Protein Arginine Methyltransferase 7 (PRMT7)

Arginine methylation is an apparently irreversible protein modification catalyzed by arginine methyltransferases, such as PMT7, using S-adenosylmethionine (AdoMet) as the methyl donor. Arginine methylation is implicated in signal transduction, RNA transport, and RNA splicing. The deduced 692-amino acid protein has 2 methyltransferase domains, each containing a putative AdoMet-binding motif. The N-terminal methyltransferase domain is most similar to the catalytic core of PRMT5, and the C-terminal domain is most similar to PRMT1. Database analysis revealed PRMT7 homologs in several animal and plant species, but not in yeast or prokaryotes. Transfection of COS cells with the longest variant resulted in localization of epitope-tagged PRMT7 to the nucleus and cytoplasm.