RNASE1 ribonuclease, RNase A family, 1 (pancreatic) [Bos taurus (cattle)] - Gene

Summary

Gene symbol: RNASE1
Gene description: ribonuclease, RNase A family, 1 (pancreatic)
See related: BGD:BT10837; EnsemblRapid: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
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Genomic context

Location:: chromosome: 10

Exon count:: 2

Annotation release	Status	Assembly	Chr	Location
106	current	ARS-UCD1.2 (GCF_002263795.1)	10	NC_037337.1 (26223844..26225388)
105	previous assembly	Bos_taurus_UMD_3.1.1 (GCF_000003055.6)	10	AC_000167.1 (26255989..26257533)

Chromosome 10 - NC_037337.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
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.
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.
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.
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.
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.
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.
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.
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.
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

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Markers

MB081 (e-PCR)
- UniSTS:250900

SRN (e-PCR)
- UniSTS:251763

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables RNA nuclease activity	IDA Inferred from Direct Assay more info	PubMed
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables lyase activity	IEA Inferred from Electronic Annotation more info
enables nucleic acid binding	IEA Inferred from Electronic Annotation more info
enables ribonuclease A activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
NOT involved_in defense response to virus	IDA Inferred from Direct Assay more info	PubMed
involved_in metabolic process	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in extracellular region	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: seminal ribonuclease

Names: S-RNase; ribonuclease A C1; ribonuclease BS-1; seminal RNase

NP_861526.1

EC 4.6.1.18

NCBI Reference Sequences (RefSeq)

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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.