MORC3_HUMAN
ID MORC3_HUMAN Reviewed; 939 AA.
AC Q14149; A8KA92; Q9UEZ2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=MORC family CW-type zinc finger protein 3;
DE AltName: Full=Nuclear matrix protein 2 {ECO:0000303|PubMed:11927593};
DE AltName: Full=Zinc finger CW-type coiled-coil domain protein 3;
GN Name=MORC3 {ECO:0000312|HGNC:HGNC:23572};
GN Synonyms=KIAA0136 {ECO:0000312|HGNC:HGNC:23572},
GN NXP2 {ECO:0000312|HGNC:HGNC:23572}, ZCWCC3 {ECO:0000312|HGNC:HGNC:23572};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=11927593; DOI=10.1074/jbc.m201440200;
RA Kimura Y., Sakai F., Nakano O., Kisaki O., Sugimoto H., Sawamura T.,
RA Sadano H., Osumi T.;
RT "The newly identified human nuclear protein NXP-2 possesses three distinct
RT domains, the nuclear matrix-binding, RNA-binding, and coiled-coil
RT domains.";
RL J. Biol. Chem. 277:20611-20617(2002).
RN [5]
RP FUNCTION, INTERACTION WITH TP53 AND PML, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLU-35.
RX PubMed=17332504; DOI=10.1091/mbc.e06-08-0747;
RA Takahashi K., Yoshida N., Murakami N., Kawata K., Ishizaki H.,
RA Tanaka-Okamoto M., Miyoshi J., Zinn A.R., Shime H., Inoue N.;
RT "Dynamic regulation of p53 subnuclear localization and senescence by
RT MORC3.";
RL Mol. Biol. Cell 18:1701-1709(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP FUNCTION, SUMOYLATION AT LYS-597; LYS-650; LYS-651; LYS-740 AND LYS-794,
RP SUBUNIT, INTERACTION WITH PML, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-67; GLY-101; TRP-419; LYS-597; LYS-650; LYS-651; LYS-740 AND LYS-794.
RX PubMed=20501696; DOI=10.1242/jcs.063586;
RA Mimura Y., Takahashi K., Kawata K., Akazawa T., Inoue N.;
RT "Two-step colocalization of MORC3 with PML nuclear bodies.";
RL J. Cell Sci. 123:2014-2024(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514; SER-540; SER-560 AND
RP SER-765, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-650, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-740, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-650, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [14]
RP FUNCTION, AND INTERACTION WITH INFLUENZA A VIRUS PA AND PB1 POLYMERASE
RP SUBUNITS (MICROBIAL INFECTION).
RX PubMed=26202233; DOI=10.1128/jvi.01530-15;
RA Ver L.S., Marcos-Villar L., Landeras-Bueno S., Nieto A., Ortin J.;
RT "The Cellular Factor NXP2/MORC3 Is a Positive Regulator of Influenza Virus
RT Multiplication.";
RL J. Virol. 89:10023-10030(2015).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-650 AND LYS-651, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HERPES SIMPLEX VIRUS
RP 1/HHV-1 PROTEIN ICP0 (MICROBIAL INFECTION).
RX PubMed=27440897; DOI=10.1128/jvi.00621-16;
RA Sloan E., Orr A., Everett R.D.;
RT "MORC3, a Component of PML Nuclear Bodies, Has a Role in Restricting Herpes
RT Simplex Virus 1 and Human Cytomegalovirus.";
RL J. Virol. 90:8621-8633(2016).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-191; LYS-205; LYS-231; LYS-280;
RP LYS-293; LYS-555; LYS-597; LYS-650; LYS-651; LYS-794 AND LYS-855, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [18]
RP FUNCTION, AND INTERACTION WITH HERPES SIMPLEX VIRUS 1 /HHV-1 PROTEIN ICP0
RP (MICROBIAL INFECTION).
RX PubMed=34759314; DOI=10.1038/s41586-021-04054-5;
RA Gaidt M.M., Morrow A., Fairgrieve M.R., Karr J.P., Yosef N., Vance R.E.;
RT "Self-guarding of MORC3 enables virulence factor-triggered immunity.";
RL Nature 600:138-142(2021).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 400-460 IN COMPLEX WITH THE AMINO
RP TERMINUS OF HISTONE H3, FUNCTION, AND DOMAIN CW-TYPE ZINC FINGER.
