RNASE1

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Ribonuclease, RNase A family, 1 (pancreatic)
File:PBB Protein RNASE1 image.jpg
PDB rendering based on 1dza.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols RNASE1 ; MGC12408; RIB1; RNS1
External IDs Template:OMIM5 Template:MGI HomoloGene: 7919
RNA expression pattern
File:PBB GE RNASE1 201785 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Ribonuclease, RNase A family, 1 (pancreatic), also known as RNASE1, is a human gene.[1]

This gene encodes a member of the pancreatic-type of secretory ribonucleases, a subset of the ribonuclease A superfamily. The encoded endonuclease cleaves internal phosphodiester RNA bonds on the 3'-side of pyrimidine bases. It prefers poly(C) as a substrate and hydrolyzes 2',3'-cyclic nucleotides, with a pH optimum near 8.0. The encoded protein is monomeric and more commonly acts to degrade ds-RNA over ss-RNA. Alternative splicing occurs at this locus and four transcript variants encoding the same protein have been identified.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: RNASE1 ribonuclease, RNase A family, 1 (pancreatic)".

Further reading

  • Nogués MV, Vilanova M, Cuchillo CM (1996). "Bovine pancreatic ribonuclease A as a model of an enzyme with multiple substrate binding sites". Biochim. Biophys. Acta. 1253 (1): 16–24. PMID 7492594.
  • Schienman JE, Holt RA, Auerbach MR, Stewart CB (2006). "Duplication and divergence of 2 distinct pancreatic ribonuclease genes in leaf-eating African and Asian colobine monkeys". Mol. Biol. Evol. 23 (8): 1465–79. doi:10.1093/molbev/msl025. PMID 16751256.
  • Sakakibara R, Hashida K, Kitahara T, Ishiguro M (1992). "Characterization of a unique nonsecretory ribonuclease from urine of pregnant women". J. Biochem. 111 (3): 325–30. PMID 1587793.
  • Haugg M, Schein CH (1992). "The DNA sequences of the human and hamster secretory ribonucleases determined with the polymerase chain reaction (PCR)". Nucleic Acids Res. 20 (3): 612. PMID 1741299.
  • Sakakibara R, Hashida K, Tominaga N; et al. (1991). "A putative mouse oocyte maturation inhibitory protein from urine of pregnant women: N-terminal sequence homology with human nonsecretory ribonuclease". Chem. Pharm. Bull. 39 (1): 146–9. PMID 2049798.
  • Mizuta K, Awazu S, Yasuda T, Kishi K (1990). "Purification and characterization of three ribonucleases from human kidney: comparison with urine ribonucleases". Arch. Biochem. Biophys. 281 (1): 144–51. PMID 2383019.
  • Beintema JJ, Blank A, Schieven GL; et al. (1989). "Differences in glycosylation pattern of human secretory ribonucleases". Biochem. J. 255 (2): 501–5. PMID 3202829.
  • Beintema JJ, Wietzes P, Weickmann JL, Glitz DG (1984). "The amino acid sequence of human pancreatic ribonuclease". Anal. Biochem. 136 (1): 48–64. PMID 6201087.
  • Russo N, de Nigris M, Ciardiello A; et al. (1995). "Expression in mammalian cells, purification and characterization of recombinant human pancreatic ribonuclease". FEBS Lett. 369 (2–3): 352. PMID 7649283.
  • Seno M, Futami J, Kosaka M; et al. (1994). "Nucleotide sequence encoding human pancreatic ribonuclease". Biochim. Biophys. Acta. 1218 (3): 466–8. PMID 8049276.
  • Yasuda T, Nadano D, Takeshita H, Kishi K (1994). "Two distinct secretory ribonucleases from human cerebrum: purification, characterization and relationships to other ribonucleases". Biochem. J. 296 ( Pt 3): 617–25. PMID 8280059.
  • Kochetov AV, Lukasheva VV, Filipenko ML; et al. (1996). "[Primary structure of the coding part of the gene for human pancreatic ribonuclease and its chromosomal location]". Bioorg. Khim. 21 (9): 691–4. PMID 8588814.
  • Papageorgiou AC, Shapiro R, Acharya KR (1997). "Molecular recognition of human angiogenin by placental ribonuclease inhibitor--an X-ray crystallographic study at 2.0 A resolution". EMBO J. 16 (17): 5162–77. doi:10.1093/emboj/16.17.5162. PMID 9311977.
  • Klink TA, Woycechowsky KJ, Taylor KM, Raines RT (2000). "Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A.". Eur. J. Biochem. 267 (2): 566–72. PMID 10632727.
  • Pous J, Canals A, Terzyan SS; et al. (2000). "Three-dimensional structure of a human pancreatic ribonuclease variant, a step forward in the design of cytotoxic ribonucleases". J. Mol. Biol. 303 (1): 49–60. doi:10.1006/jmbi.2000.4506. PMID 11021969.
  • Pous J, Mallorquí-Fernández G, Peracaula R; et al. (2001). "Three-dimensional structure of human RNase 1 delta N7 at 1.9 A resolution". Acta Crystallogr. D Biol. Crystallogr. 57 (Pt 4): 498–505. PMID 11264578.
  • Gaur D, Swaminathan S, Batra JK (2001). "Interaction of human pancreatic ribonuclease with human ribonuclease inhibitor. Generation of inhibitor-resistant cytotoxic variants". J. Biol. Chem. 276 (27): 24978–84. doi:10.1074/jbc.M102440200. PMID 11342552.
  • Futami J, Maeda T, Kitazoe M; et al. (2001). "Preparation of potent cytotoxic ribonucleases by cationization: enhanced cellular uptake and decreased interaction with ribonuclease inhibitor by chemical modification of carboxyl groups". Biochemistry. 40 (25): 7518–24. PMID 11412105.
  • Canals A, Pous J, Guasch A; et al. (2002). "The structure of an engineered domain-swapped ribonuclease dimer and its implications for the evolution of proteins toward oligomerization". Structure. 9 (10): 967–76. PMID 11591351.

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