Although the two known naturally-occurring SNPs do not appear to confer any observable consequences to the people who have them, biologists have learned much about the molecular function of the hRNase-1 gene and its encoded protein through various molecular genetic studies.
For example, one of these studies has shown that the first 28 amino acid residues of the hRNase-1 protein serve as a signal peptide, which is a protein sequence that directs the transport of a protein to specific locations within and outside of the cells in which that protein is synthesized. Further, it is known that each one of the asparagine amino acid residues at positions 62, 104 and 116 of the hRNase-1 protein are necessary for glycosylation to occur (glycosylation is a cellular process that is needed for proper protein folding and preservation of protein integrity, among other things).
Finally, it is known that the asparagine and glycine amino acid residues at positions 116 and 117, respectively, of the hRNase-1 protein are not critical to inhibition of the protein by RNase1 inhibitor 1, which is an enzyme that blocks the activity of the hRNase-1 protein by binding to it. That is, when an arginine residue and a serine residue, respectively, are substituted for the asparagine and glycine amino acid residues at positions 116 and 117, RNase1 inhibitor 1 is still able to bind to hRNase1 to effectively block its activity.
While a fair amount in known about hRNAse-1, there is much more left to learn. Fortunately, several groups of scientists are actively studying this gene. Identification of additional ribonuclease-1 gene mutations in the general population and further molecular genetic studies should help facilitate the goal of better understanding the function of this interesting and important gene.