Essential for epigenetic silencing by the HUSH complex. Recruited by HUSH to target site in heterochromatin, the ATPase activity and homodimerization are critical for HUSH-mediated silencing (By similarity). Represses germ cell-related genes and L1 retrotransposons in collaboration with SETDB1 and the HUSH complex, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark (PubMed:29728365). Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression. During DNA damage response, regulates chromatin remodeling through ATP hydrolysis (By similarity). During DNA damage response, may regulate chromatin remodeling through ATP hydrolysis (By similarity). ATP + H2O = ADP + H(+) + phosphate ATPase activity is dependent of phosphorylation by PAK1 and presence of DNA. Homodimerizes upon ATP-binding and dissociate upon ATP hydrolysis; homodimerization is required for gene silencing (By similarity). Binds histone H3 independently of the methylation status at 'Lys-9' (PubMed:29728365). Interacts with HDAC4. Interacts with FAM208A/TASOR and MPHOSPH8; the interactions associate MORC2 with the HUSH complex which recruits MORC2 to heterochromatic loci (By similarity). Interacts with Morc2b (PubMed:29329290). Mainly located in the nucleus. Upon phosphorylation at Ser-737, recruited to damaged chromatin. Expressed in the axons and Schwann cells of peripheral nerves. Expressed in testes (PubMed:29329290). Phosphorylated by PAK1 at Ser-737 upon DNA damage. Phosphorylation is required for ATPase activity and recruitment to damaged chromatin. Extended N-terminus.