MORC2_ARATH
ID MORC2_ARATH Reviewed; 626 AA.
AC Q5FV35; O65519; Q84WN9;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein MICRORCHIDIA 2 {ECO:0000303|PubMed:24799676};
DE Short=AtMORC2 {ECO:0000303|PubMed:24799676};
DE EC=3.6.-.-;
DE AltName: Full=Protein CRT1-homolog 1 {ECO:0000303|PubMed:19704828};
DE Short=CRT1-h1 {ECO:0000303|PubMed:19704828};
GN Name=MORC2 {ECO:0000303|PubMed:19704828};
GN Synonyms=CRH1 {ECO:0000303|PubMed:24799676};
GN OrderedLocusNames=At4g36280 {ECO:0000312|Araport:AT4G36280};
GN ORFNames=F23E13.170 {ECO:0000312|EMBL:CAA18134.1};
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:AAW70385.1};
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.
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, 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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20332379; DOI=10.1105/tpc.109.071662;
RA Kang H.-G., Oh C.-S., Sato M., Katagiri F., Glazebrook J., Takahashi H.,
RA Kachroo P., Martin G.B., Klessig D.F.;
RT "Endosome-associated CRT1 functions early in resistance gene-mediated
RT defense signaling in Arabidopsis and tobacco.";
RL Plant Cell 22:918-936(2010).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23250427; DOI=10.1038/ncomms2279;
RA Kang H.-G., Hyong W.C., von Einem S., Manosalva P., Ehlers K., Liu P.-P.,
RA Buxa S.V., Moreau M., Mang H.-G., Kachroo P., Kogel K.-H., Klessig D.F.;
RT "CRT1 is a nuclear-translocated MORC endonuclease that participates in
RT multiple levels of plant immunity.";
RL Nat. Commun. 3:1297-1297(2012).
RN [8]
RP SUBUNIT, AND INTERACTION WITH MORC6 AND SUVH9.
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 MORC6, GENE FAMILY, AND
RP 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: Mediator of defense signaling triggered by distinct classes
CC of R proteins. Required during hypersensitive response (HR) that
CC confers disease resistance to turnip crinkle virus (TCV)
CC (PubMed:19704828). Contributes to resistance against Pseudomonas
CC syringae and Hyaloperonospora arabidopsidis, at early stages prior to
CC cytosolic calcium ions Ca(2+) accumulation (PubMed:20332379). Required
CC for pathogen-associated molecular pattern (PAMP)-triggered immunity,
CC basal resistance, non-host resistance and systemic acquired resistance
CC (SAR) (PubMed:23250427). Involved in RNA-directed DNA methylation
CC (RdDM) as a component of the RdDM machinery and required for gene
CC silencing. May also be involved in the regulation of chromatin
CC architecture to maintain gene silencing (PubMed:24799676). Exhibits
CC ATPase activity (By similarity). {ECO:0000250|UniProtKB:Q56Y74,
CC ECO:0000269|PubMed:19704828, ECO:0000269|PubMed:20332379,
CC ECO:0000269|PubMed:23250427, ECO:0000269|PubMed:24799676}.
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 with MORC6. Component of an RNA-
CC directed DNA methylation (RdDM) complex that contains at least MORC6,
CC MORC1/CRT1, MORC2, SWI3D and SUVH9. Binds directly to SUVH9.
CC {ECO:0000269|PubMed:24465213, ECO:0000269|PubMed:24799676}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q84WV6,
CC ECO:0000255|PROSITE-ProRule:PRU00768}. Endosome
CC {ECO:0000250|UniProtKB:Q84WV6}. Note=Present in nuclear bodies near
CC chromocenters. Localized in endosome-like vesicles displaying rapid
CC cytosolic streaming. Accumulates in the nucleus following pathogen-
CC associated molecular pattern (PAMP) treatment or infection with an
CC avirulent pathogen. {ECO:0000250|UniProtKB:Q84WV6}.
