Search by BoMiProt ID - Bomi137

Primary Information

BoMiProt ID Bomi137
Protein Name RNASET2 protein (Fragment)
Organism Bos taurus
Uniprot IdQ0III8
Milk FractionWhey
Ref Sequence Id NP_001193266.1
Amino Acid Lenth 291
Molecular Weight 32830
Fasta Sequence
Gene Name RNASET2
Gene Id 508245
Protein Existence Status Unreviewed: Experimental evidence at transcript level

Secondry Information

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.
2. Uchida, T. (1966). Purification and properties of RNase T2. Journal of Biochemistry, 60(2), 115–132.
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
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.
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.
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.
7. Irie, M. (1999). Structure-function relationships of acid ribonucleases: lysosomal, vacuolar, and periplasmic enzymes. Pharmacology & Therapeutics, 81(2), 77–89.