MORC6_ARATH
ID MORC6_ARATH Reviewed; 663 AA.
AC Q56Y74; Q9LMB8;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Protein MICRORCHIDIA 6 {ECO:0000303|PubMed:22555433};
DE Short=AtMORC6 {ECO:0000303|PubMed:22555433};
DE EC=3.6.-.- {ECO:0000269|PubMed:22560611};
DE AltName: Full=Protein CRT1-homolog 6 {ECO:0000303|PubMed:19704828};
DE Short=CRT1-h6 {ECO:0000303|PubMed:19704828};
DE AltName: Full=Protein DEFECTIVE IN MERISTEM SILENCING 11 {ECO:0000303|PubMed:22560611};
GN Name=MORC6 {ECO:0000303|PubMed:22555433};
GN Synonyms=CRH6 {ECO:0000303|PubMed:19704828},
GN DMS11 {ECO:0000303|PubMed:22560611};
GN OrderedLocusNames=At1g19100 {ECO:0000312|EMBL:AEE29802.1};
GN ORFNames=F14D16.25 {ECO:0000312|EMBL:AAF79293.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|EMBL:BAD94510.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19704828; DOI=10.4161/psb.3.9.5822;
RA Kang H.-G., Klessig D.F.;
RT "The involvement of the Arabidopsis CRT1 ATPase family in disease
RT resistance protein-mediated signaling.";
RL Plant Signal. Behav. 3:689-690(2008).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH DMS3, AND ACTIVITY
RP REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=22560611; DOI=10.1016/j.cub.2012.03.061;
RA Lorkovic Z.J., Naumann U., Matzke A.J., Matzke M.;
RT "Involvement of a GHKL ATPase in RNA-directed DNA methylation in
RT Arabidopsis thaliana.";
RL Curr. Biol. 22:933-938(2012).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=23675613; DOI=10.1111/tpj.12246;
RA Brabbs T.R., He Z., Hogg K., Kamenski A., Li Y., Paszkiewicz K.H.,
RA Moore K.A., O'Toole P., Graham I.A., Jones L.;
RT "The stochastic silencing phenotype of Arabidopsis morc6 mutants reveals a
RT role in efficient RNA-directed DNA methylation.";
RL Plant J. 75:836-846(2013).
RN [8]
RP SUBUNIT, INTERACTION WITH SUVH9; MORC1/CRT1 AND MORC2, AND
RP HOMODIMERIZATION.
RX PubMed=24465213; DOI=10.1371/journal.pgen.1003948;
RA Liu Z.-W., Shao C.-R., Zhang C.-J., Zhou J.-X., Zhang S.-W., Li L.,
RA Chen S., Huang H.-W., Cai T., He X.-J.;
RT "The SET domain proteins SUVH2 and SUVH9 are required for Pol V occupancy
RT at RNA-directed DNA methylation loci.";
RL PLoS Genet. 10:E1003948-E1003948(2014).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH MORC1/CRT1 AND MORC2, GENE
RP FAMILY, AND NOMENCLATURE.
RX PubMed=24799676; DOI=10.1073/pnas.1406611111;
RA Moissiard G., Bischof S., Husmann D., Pastor W.A., Hale C.J., Yen L.,
RA Stroud H., Papikian A., Vashisht A.A., Wohlschlegel J.A., Jacobsen S.E.;
RT "Transcriptional gene silencing by Arabidopsis microrchidia homologues
RT involves the formation of heteromers.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7474-7479(2014).
RN [10]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=27171361; DOI=10.1371/journal.pgen.1005998;
RA Harris C.J., Husmann D., Liu W., Kasmi F.E., Wang H., Papikian A.,
RA Pastor W.A., Moissiard G., Vashisht A.A., Dangl J.L., Wohlschlegel J.A.,
RA Jacobsen S.E.;
RT "Arabidopsis AtMORC4 and AtMORC7 form nuclear bodies and repress a large
RT number of protein-coding genes.";
RL PLoS Genet. 12:E1005998-E1005998(2016).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH IDN2; SWI3B; SWI3C AND
RP SWI3D.
