MORC1_CAEEL
ID MORC1_CAEEL Reviewed; 845 AA.
AC Q23243;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=ATPase morc-1 {ECO:0000305};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:Q9Y6X9};
GN Name=morc-1 {ECO:0000312|WormBase:ZC155.3};
GN ORFNames=ZC155.3 {ECO:0000312|WormBase:ZC155.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22555433; DOI=10.1126/science.1221472;
RA Moissiard G., Cokus S.J., Cary J., Feng S., Billi A.C., Stroud H.,
RA Husmann D., Zhan Y., Lajoie B.R., McCord R.P., Hale C.J., Feng W.,
RA Michaels S.D., Frand A.R., Pellegrini M., Dekker J., Kim J.K.,
RA Jacobsen S.E.;
RT "MORC family ATPases required for heterochromatin condensation and gene
RT silencing.";
RL Science 336:1448-1451(2012).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLU-39.
RX PubMed=28535375; DOI=10.1016/j.devcel.2017.04.023;
RA Weiser N.E., Yang D.X., Feng S., Kalinava N., Brown K.C., Khanikar J.,
RA Freeberg M.A., Snyder M.J., Csankovszki G., Chan R.C., Gu S.G.,
RA Montgomery T.A., Jacobsen S.E., Kim J.K.;
RT "MORC-1 integrates nuclear RNAi and transgenerational chromatin
RT architecture to promote germline immortality.";
RL Dev. Cell 41:408-423(2017).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28533440; DOI=10.1534/genetics.116.198812;
RA Spracklin G., Fields B., Wan G., Vijayendran D., Wallig A., Shukla A.,
RA Kennedy S.;
RT "Identification and characterization of Caenorhabditis elegans RNAi
RT inheritance machinery.";
RL Genetics 206:1403-1416(2017).
RN [5]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=31442422; DOI=10.1016/j.molcel.2019.07.032;
RA Kim H., Yen L., Wongpalee S.P., Kirshner J.A., Mehta N., Xue Y.,
RA Johnston J.B., Burlingame A.L., Kim J.K., Loparo J.J., Jacobsen S.E.;
RT "The Gene-Silencing Protein MORC-1 Topologically Entraps DNA and Forms
RT Multimeric Assemblies to Cause DNA Compaction.";
RL Mol. Cell 75:700-710(2019).
CC -!- FUNCTION: Binds non-specifically to DNA and forms static foci which
CC grow by recruiting other morc-1 molecules, and thereby stimulates
CC conformational changes and compaction of DNA, which appears to be
CC enhanced by ATP-binding, but does not require ATP activity
CC (PubMed:31442422). Preferentially binds to long DNAs (PubMed:31442422).
CC Compacts and entraps segments of DNA by sequentially forming loops
CC along the DNA, beginning at the free ends of single- and double-
CC tethered DNA (PubMed:31442422). Does not extrude the DNA loops on
CC compacted double-tethered DNA (PubMed:31442422). Involved in gene
CC silencing (PubMed:22555433). Plays a role in germline RNA interference
CC (RNAi), and in particular, the silencing of endogenous small
CC interfering RNA (endo-siRNA) target genes (PubMed:28535375). May play a
CC role in heterochromatin localization and condensation, and the siRNAi-
CC directed trimethylation of 'Lys-9' of histone H3 in hermaphrodite X
CC chromosomes (PubMed:28535375). Promotes transgenerational epigenetic
CC inheritance and germline immortality (PubMed:28535375,
CC PubMed:28533440). {ECO:0000269|PubMed:22555433,
CC ECO:0000269|PubMed:28533440, ECO:0000269|PubMed:28535375,
CC ECO:0000269|PubMed:31442422}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6X9};
CC -!- SUBUNIT: Predominantly forms monomers and dimers, but multimerizes to
CC form trimers and tetramers upon DNA binding.
CC {ECO:0000269|PubMed:31442422}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28535375}. Nucleus,
CC nuclear body {ECO:0000269|PubMed:31442422}. Note=Localizes to punctate
CC nuclear bodies in germline stem cells and gonadal meiotic nuclei.
CC {ECO:0000269|PubMed:31442422}.
CC -!- TISSUE SPECIFICITY: Expressed in germline and somatic cells.
CC {ECO:0000269|PubMed:28535375}.
CC -!- DISRUPTION PHENOTYPE: Mortal germline (Mrt) phenotype in which there is
CC a progressive decline in fertility with each generation at 25 degrees
CC Celsius culminating in complete sterility after five to six generations
CC (PubMed:28535375, PubMed:28533440). Resistant to nuclear RNAi and
CC defective RNAi inheritance (PubMed:28535375). Reduced trimethylation of
CC 'Lys-9' of histone H3 at endogenous siRNA-directed targets, a small
CC degree of irregularly localized heterochromatin, with 70% correctly
CC localized, defective chromatin compaction in hermaphrodite X
CC chromosomes (PubMed:28535375). Double knockout with the histone
CC methyltransferase met-1 rescues the progressive germline mortality
CC defect in the morc-1 single mutant (PubMed:28535375). RNAi-mediated
CC knockdown results in defective gene silencing (PubMed:22555433).
