Morc3
entrez
338467
canonical
uniprot
F7BJB9
canonical
ensembl
ENSMUSG00000039456
resolver
ensp
ENSMUSP00000144369
resolver
enst
ENSMUST00000202261
resolver
genesymbol
Morc3
resolver
genesymbol_syn
Nxp2
resolver
genesymbol_syn
Zcwcc3
resolver
uniprot
A6H605
resolver
uniprot
Q4QQR6
resolver
uniprot
Q6A0C2
resolver
uniprot
Q8R0R0
resolver
uniprot_entry
MORC3_MOUSE
resolver
uniprot_sec
A6H605
resolver
uniprot_sec
Q4QQR6
resolver
uniprot_sec
Q6A0C2
resolver
uniprot_sec
Q8R0R0
resolver
activity_regulation
ACTIVITY REGULATION: Dimerization of the ATPase domain is strictly required for the catalytic activity and binding to double-stranded DNA. Disrupting the interface between ATPase and the CW domains releases autoinhibition since the CW domain sterically impedes binding of the ATPase domain to DNA. {ECO:0000250|UniProtKB:Q14149}.
uniprot
proteins
amino_acid_sequence
MAAQPPTGIRLSALCPKFLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVISDHICLTFTDNGNGMTADKLHKMLSFGFSDKVTMNGHVPVGLYGNGFKSGSMRLGKDAMVFTKNGETMSVGFLSQTYLEVIKAEHVVVPIVTFNKHRQMINLTESKASLAAILEHSLFSTEQKLLAELNAIMGKKGTRIIIWNLRSYKNATEFDFEKDKYDIRIPEDLDETAGRKGYKKQERMDQIAPESDYSLRAYCSILYLKPRMQIIIRGQKVKTQLVSKSLAYIERDVYRPKFLTRTVRITFGFNCRNKDHYGIMMYHKNRLIKAYEKVGCQLKANNMGVGVVGIIECNFLKPTHNKQDFDYTNEYRLTILALGEKLNDYWNEMKVKKNAEYPVNLPVEDIQKRPDQTWVQCDACLKWRKLPDGIDQLPEKWYCSNNPDPQFRNCEVPEEPEDEDLVHPTYEKTYKKTSKERFRIRQPEILPRILPQINPELLYQTSVSSQSFSPVKESVPRPHLSEVTSPFAARIINLNLASPASEPENSSMKRKLGVHSSILNAKTRRLSNPPVENSSYKNDDDEDVIILEENSTPKPAVDLEVKSDIEVKSEQSHTEQSGIHVDLVSSPKPCVQASSTSTSTSRSDPGITVSTQTDAPGLTVKKEESMEEDMGVRNGTATLSCVGTEAKVQETSAESVDATSHQLQELRSELLVVTQERDDYKRQCQMFTDQIQVLQQRLLEMNDKCVKKEKCHQSTETDAVFLLDSVNGQAESLDHLGSQYQQALQEIERLKRQCSALQQVKSECSQASCTESKSEVDEMAVQLDDVFRQLDKCTIERDQYKNEVQLLEIEKSHIHSQCEELQTEVEQLKSTGQQAAADGSTASNAEEPVSYVDGESLKLRSLRVNVGQLLAMIVPDLDLQQVNYDVDVVDEILGQVVEQMSEISST
uniprot
proteins
function
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. 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. Sumoylated MORC3-NBs associates with PML-NBs and recruits TP53 and SP100, thus regulating TP53 activity (PubMed:17332504). Binds RNA in vitro. Histone methylation reader which binds to non-methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and trimethylated (H3K4me3) 'Lys-4' on histone H3. The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0. {ECO:0000250|UniProtKB:Q14149, ECO:0000269|PubMed:17332504}.
uniprot
proteins
mass_dalton
106522
uniprot
proteins
post_translational_modification
PTM: Sumoylation is involved in interaction with PML and localization to PML nuclear bodies. {ECO:0000250|UniProtKB:Q14149}.
uniprot
proteins
pubmed
15449545
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17332504
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
27188231
uniprot
proteins
pubmed
27528681
uniprot
proteins
sequence_length
942
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:17332504}. Nucleus matrix {ECO:0000250|UniProtKB:Q14149}. Nucleus, PML body {ECO:0000269|PubMed:17332504}. Chromosome {ECO:0000269|PubMed:27528681}. Note=Also found in PML-independent nuclear bodies. Localization to nuclear bodies is ATP-dependent. {ECO:0000250|UniProtKB:Q14149}.
uniprot
proteins