RX PubMed=26933034; DOI=10.1074/jbc.m116.718973;
RA Liu Y., Tempel W., Zhang Q., Liang X., Loppnau P., Qin S., Min J.;
RT "Family-wide Characterization of Histone Binding Abilities of Human CW
RT Domain-containing Proteins.";
RL J. Biol. Chem. 291:9000-9013(2016).
RN [20] {ECO:0007744|PDB:6O1E}
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 1-455, ACTIVITY REGULATION,
RP SUBUNIT, AND MUTAGENESIS OF TRP-419.
RX PubMed=30850548; DOI=10.1073/pnas.1819524116;
RA Zhang Y., Klein B.J., Cox K.L., Bertulat B., Tencer A.H., Holden M.R.,
RA Wright G.M., Black J., Cardoso M.C., Poirier M.G., Kutateladze T.G.;
RT "Mechanism for autoinhibition and activation of the MORC3 ATPase.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:6111-6119(2019).
RN [21] {ECO:0007744|PDB:6O5W}
RP X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 407-455, INTERACTION WITH
RP INFLUENZA VIRUS PROTEIN NS1 (MICROBIAL INFECTION), AND MUTAGENESIS OF
RP ASP-67 AND GLU-431.
RX PubMed=31006586; DOI=10.1016/j.str.2019.03.015;
RA Zhang Y., Ahn J., Green K.J., Vann K.R., Black J., Brooke C.B.,
RA Kutateladze T.G.;
RT "MORC3 Is a Target of the Influenza A Viral Protein NS1.";
RL Structure 27:1029-1033.e3(2019).
CC -!- FUNCTION: Nuclear matrix protein which forms MORC3-NBs (nuclear bodies)
CC via an ATP-dependent mechanism and plays a role in innate immunity by
CC restricting different viruses through modulation of the IFN response
CC (PubMed:27440897, PubMed:34759314). Mechanistically, possesses a
CC primary antiviral function through a MORC3-regulated element that
CC activates IFNB1, and this function is guarded by a secondary IFN-
CC repressing function (PubMed:34759314). Sumoylated MORC3-NBs associates
CC with PML-NBs and recruits TP53 and SP100, thus regulating TP53 activity
CC (PubMed:17332504, PubMed:20501696). Binds RNA in vitro
CC (PubMed:11927593). Histone methylation reader which binds to non-
CC methylated (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2)
CC and trimethylated (H3K4me3) 'Lys-4' on histone H3 (PubMed:26933034).
CC The order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 >
CC H3K4me0 (PubMed:26933034). {ECO:0000269|PubMed:11927593,
CC ECO:0000269|PubMed:17332504, ECO:0000269|PubMed:20501696,
CC ECO:0000269|PubMed:26933034, ECO:0000269|PubMed:27440897,
CC ECO:0000269|PubMed:34759314}.
CC -!- FUNCTION: (Microbial infection) May be required for influenza A
CC transcription during viral infection (PubMed:26202233).
CC {ECO:0000269|PubMed:26202233}.
CC -!- ACTIVITY REGULATION: Dimerization of the ATPase domain is strictly
CC required for the catalytic activity and binding to double-stranded DNA.
CC Disrupting the interface between ATPase and the CW domains releases
CC autoinhibition since the CW domain sterically impedes binding of the
CC ATPase domain to DNA. {ECO:0000269|PubMed:30850548}.
CC -!- SUBUNIT: Homodimer (PubMed:17332504, PubMed:30850548). The sumoylated
CC form interacts with PML (via SUMO-interacting motif) (PubMed:20501696,
CC PubMed:17332504). Interacts with TP53 (PubMed:17332504).
CC {ECO:0000269|PubMed:17332504, ECO:0000269|PubMed:20501696,
CC ECO:0000269|PubMed:30850548}.
CC -!- SUBUNIT: (Microbial infection) Interacts with influenza A virus PA and
CC PB1 polymerase subunits during infection (PubMed:26202233). Interacts
CC (via CW domain) with influenza A protein NS1 (PubMed:31006586).
