Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. Zinc finger matrin-type protein 4 (ZMAT4) is a 229 amino acid protein that contains four matrin-type zinc fingers. The matrin-type zinc finger, which is very similar in structure to the classical DNA-binding C2H2 zinc finger, was first identified in the protein matrin-3. It has also been identified in several spliceosome RNA-binding proteins, suggesting a role in pre-mRNA binding. ZMAT4 is localized to the nucleus, and two isoforms of this protein exist as a result of alternative splicing events.