MORC3
Domain
The CW-TYPE zinc finger mediates its binding to trimethylated histone H3K4me3.
Function
Nuclear matrix protein which forms MORC3-NBs (nuclear bodies) via an ATP-dependent mechanism and plays a role in innate immunity by restricting different viruses through modulation of the IFN response (PubMed:27440897, PubMed:34759314). Mechanistically, possesses a primary antiviral function through a MORC3-regulated element that activates IFNB1, and this function is guarded by a secondary IFN-repressing function (PubMed:34759314). Sumoylated MORC3-NBs associates with PML-NBs and recruits TP53 and SP100, thus regulating TP53 activity (PubMed:17332504, PubMed:20501696). Binds RNA in vitro (PubMed:11927593). Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3 (PubMed:26933034). The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0 (PubMed:26933034).
(Microbial infection) May be required for influenza A transcription during viral infection (PubMed:26202233).
Post-translational modifications
Sumoylation is involved in interaction with PML and localization to PML nuclear bodies.
Tissue Specificity
Expressed in heart, placenta, skeletal muscle, brain, pancreas, lung, liver, but not kidney.
Cellular localization
- Nucleus
- Nucleoplasm
- Nucleus matrix
- Nucleus
- PML body
- Chromosome
- Also found in PML-independent nuclear bodies. Localization to nuclear bodies is ATP-dependent.
Alternative names
KIAA0136, NXP2, ZCWCC3, MORC3, MORC family CW-type zinc finger protein 3, Nuclear matrix protein 2, Zinc finger CW-type coiled-coil domain protein 3