| IED ID | IndEnz0002008271 |
| Enzyme Type ID | protease008271 |
| Protein Name |
Ribonuclease T2 EC 4.6.1.19 |
| Gene Name | RNASET2 |
| Organism | Sus scrofa (Pig) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | HEWKKLIMVHHWPMTVCNEKNCEHPPDYWTIHGLWPDKSGECNRSWPFNPDEIKGLLPDMRLYWPDVLHSSPNHSVHFWRHEWEKHGTCAAQLDALNSQRKYFGKTLDLYKELALNSTLQKLGIKPSISYYQISDIKHALVGVYGVVPKVQCLPPKSGEKVQTLGQIELCLTRDLQLQDCPEPGLEICEDGPVFYPPPKE |
| Enzyme Length | 200 |
| Uniprot Accession Number | Q7M329 |
| Absorption | |
| Active Site | ACT_SITE 32; /evidence=ECO:0000255|PROSITE-ProRule:PRU10045; ACT_SITE 82; /evidence=ECO:0000250|UniProtKB:P08056; ACT_SITE 86; /evidence=ECO:0000255|PROSITE-ProRule:PRU10046 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by Zn(2+) and Cu(2+). {ECO:0000250|UniProtKB:O00584}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284, ChEBI:CHEBI:173118; EC=4.6.1.19; Evidence={ECO:0000255|PROSITE-ProRule:PRU10045}; |
| DNA Binding | |
| EC Number | 4.6.1.19 |
| Enzyme Function | FUNCTION: Ribonuclease that plays an essential role in innate immune response by recognizing and degrading RNAs from microbial pathogens that are subsequently sensed by TLR8. Cleaves preferentially single-stranded RNA molecules between purine and uridine residues, which critically contributes to the supply of catabolic uridine and the generation of purine-2',3'-cyclophosphate-terminated oligoribonucleotides. In turn, RNase T2 degradation products promote the RNA-dependent activation of TLR8. Plays also a key role in degradation of mitochondrial RNA and processing of non-coding RNA imported from the cytosol into mitochondria. Participates as well in degradation of mitochondrion-associated cytosolic rRNAs. {ECO:0000250|UniProtKB:O00584}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (4); Glycosylation (3) |
| Keywords | Direct protein sequencing;Disulfide bond;Endonuclease;Endoplasmic reticulum;Glycoprotein;Hydrolase;Immunity;Innate immunity;Lyase;Lysosome;Mitochondrion;Nuclease;Reference proteome;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O00584}. Lysosome lumen {ECO:0000250|UniProtKB:O00584}. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:O00584}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:O00584}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,136 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:68052 |
| Cross Reference Brenda |