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PROSITE documentation PDOC00118 [for PROSITE entry PS00127]

Pancreatic ribonuclease family signature





Description

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.

                        +---------------------------+
                        |        +------------------|------+
                        |        |                  |      |
     xxxxx#xxxxxxCxxxxxxC#xxxxxxxCxxCxxxCxxxxxCxxxxxCxxxxxxCxxx#xxx
                 |      ****        |   |     |
                 |                  +---+     |
                 +----------------------------+
'C': conserved cysteine involved in a disulfide bond.
'#': active site residue.
'*': position of the pattern.

A number of other proteins belongs to the pancreatic RNAse family and these are listed below.

  • Bovine seminal vesicle and bovine brain ribonucleases.
  • The kidney non-secretory ribonucleases (also known as eosinophil-derived neurotoxin (EDN) [3]).
  • Liver-type ribonucleases [4].
  • 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.

Last update:

October 1993 / Text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

RNASE_PANCREATIC, PS00127; Pancreatic ribonuclease family signature  (PATTERN)


References

1AuthorsBeintema J.J. Schuller C. Irie M. Carsana A.
TitleMolecular evolution of the ribonuclease superfamily.
SourceProg. Biophys. Mol. Biol. 51:165-192(1988).
PubMed ID3074337

2AuthorsBeintema J.J. van der Laan J.M.
TitleComparison of the structure of turtle pancreatic ribonuclease with those of mammalian ribonucleases.
SourceFEBS Lett. 194:338-342(1986).
PubMed ID3940901

3AuthorsRosenberg H.F. Tenen D.G. Ackerman S.J.
TitleMolecular cloning of the human eosinophil-derived neurotoxin: a member of the ribonuclease gene family.
SourceProc. Natl. Acad. Sci. U.S.A. 86:4460-4464(1989).
PubMed ID2734298

4AuthorsHofsteenge J. Matthies R. Stone S.R.
TitlePrimary structure of a ribonuclease from porcine liver, a new member of the ribonuclease superfamily.
SourceBiochemistry 28:9806-9813(1989).
PubMed ID2611266

5AuthorsRosenberg H.F. Ackerman S.J. Tenen D.G.
TitleHuman eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity.
SourceJ. Exp. Med. 170:163-176(1989).
PubMed ID2473157

6AuthorsLewis M.T. Hunt L.T. Barker W.C.
TitleStriking sequence similarity among sialic acid-binding lectin, pancreatic ribonucleases, and angiogenin: possible structural and functional relationships.
SourceProtein Seq. Data Anal. 2:101-105(1989).
PubMed ID2710786



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