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Description

Tudor domain-containing protein 3 (UniProt: Q9H7E2, also known as TDRD3) is encoded by the TDRD3 gene (Gene ID: 81550) in human. TDRD3 belongs to an evolutionarily conserved family of 12 proteins (TDRD1-TDRD12) that contain one or more Tudor domains, which recognize symmetric dimethylarginine (sDMA) residues with the exception of TDRD3, which associates selectively with asymmetric dimethylarginine. TDRD3, in addition to its Tudor domain, contains a putative nucleic acid recognition motif and an ubiquitin-associated domain. Tudor domains are highly conserved throughout evolution: they can be found in virtually all organisms, from bacteria to mammals. TDRD3 has been reported in heart, brain, placenta, lung, liver, skeletal muscle, kidney, and pancreas. It is found both in the nucleus and in cytoplasm. In nucleus, it acts as a coactivator and recognizes and binds asymmetric dimethylation on the core histone tails. The Tudor domain specifically recognizes and binds asymmetric dimethylation of histone H3 &prime,Arg-17&prime, (H3R17me2a) and histones H4 &prime,Arg-3&prime,, 2 tags for epigenetic transcriptional activation. In cytoplasm, it may play a role in the assembly and/or disassembly of mRNA stress granules and in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins. TDRD3 is reported to act as a positive regulator of c-MYC gene transcription by recruiting topoisomerase IIIB (TOP3B) to the c-MYC gene promoter region via H4R3me2a recognition. Overexpression of TDRD3 gene has a strong predictive value for poor prognosis of estrogen receptor-negative breast cancers. (Ref.: Goulet, I et al. (2008). Hum. Mol. Genet. 17(19):3055-3074, Sikorsky, T et al. (2012). Nucleic Acids Res. 40(22):11748-55).