CC {ECO:0000269|PubMed:26202233, ECO:0000269|PubMed:31006586}.
CC -!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus
CC 1/HHV-1 protein ICP0; this interaction mediates MORC3 degradation,
CC which leads to de-repression of a MORC3-regulated DNA element (MRE)
CC adjacent to the IFNB1 locus. {ECO:0000269|PubMed:27440897,
CC ECO:0000269|PubMed:34759314}.
CC -!- INTERACTION:
CC Q14149; Q9NWF9: RNF216; NbExp=3; IntAct=EBI-2556145, EBI-723313;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:11927593, ECO:0000269|PubMed:17332504}. Nucleus
CC matrix {ECO:0000269|PubMed:11927593, ECO:0000269|PubMed:20501696}.
CC Nucleus, PML body {ECO:0000269|PubMed:17332504,
CC ECO:0000269|PubMed:27440897}. Chromosome
CC {ECO:0000250|UniProtKB:F7BJB9}. Note=Also found in PML-independent
CC nuclear bodies. Localization to nuclear bodies is ATP-dependent.
CC {ECO:0000269|PubMed:20501696}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, placenta, skeletal muscle,
CC brain, pancreas, lung, liver, but not kidney.
CC {ECO:0000269|PubMed:11927593}.
CC -!- DOMAIN: The CW-TYPE zinc finger mediates its binding to trimethylated
CC histone H3K4me3. {ECO:0000269|PubMed:26933034}.
CC -!- PTM: Sumoylation is involved in interaction with PML and localization
CC to PML nuclear bodies. {ECO:0000269|PubMed:20501696}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09485.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA89432.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D50926; BAA09485.2; ALT_INIT; mRNA.
DR EMBL; AK292957; BAF85646.1; -; mRNA.
DR EMBL; AP000693; BAA89432.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP000692; BAA89432.1; JOINED; Genomic_DNA.
DR CCDS; CCDS42924.1; -.
DR RefSeq; NP_056173.1; NM_015358.2.
DR PDB; 4QQ4; X-ray; 1.75 A; A/B=400-460.
DR PDB; 5SVI; X-ray; 1.61 A; A=407-453.
DR PDB; 5SVX; X-ray; 1.56 A; A=407-454.
DR PDB; 5SVY; X-ray; 1.05 A; A=407-455.
DR PDB; 6O1E; X-ray; 2.41 A; A=1-455.
DR PDB; 6O5W; X-ray; 1.41 A; A=407-455.
DR PDBsum; 4QQ4; -.
DR PDBsum; 5SVI; -.
DR PDBsum; 5SVX; -.
DR PDBsum; 5SVY; -.
DR PDBsum; 6O1E; -.
DR PDBsum; 6O5W; -.
DR AlphaFoldDB; Q14149; -.
DR SMR; Q14149; -.
DR BioGRID; 117062; 41.
DR IntAct; Q14149; 20.
DR MINT; Q14149; -.
DR STRING; 9606.ENSP00000383333; -.
DR GlyGen; Q14149; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14149; -.
DR PhosphoSitePlus; Q14149; -.
DR BioMuta; MORC3; -.
DR DMDM; 108935853; -.
DR EPD; Q14149; -.
DR jPOST; Q14149; -.
DR MassIVE; Q14149; -.
DR MaxQB; Q14149; -.
DR PaxDb; Q14149; -.
DR PeptideAtlas; Q14149; -.
DR PRIDE; Q14149; -.
DR ProteomicsDB; 59852; -.
DR Antibodypedia; 5016; 94 antibodies from 23 providers.
DR DNASU; 23515; -.
DR Ensembl; ENST00000400485.6; ENSP00000383333.1; ENSG00000159256.13.
DR GeneID; 23515; -.
DR KEGG; hsa:23515; -.
DR MANE-Select; ENST00000400485.6; ENSP00000383333.1; NM_015358.3; NP_056173.1.
DR UCSC; uc002yvi.3; human.
DR CTD; 23515; -.
DR DisGeNET; 23515; -.
DR GeneCards; MORC3; -.
DR HGNC; HGNC:23572; MORC3.
DR HPA; ENSG00000159256; Low tissue specificity.
DR MIM; 610078; gene.