CC -!- DISRUPTION PHENOTYPE: In the double mutant crt1-2 crh1-1, compromised
CC resistance to avirulent Pseudomonas syringae and Hyaloperonospora
CC arabidopsidis associated with compromised cytosolic calcium
CC accumulation upon infection (PubMed:20332379, PubMed:24799676). The
CC double mutant crt1-2 crh1-1 exhibits also an increased sensitivity to
CC turnip crinkle virus (TCV), and reduced defense response mediated by
CC flg22 against Pseudomonas syringae (Pst). Impaired non-host resistance
CC toward Phytophthora infestans and altered systemic acquired resistance
CC (SAR) triggered by P. syringae pv. maculicola (Psm) AvrRpt2 cor(-)
CC (PubMed:23250427). {ECO:0000269|PubMed:20332379,
CC ECO:0000269|PubMed:23250427, ECO:0000269|PubMed:24799676}.
CC -!- SIMILARITY: Belongs to the MORC ATPase protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18134.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80299.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022141; CAA18134.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161589; CAB80299.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86643.1; -; Genomic_DNA.
DR EMBL; BT002955; AAO22768.1; -; mRNA.
DR EMBL; BT020539; AAW70385.1; -; mRNA.
DR PIR; T04597; T04597.
DR RefSeq; NP_195351.2; NM_119796.4.
DR AlphaFoldDB; Q5FV35; -.
DR SMR; Q5FV35; -.
DR STRING; 3702.AT4G36280.1; -.
DR PaxDb; Q5FV35; -.
DR PRIDE; Q5FV35; -.
DR ProteomicsDB; 238307; -.
DR EnsemblPlants; AT4G36280.1; AT4G36280.1; AT4G36280.
DR GeneID; 829785; -.
DR Gramene; AT4G36280.1; AT4G36280.1; AT4G36280.
DR KEGG; ath:AT4G36280; -.
DR Araport; AT4G36280; -.
DR TAIR; locus:2122254; AT4G36280.
DR eggNOG; KOG1845; Eukaryota.
DR HOGENOM; CLU_011516_4_1_1; -.
DR InParanoid; Q5FV35; -.
DR OMA; FEDVGTH; -.
DR OrthoDB; 378346at2759; -.
DR PhylomeDB; Q5FV35; -.
DR PRO; PR:Q5FV35; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q5FV35; baseline and differential.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:UniProtKB.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:1901672; P:positive regulation of systemic acquired resistance; IMP:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; 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 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; Coiled coil; DNA damage; DNA repair;
KW DNA-binding; Endonuclease; Endosome; Hydrolase; Hypersensitive response;
KW Kinase; Nuclease; Nucleotide-binding; Nucleus; Plant defense;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing; Transferase.
FT CHAIN 1..626
FT /note="Protein MICRORCHIDIA 2"
FT /id="PRO_0000434977"
FT COILED 579..626
FT /evidence="ECO:0000255"
FT CONFLICT 233
FT /note="S -> C (in Ref. 3; AAO22768)"
FT /evidence="ECO:0000305"
FT CONFLICT 580
FT /note="R -> K (in Ref. 3; AAO22768)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 626 AA; 69977 MW; 367B734F8944FC68 CRC64;
MPPMAKNAAV TDVVHLDSDS DSDNGVVGGR ESASTIAGAA TMAPRETLEC RSFWKAGDYF
VIPNVVTPTA PGMLEHARVH PRFLHSNATS HKWAFGAIAE LLDNAVDEIQ NGATFVKIDK
INIVKDNSPA LVFQDDGGGM DPAGLRKCMS LGYSSKKSNT TIGQYGNGFK TSTMRLGADA
IVFSRSTRGG TSTQSVGILS YTFLRKTGQD DVTVPMIDID ISKERPQPII YGSPEDWAAN
LEILLKWSPF STEDELLQQF EDVGTHGTKV IIYNLWLNDE GIYELSFDDD EEDIRLRDES
VNDGKRLHHK ILELRSHISY HLRYSLRAYA SMLYLKKFKN FKIIIRGIPV EQFNIADGFR
FPEIIKYKPH TATTEQASTE IKIGFVKEAP KLAICGFNVY HKNRLIRPFW KVTMGGDSTG
HGVVGVLEAN FIEPAHDKQD FERSSLFQRL EARLKKIVYS YWYSHCHLLG YHKYQMPADK
SKKIAIPDQP PTISTVNPSP LPSDKISQGG PIIREINLSN ATSSRTVAFA SPHLRNSTGL
RSNFQPVQLN PQPTAADTGN NLDGKSAGEI RQENLQLFMR CEEYIKKENE TEQTVKSLEK
ELEEFKSKCA HLALLVDAKK KEMQQA
