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InterPro: IPR001427 Pancreatic ribonuclease

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481 proteins

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Accession

IPR001427 RNaseA

Type

Family

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.10.130.10	RNaseA	450
ProDom	PD000535	RNaseA	467
Pfam	PF00074	RnaseA	438
PRINTS	PR00794	RIBONUCLEASE	403
PROSITE pattern	PS00127	RNASE_PANCREATIC	417
PANTHER	PTHR11437	RNaseA	455
SMART	SM00092	RNAse_Pc	404
SuperFamily	SSF54076	RNaseA	473
Signatures in BioMart

GO Term annotation Help

Function

GO:0003676 nucleic acid binding
GO:0004522 pancreatic ribonuclease activity

InterPro annotation

Entry Details in BioMart

Abstract

Pancreatic ribonucleases (RNAse) 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 disulphide bonds and three amino acid residues involved in the catalytic activity.

Structural links Help

PDB - click here

SCOP: d.5.1.1

CATH: 3.10.130.10

Database links Help

PDBe-motif: PS00127

Enzyme: EC:3.1.27

PROSITE doc: PDOC00118

PANDIT: PF00074

Blocks: IPB001427

Taxonomic coverage Help

Example proteins Help

P00669 Seminal ribonuclease

P03950 Angiogenin

P21570 Angiogenin

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001427	Pancreatic ribonuclease
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Beintema JJ, van der Laan JM. Comparison of the structure of turtle pancreatic ribonuclease with those of mammalian ribonucleases. FEBS Lett. 194 338-42 1986 [PubMed: 3940901] http://dx.doi.org/10.1016/0014-5793(86)80113-2
2.	Rosenberg HF, Tenen DG, Ackerman SJ. Molecular cloning of the human eosinophil-derived neurotoxin: a member of the ribonuclease gene family. Proc. Natl. Acad. Sci. U.S.A. 86 4460-4 1989 [PubMed: 2734298] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=2734298
3.	Hofsteenge J, Matthies R, Stone SR. Primary structure of a ribonuclease from porcine liver, a new member of the ribonuclease superfamily. Biochemistry 28 9806-13 1989 [PubMed: 2611266] http://dx.doi.org/10.1021/bi00451a040
4.	Rosenberg HF, Ackerman SJ, Tenen DG. Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity. J. Exp. Med. 170 163-76 1989 [PubMed: 2473157] http://dx.doi.org/10.1084/jem.170.1.163

Additional Reading Open in usermanual
	Lewis MT, Hunt LT, Barker WC. Striking sequence similarity among sialic acid-binding lectin, pancreatic ribonucleases, and angiogenin: possible structural and functional relationships. Protein Seq. Data Anal. 2 1989 101-5 [PubMed: 2710786]
	Wlodawer A, Svensson LA, Sjolin L, Gilliland GL. Structure of phosphate-free ribonuclease A refined at 1.26 A. Biochemistry 27 1988 2705-17 [PubMed: 3401445] http://dx.doi.org/10.1021/bi00408a010
	Lee JE, Bae E, Bingman CA, Phillips GN Jr, Raines RT. Structural basis for catalysis by onconase. J. Mol. Biol. 375 2008 165-77 [PubMed: 18001769] http://dx.doi.org/10.1016/j.jmb.2007.09.089
	Merlino A, Ercole C, Picone D, Pizzo E, Mazzarella L, Sica F. The buried diversity of bovine seminal ribonuclease: shape and cytotoxicity of the swapped non-covalent form of the enzyme. J. Mol. Biol. 376 2008 427-37 [PubMed: 18164315] http://dx.doi.org/10.1016/j.jmb.2007.11.008
	Boerema DJ, Tereshko VA, Kent SB. Total synthesis by modern chemical ligation methods and high resolution (1.1 A) X-ray structure of ribonuclease A. Biopolymers 90 2008 278-86 [PubMed: 17610259] http://dx.doi.org/10.1002/bip.20800
	Tereshko V, Uysal S, Koide A, Margalef K, Koide S, Kossiakoff AA. Toward chaperone-assisted crystallography: protein engineering enhancement of crystal packing and X-ray phasing capabilities of a camelid single-domain antibody (VHH) scaffold. Protein Sci. 17 2008 1175-87 [PubMed: 18445622] http://dx.doi.org/10.1110/ps.034892.108
	Beintema JJ, Schuller C, Irie M, Carsana A. Molecular evolution of the ribonuclease superfamily. Prog. Biophys. Mol. Biol. 51 1988 165-92 [PubMed: 3074337] http://dx.doi.org/10.1016/0079-6107(88)90001-6
	Kover KE, Bruix M, Santoro J, Batta G, Laurents DV, Rico M. The solution structure and dynamics of human pancreatic ribonuclease determined by NMR spectroscopy provide insight into its remarkable biological activities and inhibition. J. Mol. Biol. 379 2008 953-65 [PubMed: 18495155] http://dx.doi.org/10.1016/j.jmb.2008.04.042

InterPro 23.1