MORC3
entrez
23515
canonical
uniprot
Q14149
canonical
ensembl
ENSG00000159256
resolver
ensp
ENSP00000383333
resolver
enst
ENST00000400485
resolver
genesymbol
MORC3
resolver
genesymbol_syn
KIAA0136
resolver
genesymbol_syn
NXP2
resolver
genesymbol_syn
ZCWCC3
resolver
hgnc
HGNC:23572
resolver
uniprot
A8KA92
resolver
uniprot
B4DHJ4
resolver
uniprot
Q4VBZ9
resolver
uniprot
Q9UEZ2
resolver
uniprot_entry
B4DHJ4_HUMAN
resolver
uniprot_entry
MORC3_HUMAN
resolver
uniprot_entry
Q4VBZ9_HUMAN
resolver
uniprot_sec
A8KA92
resolver
uniprot_sec
Q9UEZ2
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:0000269|PubMed:30850548}.
uniprot
proteins
amino_acid_sequence
MAAQPPRGIRLSALCPKFLHTNSTSHTWPFSAVAELIDNAYDPDVNAKQIWIDKTVINDHICLTFTDNGNGMTSDKLHKMLSFGFSDKVTMNGHVPVGLYGNGFKSGSMRLGKDAIVFTKNGESMSVGLLSQTYLEVIKAEHVVVPIVAFNKHRQMINLAESKASLAAILEHSLFSTEQKLLAELDAIIGKKGTRIIIWNLRSYKNATEFDFEKDKYDIRIPEDLDEITGKKGYKKQERMDQIAPESDYSLRAYCSILYLKPRMQIILRGQKVKTQLVSKSLAYIERDVYRPKFLSKTVRITFGFNCRNKDHYGIMMYHRNRLIKAYEKVGCQLRANNMGVGVVGIIECNFLKPTHNKQDFDYTNEYRLTITALGEKLNDYWNEMKVKKNTEYPLNLPVEDIQKRPDQTWVQCDACLKWRKLPDGMDQLPEKWYCSNNPDPQFRNCEVPEEPEDEDLVHPTYEKTYKKTNKEKFRIRQPEMIPRINAELLFRPTALSTPSFSSPKESVPRRHLSEGTNSYATRLLNNHQVPPQSEPESNSLKRRLSTRSSILNAKNRRLSSQFENSVYKGDDDDEDVIILEENSTPKPAVDHDIDMKSEQSHVEQGGVQVEFVGDSEPCGQTGSTSTSSSRCDQGNTAATQTEVPSLVVKKEETVEDEIDVRNDAVILPSCVEAEAKIHETQETTDKSADDAGCQLQELRNQLLLVTEEKENYKRQCHMFTDQIKVLQQRILEMNDKYVKKETCHQSTETDAVFLLESINGKSESPDHMVSQYQQALEEIERLKKQCSALQHVKAECSQCSNNESKSEMDEMAVQLDDVFRQLDKCSIERDQYKSEVELLEMEKSQIRSQCEELKTEVEQLKSTNQQTATDVSTSSNIEESVNHMDGESLKLRSLRVNVGQLLAMIVPDLDLQQVNYDVDVVDEILGQVVEQMSEISST
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 (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). {ECO:0000269|PubMed:11927593, ECO:0000269|PubMed:17332504, ECO:0000269|PubMed:20501696, ECO:0000269|PubMed:26933034, ECO:0000269|PubMed:27440897, ECO:0000269|PubMed:34759314}.; FUNCTION: (Microbial infection) May be required for influenza A transcription during viral infection (PubMed:26202233). {ECO:0000269|PubMed:26202233}.
uniprot
proteins
mass_dalton
107113
uniprot
proteins
mutagenesis
MUTAGEN 35; /note="E->A: Fails to localize to PML nuclear bodies and activate TP53."; /evidence="ECO:0000269|PubMed:17332504"; MUTAGEN 67; /note="D->N: Forms nuclear bodies, but rapidly diffuses throughout the nucleus under conditions of ATP depletion."; /evidence="ECO:0000269|PubMed:20501696"; MUTAGEN 101; /note="G->A: Diffuse nuclear localization. Fails to form nuclear bodies in the presence of ATP."; /evidence="ECO:0000269|PubMed:20501696"; MUTAGEN 419; /note="W->A: About threefold increase in catalytic activity."; /evidence="ECO:0000269|PubMed:30850548"; MUTAGEN 419; /note="W->A: Diffuse nuclear localization, possibly due to loss of DNA or nucleosome binding."; /evidence="ECO:0000269|PubMed:20501696"; MUTAGEN 431; /note="E->A: Strong decrease of binding to NS1."; /evidence="ECO:0000269|PubMed:31006586"; MUTAGEN 597; /note="K->R: Loss of sumoylation; when associated with R-650; R-651; R-740 and R-794."; /evidence="ECO:0000269|PubMed:20501696"; MUTAGEN 650; /note="K->R: Loss of sumoylation; when associated with R-597; R-651; R-740 and R-794."; /evidence="ECO:0000269|PubMed:20501696"; MUTAGEN 651; /note="K->R: Loss of sumoylation; when associated with R-597; R-650; R-740 and R-794."; /evidence="ECO:0000269|PubMed:20501696"; MUTAGEN 740; /note="K->R: Loss of sumoylation; when associated with R-597; R-650; R-651 and R-794."; /evidence="ECO:0000269|PubMed:20501696"; MUTAGEN 794; /note="K->R: Loss of sumoylation; when associated with R-597; R-650; R-651 and R-740."; /evidence="ECO:0000269|PubMed:20501696
uniprot
proteins
post_translational_modification
PTM: Sumoylation is involved in interaction with PML and localization to PML nuclear bodies. {ECO:0000269|PubMed:20501696}.
uniprot
proteins
pubmed
10830953
uniprot
proteins
pubmed
11927593
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
17332504
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20501696
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
26202233
uniprot
proteins
pubmed
26933034
uniprot
proteins
pubmed
27440897
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
30850548
uniprot
proteins
pubmed
31006586
uniprot
proteins
pubmed
34759314
uniprot
proteins
pubmed
8590280
uniprot
proteins
sequence_length
939
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:11927593, ECO:0000269|PubMed:17332504}. Nucleus matrix {ECO:0000269|PubMed:11927593, ECO:0000269|PubMed:20501696}. Nucleus, PML body {ECO:0000269|PubMed:17332504, ECO:0000269|PubMed:27440897}. Chromosome {ECO:0000250|UniProtKB:F7BJB9}. Note=Also found in PML-independent nuclear bodies. Localization to nuclear bodies is ATP-dependent. {ECO:0000269|PubMed:20501696}.
uniprot
proteins