MORC3_ARATH
ID MORC3_ARATH Reviewed; 589 AA.
AC F4JPP0; O65518;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 2.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Protein MICRORCHIDIA 3 {ECO:0000303|PubMed:24799676};
DE Short=AtMORC3 {ECO:0000303|PubMed:24799676};
DE EC=3.6.-.-;
DE AltName: Full=Protein CRT1-homolog 2 {ECO:0000303|PubMed:19704828};
DE Short=CRT1-h2 {ECO:0000303|PubMed:18191794};
GN Name=MORC3 {ECO:0000303|PubMed:24799676};
GN Synonyms=CRH2 {ECO:0000303|PubMed:19704828};
GN OrderedLocusNames=At4g36270 {ECO:0000312|Araport:AT4G36270};
GN ORFNames=F23E13.160 {ECO:0000312|EMBL:CAA18133.1};
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|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION.
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 DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18191794; DOI=10.1016/j.chom.2007.11.006;
RA Kang H.-G., Kuhl J.C., Kachroo P., Klessig D.F.;
RT "CRT1, an Arabidopsis ATPase that interacts with diverse resistance
RT proteins and modulates disease resistance to turnip crinkle virus.";
RL Cell Host Microbe 3:48-57(2008).
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 GENE 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).
CC -!- FUNCTION: Exhibits ATPase activity. Binds DNA/RNA in a non-specific
CC manner and exhibits endonuclease activity. Probably involved in DNA
CC repair. Involved in RNA-directed DNA methylation (RdDM) as a component
CC of the RdDM machinery and required for gene silencing. May also be
CC involved in the regulation of chromatin architecture to maintain gene
CC silencing. {ECO:0000250|UniProtKB:Q84WV6}.
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 -!- SUBUNIT: Homodimer and heterodimer. Component of an RNA-directed DNA
CC methylation (RdDM) complex. {ECO:0000250|UniProtKB:Q84WV6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q56Y74,
CC ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- DISRUPTION PHENOTYPE: Likely lethal, leading to seeds abortion.
CC {ECO:0000269|PubMed:18191794}.
CC -!- SIMILARITY: Belongs to the MORC ATPase protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE86642.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA18133.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80298.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022141; CAA18133.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161589; CAB80298.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86642.1; ALT_SEQ; Genomic_DNA.
DR PIR; T04596; T04596.
DR RefSeq; NP_195350.5; NM_119795.5.
DR AlphaFoldDB; F4JPP0; -.
DR SMR; F4JPP0; -.
DR PeptideAtlas; F4JPP0; -.
DR PRIDE; F4JPP0; -.
DR GeneID; 829784; -.
DR KEGG; ath:AT4G36270; -.
DR Araport; AT4G36270; -.
DR TAIR; locus:2122244; AT4G36270.
DR HOGENOM; CLU_011516_4_1_1; -.
DR InParanoid; F4JPP0; -.
DR OrthoDB; 378346at2759; -.
DR PRO; PR:F4JPP0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JPP0; baseline and differential.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0031349; P:positive regulation of defense response; IEA:UniProt.
DR GO; GO:0002833; P:positive regulation of response to biotic stimulus; IEA:UniProt.
DR GO; GO:0032103; P:positive regulation of response to external stimulus; IEA:UniProt.
DR GO; GO:0006282; P:regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0060966; P:regulation of gene silencing by RNA; ISS: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 3: Inferred from homology;
KW ATP-binding; Chromatin regulator; Coiled coil; DNA damage; DNA repair;
KW DNA-binding; Endonuclease; Hydrolase; Nuclease; Nucleotide-binding;
KW Nucleus; Reference proteome; RNA-binding; RNA-mediated gene silencing.
FT CHAIN 1..589
FT /note="Protein MICRORCHIDIA 3"
FT /id="PRO_0000434978"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 542..589
FT /evidence="ECO:0000255"
SQ SEQUENCE 589 AA; 65939 MW; D6BB9529FAAC2EF0 CRC64;
MAPESKNAGV SVVVNLDSDS DSDNDDGVGG RGAFRSMASL MDKHQVPSTT ADATVAPREN
LECRSFWKAG ENFVIPTGVT NPAAPAIAEL IDNAVDEIQN GATFVKIDKI NIVKDNSPAL
VFQDDGGGMD PDGLRKCMSL GYSSKKSNTT IGQYGNGFKT STMRLGADDI VFTRSTRGGK
STQSVGLLSY TFLRKTGQDD VVVPMIDIDT SKERPQPIIY GSAEDWAASL EIILKWSPFS
TEGELWQQLE DIGTHGTKVI IYNLWLNDEG IYELSFHDDN EDIRLRDESV HDSKRVHHNL
LELRSHISYH LRYSLRAYAS MLYLKRFNNF KIILRGIPVE QFNIADELRL PETIKYNPHT
TKEKAPTEIK VGFIKEAPKL AVCGFNVYHK NRLIRPFWKV TMGGERRGSG VVGVLEANFI
EPAHDKQDFE RSSLFQRLEA RLKKIVSNYW NTHCHVFGYC TYGMPADKSK RIAIPDQPPT
VNTFNPLPLP SDEIRVSQGG PIIREISLSN ATSSRIAAVD TENNLVGKSA HEISEENIQL
FMRCEEYVKK ETELEQTVSN LAKELEETKS KCARLALLVD AKRREMQQV