RX PubMed=27171427; DOI=10.1371/journal.pgen.1006026;
RA Liu Z.-W., Zhou J.-X., Huang H.-W., Li Y.-Q., Shao C.-R., Li L., Cai T.,
RA Chen S., He X.-J.;
RT "Two components of the RNA-Directed DNA methylation pathway associate with
RT MORC6 and silence loci targeted by MORC6 in Arabidopsis.";
RL PLoS Genet. 12:E1006026-E1006026(2016).
CC -!- FUNCTION: Involved in RNA-directed DNA methylation (RdDM) as a
CC component of the RdDM machinery and required for gene silencing
CC (PubMed:22560611, PubMed:23675613, PubMed:27171427). Together with
CC SUVH2 and SUVH9, regulates the silencing of some transposable elements
CC (TEs) (PubMed:27171427). Exhibits ATPase activity (PubMed:22560611).
CC May also be involved in the regulation of chromatin
CC architecture/condensation to maintain gene silencing (PubMed:22555433,
CC PubMed:27171427). Binds DNA/RNA in a non-specific manner and exhibits
CC endonuclease activity. Probably involved in DNA repair (By similarity).
CC Positive regulator of defense against the oomycete Hyaloperonospora
CC arabidopsidis (Hpa) (PubMed:27171361). {ECO:0000250|UniProtKB:Q84WV6,
CC ECO:0000269|PubMed:22555433, ECO:0000269|PubMed:22560611,
CC ECO:0000269|PubMed:23675613, ECO:0000269|PubMed:27171361,
CC ECO:0000269|PubMed:27171427}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q84WV6};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q84WV6};
CC -!- ACTIVITY REGULATION: Stimulated by DMS3. {ECO:0000269|PubMed:22560611}.
CC -!- SUBUNIT: Homodimer and heterodimers with MORC1/CRT1 and MORC2
CC (PubMed:24465213, PubMed:24799676). Interacts directly with SUVH9
CC (PubMed:24465213). Component of an RNA-directed DNA methylation (RdDM)
CC complex that contains at least MORC6, MORC1/CRT1, MORC2, SWI3D and
CC SUVH9 (PubMed:24465213). Stimulated by interaction with DMS3
CC (PubMed:22560611). Interacts with IDN2, SWI3B, SWI3C and SWI3D
CC (PubMed:27171427). {ECO:0000269|PubMed:22560611,
CC ECO:0000269|PubMed:24465213, ECO:0000269|PubMed:24799676,
CC ECO:0000269|PubMed:27171427}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:22555433}. Note=Present in nuclear bodies near
CC chromocenters. {ECO:0000269|PubMed:22555433}.
CC -!- DISRUPTION PHENOTYPE: Accumulation of siRNAs and slight reductions of
CC repressive epigenetic modifications (e.g. decreases in DNA methylation
CC and H3K9me2 and increase in H3ac) at target sequences, especially in
CC the shoot apical meristem after rosette leaves development, leading to
CC derepression of silenced-genes (PubMed:22560611, PubMed:23675613).
CC Stochastic silencing phenotype due to randomized RNA-directed DNA
CC methylation (RdDM) (PubMed:23675613). Impaired gene silencing due to
CC decondensation of chromocenters leading to the derepression of DNA-
CC methylated genes and transposable elements (TEs); DNA and histone
CC methylation seems normal (PubMed:22555433, PubMed:24799676,
CC PubMed:27171427). {ECO:0000269|PubMed:22555433,
CC ECO:0000269|PubMed:22560611, ECO:0000269|PubMed:23675613,
CC ECO:0000269|PubMed:24799676, ECO:0000269|PubMed:27171427}.
