LSM5 contains the Sm sequence motif, which consists of two regions separated by a linker of variable length that folds as a loop . The Sm-like proteins, including LSM5, are thought to form a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing . Specifically, LSM5 is a component of the U4/U6-U5 tri-snRNP complex involved in spliceosome assembly and the precatalytic spliceosome (spliceosome B complex) .
The heptameric LSM2-8 complex, which includes LSM5, binds specifically to the 3’-terminal U-tract of U6 snRNA . This binding is essential for the proper functioning of the spliceosome, a complex responsible for the removal of introns from pre-mRNA . Additionally, LSM5 is involved in mRNA decapping and degradation, further highlighting its role in RNA processing .