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ProteinQ7293428· pop 7· linked from 7 articles

ranpirnase

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Also known as Amphinase-2, Onconase

Ranpirnase is a ribonuclease enzyme found in the oocytes of the Northern Leopard Frog (Rana pipiens). Ranpirnase is a member of the pancreatic ribonuclease (RNase A) protein superfamily and degrades RNA substrates with a sequence preference for uracil and guanine nucleotides. Along with amphinase, another leopard frog ribonuclease, Ranpirnase has been studied as a potential cancer and antiviral treatment due to its unusual mechanism of cytotoxicity tested against transformed cells and antiviral activity.

Protein · UniProt

Amphinase-2

Organism
Lithobates pipiens (Northern leopard frog)
Length
114 aa
Molecular mass
13,085 Da
Evidence
1: Evidence at protein level

Endonuclease, hydrolyzes highly polymerized RNA, poly(U) and poly(C), and the dinucleotides CpA and UpA. Hydrolyzes 18S and 28S ribosomal RNA. More active towards rCA than rUA or rUG. Has cytotoxic activity against cultured human submaxillary gland carcinoma cells

3D-structureDirect protein sequencingDisulfide bondEndonucleaseGlycoproteinHydrolaseNucleaseSecreted
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Swiss-Prot (reviewed) · via UniProt

Wikidata facts

Instance of
protein
Show 2 more facts
found in taxon
Lithobates pipiens
Commons category
Ranpirnase

via Wikidata · CC0

~6 min read

Encyclopedic overview

8 sections
Contents
  • EC number
  • Reaction pathway
  • Structure
  • Function
  • Known crystal structures
  • Known active sites
  • Structure tied to function
  • References

Ranpirnase is a ribonuclease enzyme found in the oocytes of the Northern Leopard Frog (Rana pipiens). Ranpirnase is a member of the pancreatic ribonuclease (RNase A) protein superfamily and degrades RNA substrates with a sequence preference for uracil and guanine nucleotides. Along with amphinase, another leopard frog ribonuclease, Ranpirnase has been studied as a potential cancer and antiviral treatment due to its unusual mechanism of cytotoxicity tested against transformed cells and antiviral activity.

Ranpirnase was originally discovered by scientists at TamirBio, a biotechnology company (formerly Alfacell Corporation), where it was tested in preclinical assays and in clinical trials under the name Pannon or Onconase, and TMR004. The mechanism of action of ranpirnase has been attributed to the RNA interference pathway, potentially through cleaving siRNA molecules; to cleavage of transfer RNA; and to interference with the NF-κB pathway. Currently (as of March 2020) Ranpirnase is in clinical trials as a potential antiviral.

Excerpted from Wikipedia’s “ranpirnase” article, available under the CC BY-SA 4.0 licence.

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