U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

LOC280930 ribonuclease, RNase A family, 1 (pancreatic) [ Bos taurus (domestic cattle) ]

Gene ID: 280930, updated on 4-Oct-2024

Summary

Go to the top of the page Help
Gene symbol
LOC280930
Gene description
ribonuclease, RNase A family, 1 (pancreatic)
See related
BGD:BT10837; Ensembl:ENSBTAG00000025663
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Bos taurus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
Also known as
SRN; RAC1; RNASE1
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
See LOC280930 in Genome Data Viewer
Location:
chromosome: 10
Exon count:
2
Annotation release Status Assembly Chr Location
RS_2023_09 current ARS-UCD2.0 (GCF_002263795.3) 10 NC_037337.1 (26223844..26225388)

Chromosome 10 - NC_037337.1Genomic Context describing neighboring genes Neighboring gene eosinophil cationic protein Neighboring gene ribonuclease pancreatic Neighboring gene brain ribonuclease Neighboring gene epididymal secretory protein E3-beta-like

Genomic regions, transcripts, and products

Go to the top of the page Help
Genomic Sequence:
NC_037337.1 Chromosome 10 Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. Heterogeneity of bovine seminal ribonuclease. Di Donato A, et al. Biochemistry, 1981 Dec 8. PMID 7317378
  2. Bovine seminal ribonuclease: structure at 1.9 A resolution. Mazzarella L, et al. Acta Crystallogr D Biol Crystallogr, 1993 Jul 1. PMID 15299514
  3. Role of the hinge peptide and the intersubunit interface in the swapping of N-termini in dimeric bovine seminal RNase. Ercole C, et al. Eur J Biochem, 2003 Dec. PMID 14622261
  4. Crystal structure of the dimeric unswapped form of bovine seminal ribonuclease. Berisio R, et al. FEBS Lett, 2003 Nov 6. PMID 14596923
  5. The unswapped chain of bovine seminal ribonuclease: Crystal structure of the free and liganded monomeric derivative. Sica F, et al. Proteins, 2003 Aug 1. PMID 12833549

See all (41) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. In the regions involved in 3D swapping, the study observed an accumulation of weaknesses in the monomer, which disappear in the dimer and especially in the swapped dimer.
    Title: Stability strengths and weaknesses in protein structures detected by statistical potentials: Application to bovine seminal ribonuclease.
  2. Data suggest that dimerization of seminal ribonuclease (SRN) facilitates three-dimensional domain swapping; both swapped and un-swapped dimers of SRN exhibit increased flexibility as compared to monomeric subunit SRN.
    Title: Mechanism of 3D domain swapping in bovine seminal ribonuclease.
  3. A report of the first clear experimental evidence on the formation of a C-terminal swapped dimer of the monomeric BS-RNase derivatives.
    Title: The multiple forms of bovine seminal ribonuclease: structure and stability of a C-terminal swapped dimer.
  4. Data indicate that BS-RNase oligomers are more enzymatically active than the native dimer.
    Title: Double domain swapping in bovine seminal RNase: formation of distinct N- and C-swapped tetramers and multimers with increasing biological activities.
  5. The domain swapping in BS-RNase must be influenced by the distinct features of the dimers, suggesting a prominent role for the interchain disulfide bridges.
    Title: NMR studies on structure and dynamics of the monomeric derivative of BS-RNase: new insights for 3D domain swapping.
  6. the replacement of of Arg80 by Ser significantly decreases the cytotoxic activity of BS-RNase and the stability of the NCD form with respect to the parent protein, but does not affect the ribonucleolytic activity or the dissociation mechanism
    Title: Structure-cytotoxicity relationships in bovine seminal ribonuclease: new insights from heat and chemical denaturation studies on variants.
  7. Data suggest that, in addition to Pro19 and Leu28, the presence of a glycine at the N-terminal end of the hinge peptide is also important to push the swapped form of RNase A dimer into the compact quaternary organization observed for NCD-BS.
    Title: Toward an antitumor form of bovine pancreatic ribonuclease: the crystal structure of three noncovalent dimeric mutants.
  8. Data show that all the proteins have a very poor cytotoxic activity, independently on the swapping propensity, that can even reach the same value of native BS-RNase.
    Title: Comparison of the structural and functional properties of RNase A and BS-RNase: a stepwise mutagenesis approach.
  9. The structural data enable existing kinetic data on the binding of these compounds to a variety of ribonucleases to be rationalized.
    Title: Influence of naturally-occurring 5'-pyrophosphate-linked substituents on the binding of adenylic inhibitors to ribonuclease a: an X-ray crystallographic study.
  10. Studies show the two isoforms of dimeric RNase, with interchange of the N-terminal helical segments, and without interchange.
    Title: It takes two to flirt with a dimeric RNase.
Submit: New GeneRIF Correction See all GeneRIFs (22)

General gene information

Go to the top of the page Help

Markers

Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables RNA nuclease activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables nucleic acid binding IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

Go to the top of the page Help
Preferred Names
seminal ribonuclease
Names
S-RNase
ribonuclease A C1
ribonuclease BS-1
seminal RNase
NP_861526.1

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_181810.1 → NP_861526.1  seminal ribonuclease precursor

    See identical proteins and their annotated locations for NP_861526.1

    Status: PROVISIONAL

    Source sequence(s)
    AJ000518
    UniProtKB/Swiss-Prot
    P00669
    UniProtKB/TrEMBL
    W0UV03
    Related
    ENSBTAP00000036091.3, ENSBTAT00000036229.4
    Conserved Domains (1) summary
    smart00092
    Location:27 → 150
    RNAse_Pc; Pancreatic ribonuclease

RefSeqs of Annotated Genomes: GCF_002263795.3-RS_2023_09

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference ARS-UCD2.0 Primary Assembly

Genomic

  1. NC_037337.1 Reference ARS-UCD2.0 Primary Assembly

    Range
    26223844..26225388
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P00669.2 GenPept UniProtKB/Swiss-Prot:P00669

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.