About TROVE2 / TROVE Domain Family:
The TROVE domain family is mainly found in the TEP1 and Ro60, protein components of ribonucleoproteins.
The TROVE domain family is a module of residues found in protein components (TEP1 and Ro60) of ribonucleoprotein particles. The TROVE domain family is also present in the ribonucleoprotein of bacteria. Additionally, it is associated with other domain families, such as the TEP1 N-terminal, VWFA, WD-40, and NACHT-NTPase domains.
The TROVE domain family is involved in binding three RNA components (Y RNA, telomerase RNA, and vault RNA). The TROVE domain family is made up of some absolute conserved residues, though there is little evidence to prove that they have enzymatic functions.
The Ro60 human recombinant is a single, non-glycosylated polypeptide chain with a molecular mass of 60kDa. It is produced in the E. Coli.
TROVE Domain Family Functions
The TROVE domain family (TROVE2) is mainly involved in RNA binding. The second conserved area of the proteins is a component in the vWA domain family. The vWA domain in TEP1is found to be closely related to the vWA domain found in VPARP. The vWA domain induces interaction between vaults and may also bind as an unrecognized RNP component.
TROVE2 binds several cytoplasmic RNA particles and stabilizes them from degradation. In patients with SLE, the proteins react with normal cellular SSA2 proteins.
Ribonucleoprotein components rely on a regular RNA binding module, the TROVE module. This module is found in bacterial ribonucleoproteins, which suggest that they have an ancient origin.