Telomerase RNA component interacting RNase (TRIR)

Telomerase RNA component interacting RNase (TRIR) is a protein-coding gene recognized for its role as an exoribonuclease that participates in the processing of the 3' end of telomerase RNA. It exhibits both 3'-5' and 5'-3' exonuclease activities, capable of cleaving all four unpaired RNA nucleotides, with higher cleavage efficiency for purine bases. TRIR is important in RNA catabolic processes, including the degradation and processing of ribosomal RNA (rRNA). It is classified molecularly as an enzyme, specifically an exoribonuclease, and has been annotated under several aliases, including C19orf43 and fSAP18. Disease associations are limited and mainly include rare conditions such as binocular vision disease and Tinea unguium. As of current knowledge, there are no established drugs targeting TRIR, and its use as a biomarker or notable safety concerns in therapeutic contexts have not been documented in available sources.

Other names

C19orf43MGC2803fSAP18TERCIRExoribonuclease TRIRfunctional spliceosome-associated protein 18My029 proteinuncharacterized protein C19orf43TRIR