|Protein Name||RNASET2 protein (Fragment)|
|Ref Sequence Id||NP_001193266.1|
|Amino Acid Lenth||291|
|Protein Existence Status||Unreviewed: Experimental evidence at transcript level|
|Presence in other biological fluids/tissue/cells||typically secreted from the cell, or localized to internal compartments such as the lysosome or vacuole|
|Protein Function||Endoribonucleases that cleave single stranded RNA through a 2′,3′–cyclic phosphate intermediate, producing mono- or oligonucleotides with a terminal 3′-phosphate; scavenger of nucleic acids; degradates self- RNA; modulates host immune responses and serve as extra- or intracellular cytotoxins|
|Biochemical Properties||Transferase type RNAses; more broadly distributed; optimal pH of activity of many T2 ribonucleases is between 4 and 5; acidic activity of T2 enzymes is consistent with their localization to the vacuole or lysosome; T2 ribonucleases generally cleave at all four bases; exhibit low pH stability; divalent cations like Cu2+, Zn2+, and Hg2+ are potent inhibitors and in a few cases Mg2+, Ca2+, and Cd2+ were also found to be inhibitory|
|Significance in milk||mediate an extracellular protective role; can participate in the host response against infection both by direct antimicrobial action and immune response activation; induces cytokine release in leukocytes|
|PTMs||glycosylated in eukaryotic cells- glucose, mannose, glucosamine, galactose and xylose|
|Bibliography||1. Inokuchi, N., Saitoh, S., Kobayashi, H., Itagaki, T., Koyama, T., Uchiyama, S., & Irie, M. (1999). Comparison of base specificity and other enzymatic properties of two protozoan ribonucleases from Physarum polycephalum and Dictyostelium discoideum. Bioscience, Biotechnology, and Biochemistry, 63(1), 141–145. https://doi.org/10.1271/bbb.63.141. |
2. Uchida, T. (1966). Purification and properties of RNase T2. Journal of Biochemistry, 60(2), 115–132. https://doi.org/10.1093/oxfordjournals.jbchem.a128410.
3. Shimada, H., Inokuchi, N., Okuwaki, H., Koyama, T., & Irie, M. (1991). Purification and characterization of a base non-specific and adenylic acid preferring ribonuclease from the fruit bodies of Lentinus edodes. Agricultural and Biological Chemistry, 55(4), 1167–1169. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1368676.
4. Inada, Y., Watanabe, H., Ohgi, K., & Irie, M. (1991). Isolation, characterization, and primary structure of a base non-specific and adenylic acid preferential ribonuclease with higher specific activity from Trichoderma viride. Journal of Biochemistry, 110(6), 896–904. https://doi.org/10.1093/oxfordjournals.jbchem.a123686.
5. Inokuchi, N., Koyama, T., Sawada, F., & Irie, M. (1993). Purification, some properties, and primary structure of base non-specific ribonucleases from Physarum polycephalum. Journal of Biochemistry, 113(4), 425–432. https://doi.org/10.1093/oxfordjournals.jbchem.a124062.
6. Thompson, D. M., & Parker, R. (2009). The RNase Rny1p cleaves tRNAs and promotes cell death during oxidative stress in Saccharomyces cerevisiae. The Journal of Cell Biology, 185(1), 43–50. https://doi.org/10.1083/jcb.200811119.
7. Irie, M. (1999). Structure-function relationships of acid ribonucleases: lysosomal, vacuolar, and periplasmic enzymes. Pharmacology & Therapeutics, 81(2), 77–89. https://doi.org/10.1016/s0163-7258(98)00035-7.