Sm and Sm-like proteins of the Lsm (like Sm) domain family are generally involved in essential RNA-processing tasks []. All the LSM proteins are evolutionarily conserved in eukaryotes with an N-terminal Lsm domain to bind nucleic acids followed by as yet uncharacterised C-terminal region, some of which have a C-terminal methyltransferase domain. This family includes fungal Sm-like protein 12 (LSM12), which is possibly involved in mRNA degradation or tRNA splicing [].
This entry represents Lsm12 and its homologues. Lsm12 is a putative RNA-binding and regulation protein that might be involved in mRNA degradation or tRNA splicing []. Recently, it was demonstrated that it binds nicotinic acid adenine dinucleotide phosphate (NAADP) that confers NAADP sensitivity to the two pore channel complex (TPCs) by acting as TPC accessory protein necessary for NAADP-evoked Ca2 release []. Therefore, further studies of the potential crosstalk between NAADP signaling and RNA regulation are required.Sm and Sm-like proteins of the Lsm (like Sm) domain family are generally involved in essential RNA-processing tasks []. All the LSM proteins are evolutionarily conserved in eukaryotes with an N-terminal Lsm domain to bind nucleic acids followed by a C-terminal region, some of which have a C-terminal methyltransferase domain.
This domain of approximately 100 residues is conserved from plants to humans. It is an anticodon-binding domain of a prolyl-tRNA synthetase []. It is found in Lms12 and homologues. Lsm12 is a putative RNA-binding and regulation protein that might be involved in mRNA degradation or tRNA splicing []. Recently, it was demonstrated that it binds nicotinic acid adenine dinucleotide phosphate (NAADP) that confers NAADP sensitivity to the two pore channel complex (TPCs) by acting as TPC accessory protein necessary for NAADP-evoked Ca2 release []. Therefore, further studies of the potential crosstalk between NAADP signaling and RNA regulation are required.
