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Overview

Uniprot IDQ14149
Protein NameMORC family CW-type zinc finger protein 3
Gene NameMORC3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
467 PTYEKTYKKTNKEKF
555 RSSILNAKNRRLSSQ

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)

Protein Sequence

10 MAAQPPRGIR 20 LSALCPKFLH 30 TNSTSHTWPF 40 SAVAELIDNA 50 YDPDVNAKQI 60 WIDKTVINDH 70 ICLTFTDNGN 80 GMTSDKLHKM 90 LSFGFSDKVT 100 MNGHVPVGLY 110 GNGFKSGSMR 120 LGKDAIVFTK 130 NGESMSVGLL 140 SQTYLEVIKA 150 EHVVVPIVAF 160 NKHRQMINLA 170 ESKASLAAIL 180 EHSLFSTEQK 190 LLAELDAIIG 200 KKGTRIIIWN 210 LRSYKNATEF 220 DFEKDKYDIR 230 IPEDLDEITG 240 KKGYKKQERM 250 DQIAPESDYS 260 LRAYCSILYL 270 KPRMQIILRG 280 QKVKTQLVSK 290 SLAYIERDVY 300 RPKFLSKTVR 310 ITFGFNCRNK 320 DHYGIMMYHR 330 NRLIKAYEKV 340 GCQLRANNMG 350 VGVVGIIECN 360 FLKPTHNKQD 370 FDYTNEYRLT 380 ITALGEKLND 390 YWNEMKVKKN 400 TEYPLNLPVE 410 DIQKRPDQTW 420 VQCDACLKWR 430 KLPDGMDQLP 440 EKWYCSNNPD 450 PQFRNCEVPE 460 EPEDEDLVHP 470 TYEKTYKKTN 480 KEKFRIRQPE 490 MIPRINAELL 500 FRPTALSTPS 510 FSSPKESVPR 520 RHLSEGTNSY 530 ATRLLNNHQV 540 PPQSEPESNS 550 LKRRLSTRSS 560 ILNAKNRRLS 570 SQFENSVYKG 580 DDDDEDVIIL 590 EENSTPKPAV 600 DHDIDMKSEQ 610 SHVEQGGVQV 620 EFVGDSEPCG 630 QTGSTSTSSS 640 RCDQGNTAAT 650 QTEVPSLVVK 660 KEETVEDEID 670 VRNDAVILPS 680 CVEAEAKIHE 690 TQETTDKSAD 700 DAGCQLQELR 710 NQLLLVTEEK 720 ENYKRQCHMF 730 TDQIKVLQQR 740 ILEMNDKYVK 750 KETCHQSTET 760 DAVFLLESIN 770 GKSESPDHMV 780 SQYQQALEEI 790 ERLKKQCSAL 800 QHVKAECSQC 810 SNNESKSEMD 820 EMAVQLDDVF 830 RQLDKCSIER 840 DQYKSEVELL 850 EMEKSQIRSQ 860 CEELKTEVEQ 870 LKSTNQQTAT 880 DVSTSSNIEE 890 SVNHMDGESL 900 KLRSLRVNVG 910 QLLAMIVPDL 920 DLQQVNYDVD 930 VVDEILGQVV EQMSEISST

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0016363 nuclear matrix
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0016605 PML body
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0140002 histone H3K4me3 reader activity
Molecular Function GO:0030674 protein-macromolecule adaptor activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0140374 antiviral innate immune response
Biological Process GO:0051457 maintenance of protein location in nucleus
Biological Process GO:0048147 negative regulation of fibroblast proliferation
Biological Process GO:0032688 negative regulation of interferon-beta production
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0018105 peptidyl-serine phosphorylation
Biological Process GO:2000774 positive regulation of cellular senescence
Biological Process GO:0006468 protein phosphorylation
Biological Process GO:0050821 protein stabilization

Reference

PMID: N/A