CC {ECO:0000269|PubMed:22555433, ECO:0000269|PubMed:28533440,
CC ECO:0000269|PubMed:28535375}.
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DR EMBL; BX284603; CCD66674.1; -; Genomic_DNA.
DR RefSeq; NP_498104.1; NM_065703.5.
DR AlphaFoldDB; Q23243; -.
DR SMR; Q23243; -.
DR STRING; 6239.ZC155.3; -.
DR EPD; Q23243; -.
DR PaxDb; Q23243; -.
DR PeptideAtlas; Q23243; -.
DR EnsemblMetazoa; ZC155.3.1; ZC155.3.1; WBGene00022531.
DR GeneID; 175711; -.
DR KEGG; cel:CELE_ZC155.3; -.
DR UCSC; ZC155.3; c. elegans.
DR CTD; 175711; -.
DR WormBase; ZC155.3; CE23442; WBGene00022531; morc-1.
DR eggNOG; KOG1845; Eukaryota.
DR GeneTree; ENSGT00940000153998; -.
DR HOGENOM; CLU_337149_0_0_1; -.
DR InParanoid; Q23243; -.
DR OMA; SHTHIGP; -.
DR OrthoDB; 1399833at2759; -.
DR PhylomeDB; Q23243; -.
DR Reactome; R-CEL-75105; Fatty acyl-CoA biosynthesis.
DR PRO; PR:Q23243; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00022531; Expressed in adult organism and 4 other tissues.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061776; F:topological DNA co-entrapment activity; IDA:UniProtKB.
DR GO; GO:0006265; P:DNA topological change; IDA:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR SUPFAM; SSF55874; SSF55874; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW RNA-mediated gene silencing.
FT CHAIN 1..845
FT /note="ATPase morc-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000441621"
FT REGION 566..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 284..311
FT /evidence="ECO:0000255"
FT COMPBIAS 570..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT BINDING 88..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT BINDING 97..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT BINDING 422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT MUTAGEN 39
FT /note="E->A: Hypomorphic allele which is overexpressed
FT relative to wild-type. Progressive germline mortality,
FT resistant to nuclear RNAi and displays defective RNAi
FT inheritance."
FT /evidence="ECO:0000269|PubMed:28535375"
SQ SEQUENCE 845 AA; 95793 MW; 1896FCAE63D571EF CRC64;
MPNDTNGDDY KKLEKASVNL NFLKSNSHTH IGPLSAIAEL VDNAYDADAR DLHIDFLDIN
NEQFLELRDD GLGMAREEAL HAITFGHSAK CSYKIGRYGN GLKSGAFHLG RELLLVTKKD
GIITALLISH RFHEDQGLTN SVFVPCPSFD LDGIPICQTE SEKDRFNLEM KIIGKYAPLG
SRTLAELADK ITGSTGTIII IGNLRRSVTG ELAINTTKDP TDIIVDSGEE NKPWRESLRK
YLEFIYLKPR MRIHVRGEQV LPKRISENWI AKKQQLISGD QFTAAYNKIL DEKNETVKKC
EEEKALVMSE IGGTNYTSVR REDRANQKSL RLRVDTSQKN LDSAIADRDA FKKEGKSEKS
FHLNMGIETK DRSNNGIHFY INNRLILWGN KEAKFFSKFA NSIGISMFLS LDYSLFSAAQ
NKQGFDHVKD FQVLVRKCND ALRDYSMYLE KSWIPTHLKN TWNVRIYEGD DVWAVLWGVY
GYNNTTSTTC VQTHDSARDQ VMWTTCGIWK LCQMCRTWIK ASRPNEIVGS NDDFFCCENV
NHHGCRTIVA EDNDFSKLPE KYDHILPQKR LTNSAPSSSD SQNSIRSASS CSSSSRLLNV
AKIESHERIH SSTGGHRLGE SFSTTSVKME PIPNNAHDSH IAEVQRRHST GRAISPAVSE
ISRRAGTAPS SQLDMIMGEE SDESQEALTI RAPRQRAKRP IERVSRRNRR DQSDDDSDSE
NEERYATAPK KSKVKGKAVV RAPKMTREKW LEEMLNQFLT AHGEQPLPKN GQRDFDPTNI
VEQTSRRNFK NNQRIVDAQQ AIMRQIGSVL DHLKRNPTHN FKIPASGTVE EKLKNIEHQI
KGKKK