CC -!- SIMILARITY: Belongs to the MORC ATPase protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79293.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC068602; AAF79293.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29802.1; -; Genomic_DNA.
DR EMBL; AK221449; BAD94510.1; -; mRNA.
DR PIR; D86324; D86324.
DR RefSeq; NP_173344.2; NM_101768.4.
DR AlphaFoldDB; Q56Y74; -.
DR SMR; Q56Y74; -.
DR STRING; 3702.AT1G19100.1; -.
DR iPTMnet; Q56Y74; -.
DR PaxDb; Q56Y74; -.
DR PRIDE; Q56Y74; -.
DR ProteomicsDB; 238301; -.
DR EnsemblPlants; AT1G19100.1; AT1G19100.1; AT1G19100.
DR GeneID; 838492; -.
DR Gramene; AT1G19100.1; AT1G19100.1; AT1G19100.
DR KEGG; ath:AT1G19100; -.
DR Araport; AT1G19100; -.
DR TAIR; locus:2011226; AT1G19100.
DR eggNOG; KOG1845; Eukaryota.
DR HOGENOM; CLU_011516_4_1_1; -.
DR InParanoid; Q56Y74; -.
DR OMA; GECLQYE; -.
DR OrthoDB; 378346at2759; -.
DR PhylomeDB; Q56Y74; -.
DR PRO; PR:Q56Y74; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q56Y74; baseline and differential.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0080188; P:gene silencing by RNA-directed DNA methylation; IMP:UniProtKB.
DR GO; GO:1902290; P:positive regulation of defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0060966; P:regulation of gene silencing by RNA; IMP:UniProtKB.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR045261; MORC_ATPase.
DR InterPro; IPR041006; Morc_S5.
DR PANTHER; PTHR23336; PTHR23336; 1.
DR Pfam; PF17942; Morc6_S5; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; Coiled coil; DNA damage; DNA repair;
KW DNA-binding; Endonuclease; Hydrolase; Nuclease; Nucleotide-binding;
KW Nucleus; Plant defense; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing.
FT CHAIN 1..663
FT /note="Protein MICRORCHIDIA 6"
FT /id="PRO_0000434981"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 614..659
FT /evidence="ECO:0000255"
FT MOTIF 552..559
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 24..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 74175 MW; 7C2E59E27411C941 CRC64;
MSHDRSVNVS HDAVIAKPER GTMLQSFSPR SHGSKGYSLP QDSEENRGSV GQSAGQSSTS
VVDQVRSPAD DAGVTSSSTI CPAPVCRQFW KAGSYNDELS SKSQQPNGKN YLHVHPMFLH
SNATSHKWAF GAVAELLDNA VDEIQNGATF VIVDKTTNPR DGATALLIQD DGGGMDPQAM
RHCMGFGFSD KKSDSAIGRY GNGFKTSTMR LGADVIVFSR HSKNQTLTQS IGLLSYTYLT
RTGHDRIVVP ILDYEFNASA GEFKTLQDRE HFISSLSILL EWSPFSTEAE LLQQFDDVGP
HGTKVIIYNM WLNSDAKLEL DFDSVAEDIL IEGSIKKTGS KIVNDHIASR FSYSLRVYLS
ILYLRIPETF KIILRGKVVE HHNVADDLMH PQYILYKPQA AGSEEALVVT TIGFLKEAPK
VNLHGFCVYH KNRLIMPFWQ VINYSSSRGR GVVGVLEANF VEPTHNKQDF EKTVLLQKLE
NRLKEMTVEY WSCHCVLIGY QVNKKPRLQI PQKVQPAGRQ ALSPPPGFQA VFPQGNTTSL
PRVSTQPVLL EKRKEHPDSV ASAALKRKVG NDDFTVPGHI RVEQFIHGSA SQSQDIETVK
LMEENKKLRA KCLDRKVRSQ NLEVKAMNLR SELENYKSEY ERLMVELQAL DLVKDEHRRN
VNT
