Protein Arginine Methyltransferase 3 (PRMT3)

Type I protein arginine N-methyltransferases (PRMTs), such as PRMT3, catalyze the formation of asymmetric N(G),N(G)-dimethylarginine (ADMA) residues in prote.The C-terminal region of the deduced protein, which contains the putative methyltransferase domain, is 46% identical to Prmt1. The N-terminal 194-amino acid portion is rich in acidic residues and contains a putative zinc finger motif. Immunofluorescence experiments localized Prmt3 predominantly to the cytoplasm of mammalian cells. By searching an EST database, Tang et al. (1998) identified a partial cDNA encoding the human homolog of Prmt3. The predicted human PRMT3 protein, which is missing the first 16 N-terminal amino acids, is 90% identical to rat Prmt3.