{PDOC00118}
{PS00127; RNASE_PANCREATIC}
{BEGIN}
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* Pancreatic ribonuclease family signature *
********************************************

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.

-Consensus pattern: C-K-x(2)-N-T-F
                    [C is involved in a disulfide bond]
                    [K is an active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: 4.
-Last update: October 1993 / Text revised.

[ 1] Beintema J.J., Schuller C., Irie M., Carsana A.
     "Molecular evolution of the ribonuclease superfamily."
     Prog. Biophys. Mol. Biol. 51:165-192(1988).
     PubMed=3074337
[ 2] Beintema J.J., van der Laan J.M.
     "Comparison of the structure of turtle pancreatic ribonuclease with
     those of mammalian ribonucleases."
     FEBS Lett. 194:338-342(1986).
     PubMed=3940901
[ 3] Rosenberg H.F., Tenen D.G., Ackerman S.J.
     "Molecular cloning of the human eosinophil-derived neurotoxin: a
     member of the ribonuclease gene family."
     Proc. Natl. Acad. Sci. U.S.A. 86:4460-4464(1989).
     PubMed=2734298
[ 4] Hofsteenge J., Matthies R., Stone S.R.
     "Primary structure of a ribonuclease from porcine liver, a new member
     of the ribonuclease superfamily."
     Biochemistry 28:9806-9813(1989).
     PubMed=2611266
[ 5] Rosenberg H.F., Ackerman S.J., Tenen D.G.
     "Human eosinophil cationic protein. Molecular cloning of a cytotoxin
     and helminthotoxin with ribonuclease activity."
     J. Exp. Med. 170:163-176(1989).
     PubMed=2473157
[ 6] Lewis M.T., Hunt L.T., Barker W.C.
     "Striking sequence similarity among sialic acid-binding lectin,
     pancreatic ribonucleases, and angiogenin: possible structural and
     functional relationships."
     Protein Seq. Data Anal. 2:101-105(1989).
     PubMed=2710786

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