DR neXtProt; NX_Q14149; -.
DR OpenTargets; ENSG00000159256; -.
DR PharmGKB; PA128394632; -.
DR VEuPathDB; HostDB:ENSG00000159256; -.
DR eggNOG; KOG1845; Eukaryota.
DR GeneTree; ENSGT00940000160495; -.
DR HOGENOM; CLU_011516_2_0_1; -.
DR InParanoid; Q14149; -.
DR OMA; LTMIVPD; -.
DR OrthoDB; 193855at2759; -.
DR PhylomeDB; Q14149; -.
DR TreeFam; TF329118; -.
DR PathwayCommons; Q14149; -.
DR SignaLink; Q14149; -.
DR BioGRID-ORCS; 23515; 10 hits in 1078 CRISPR screens.
DR ChiTaRS; MORC3; human.
DR GeneWiki; MORC3; -.
DR GenomeRNAi; 23515; -.
DR Pharos; Q14149; Tbio.
DR PRO; PR:Q14149; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q14149; protein.
DR Bgee; ENSG00000159256; Expressed in calcaneal tendon and 196 other tissues.
DR ExpressionAtlas; Q14149; baseline and differential.
DR Genevisible; Q14149; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; IDA:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IDA:MGI.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IDA:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
DR GO; GO:2000774; P:positive regulation of cellular senescence; IDA:MGI.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0050821; P:protein stabilization; IDA:MGI.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR045261; MORC_ATPase.
DR InterPro; IPR041006; Morc_S5.
DR InterPro; IPR011124; Znf_CW.
DR PANTHER; PTHR23336; PTHR23336; 1.
DR Pfam; PF17942; Morc6_S5; 1.
DR Pfam; PF07496; zf-CW; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS51050; ZF_CW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Coiled coil; Host-virus interaction; Immunity;
KW Innate immunity; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..939
FT /note="MORC family CW-type zinc finger protein 3"
FT /id="PRO_0000096538"
FT ZN_FING 404..454
FT /note="CW-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT REGION 326..353
FT /note="Nuclear matrix binding"
FT /evidence="ECO:0000269|PubMed:11927593"
FT REGION 500..591
FT /note="RNA binding"
FT /evidence="ECO:0000269|PubMed:11927593"
FT REGION 524..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 686..877
FT /evidence="ECO:0000255"
FT COMPBIAS 618..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 231
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 280
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 293
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 555
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 597
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:20501696"
FT CROSSLNK 597
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 650
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:20501696"
FT CROSSLNK 650
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 651
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:20501696"
FT CROSSLNK 651
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 740
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:20501696"
FT CROSSLNK 740
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 794
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:20501696"
FT CROSSLNK 794
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 855
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 35
FT /note="E->A: Fails to localize to PML nuclear bodies and
FT activate TP53."
FT /evidence="ECO:0000269|PubMed:17332504"
FT MUTAGEN 67
FT /note="D->N: Forms nuclear bodies, but rapidly diffuses
FT throughout the nucleus under conditions of ATP depletion."
FT /evidence="ECO:0000269|PubMed:20501696"
FT MUTAGEN 101
FT /note="G->A: Diffuse nuclear localization. Fails to form
FT nuclear bodies in the presence of ATP."
FT /evidence="ECO:0000269|PubMed:20501696"
FT MUTAGEN 419
FT /note="W->A: About threefold increase in catalytic
FT activity."
FT /evidence="ECO:0000269|PubMed:30850548"
FT MUTAGEN 419
FT /note="W->A: Diffuse nuclear localization, possibly due to
FT loss of DNA or nucleosome binding."
FT /evidence="ECO:0000269|PubMed:20501696"
FT MUTAGEN 431
FT /note="E->A: Strong decrease of binding to NS1."
FT /evidence="ECO:0000269|PubMed:31006586"
FT MUTAGEN 597
FT /note="K->R: Loss of sumoylation; when associated with R-
FT 650; R-651; R-740 and R-794."
FT /evidence="ECO:0000269|PubMed:20501696"
FT MUTAGEN 650
FT /note="K->R: Loss of sumoylation; when associated with R-
FT 597; R-651; R-740 and R-794."
