds and three amino acid residues involved in the catalytic activity.
Human genes encoding proteins containing this domain include:
- van der Laan JM, Beintema JJ (1986). "Comparison of the structure of turtle pancreatic ribonuclease with those of mammalian ribonucleases". FEBS Lett. 194 (2): 338–343. doi:10.1016/0014-5793(86)80113-2. PMID 3940901.
- Rosenberg HF, Ackerman SJ, Tenen DG (1989). "Molecular cloning of the human eosinophil-derived neurotoxin: a member of the ribonuclease gene family". Proc. Natl. Acad. Sci. U.S.A. 86 (12): 4460–4464. doi:10.1073/pnas.86.12.4460. PMC 287289. PMID 2734298.
- Stone SR, Hofsteenge J, Matthies R (1989). "Primary structure of a ribonuclease from porcine liver, a new member of the ribonuclease superfamily". Biochemistry 28 (25): 9806–9813. doi:10.1021/bi00451a040. PMID 2611266.
- Rosenberg HF, Ackerman SJ, Tenen DG (1989). "Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity". J. Exp. Med. 170 (1): 163–176. doi:10.1084/jem.170.1.163. PMC 2189377. PMID 2473157.
- Raines, R. T. (1998). "Ribonuclease A". Chem. Rev. 98: 1045–1066. doi:10.1021/cr960427h. PMID 11848924.
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Ribonucleases. Members include pancreatic RNAase A and angiogenins. Structure is an alpha+beta fold -- long curved beta sheet and three helices.
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR023412Pancreatic ribonucleases (RNaseA) are pyrimidine-specific endonucleases found in high quantity in the pancreas of certain mammals and of some reptiles [PUBMED: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 [PUBMED:2734298]; liver-type ribonucleases [PUBMED:2611266]; angiogenin, which induces vascularisation of normal and malignant tissues; eosinophil cationic protein [PUBMED: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.
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Curation and family details
|Seed source:||Overington and HMM_iterative_training|
|Number in seed:||108|
|Number in full:||847|
|Average length of the domain:||119.30 aa|
|Average identity of full alignment:||33 %|
|Average coverage of the sequence by the domain:||78.61 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||15|
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