FT /evidence="ECO:0000269|PubMed:20501696"
FT MUTAGEN 651
FT /note="K->R: Loss of sumoylation; when associated with R-
FT 597; R-650; R-740 and R-794."
FT /evidence="ECO:0000269|PubMed:20501696"
FT MUTAGEN 740
FT /note="K->R: Loss of sumoylation; when associated with R-
FT 597; R-650; R-651 and R-794."
FT /evidence="ECO:0000269|PubMed:20501696"
FT MUTAGEN 794
FT /note="K->R: Loss of sumoylation; when associated with R-
FT 597; R-650; R-651 and R-740."
FT /evidence="ECO:0000269|PubMed:20501696"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:6O1E"
FT HELIX 29..41
FT /evidence="ECO:0007829|PDB:6O1E"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:6O1E"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:6O1E"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:6O1E"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:6O1E"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:6O1E"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:6O1E"
FT STRAND 112..123
FT /evidence="ECO:0007829|PDB:6O1E"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:6O1E"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:6O1E"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:6O1E"
FT HELIX 159..172
FT /evidence="ECO:0007829|PDB:6O1E"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:6O1E"
FT STRAND 190..201
FT /evidence="ECO:0007829|PDB:6O1E"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:6O1E"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:6O1E"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:6O1E"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:6O1E"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:6O1E"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:6O1E"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:6O1E"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:6O1E"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:6O1E"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:6O1E"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:6O1E"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:6O1E"
FT STRAND 343..348
FT /evidence="ECO:0007829|PDB:6O1E"
FT TURN 356..359
FT /evidence="ECO:0007829|PDB:6O1E"
FT HELIX 365..389
FT /evidence="ECO:0007829|PDB:6O1E"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:6O1E"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:6O1E"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:5SVY"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:5SVY"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:5SVY"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:5SVY"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:5SVY"
SQ SEQUENCE 939 AA; 107113 MW; 7DF0EC31936BF5FF CRC64;
MAAQPPRGIR LSALCPKFLH TNSTSHTWPF SAVAELIDNA YDPDVNAKQI WIDKTVINDH
ICLTFTDNGN GMTSDKLHKM LSFGFSDKVT MNGHVPVGLY GNGFKSGSMR LGKDAIVFTK
NGESMSVGLL SQTYLEVIKA EHVVVPIVAF NKHRQMINLA ESKASLAAIL EHSLFSTEQK
LLAELDAIIG KKGTRIIIWN LRSYKNATEF DFEKDKYDIR IPEDLDEITG KKGYKKQERM
DQIAPESDYS LRAYCSILYL KPRMQIILRG QKVKTQLVSK SLAYIERDVY RPKFLSKTVR
ITFGFNCRNK DHYGIMMYHR NRLIKAYEKV GCQLRANNMG VGVVGIIECN FLKPTHNKQD
FDYTNEYRLT ITALGEKLND YWNEMKVKKN TEYPLNLPVE DIQKRPDQTW VQCDACLKWR
KLPDGMDQLP EKWYCSNNPD PQFRNCEVPE EPEDEDLVHP TYEKTYKKTN KEKFRIRQPE
MIPRINAELL FRPTALSTPS FSSPKESVPR RHLSEGTNSY ATRLLNNHQV PPQSEPESNS
LKRRLSTRSS ILNAKNRRLS SQFENSVYKG DDDDEDVIIL EENSTPKPAV DHDIDMKSEQ
SHVEQGGVQV EFVGDSEPCG QTGSTSTSSS RCDQGNTAAT QTEVPSLVVK KEETVEDEID
VRNDAVILPS CVEAEAKIHE TQETTDKSAD DAGCQLQELR NQLLLVTEEK ENYKRQCHMF
TDQIKVLQQR ILEMNDKYVK KETCHQSTET DAVFLLESIN GKSESPDHMV SQYQQALEEI
ERLKKQCSAL QHVKAECSQC SNNESKSEMD EMAVQLDDVF RQLDKCSIER DQYKSEVELL
EMEKSQIRSQ CEELKTEVEQ LKSTNQQTAT DVSTSSNIEE SVNHMDGESL KLRSLRVNVG
QLLAMIVPDL DLQQVNYDVD VVDEILGQVV EQMSEISST
