MORC4_ARATH
ID MORC4_ARATH Reviewed; 800 AA.
AC F4KAF2; Q9FGW3;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Protein MICRORCHIDIA 4 {ECO:0000303|PubMed:24799676};
DE Short=AtMORC4 {ECO:0000303|PubMed:24799676};
DE EC=3.6.-.-;
DE AltName: Full=Protein CRT1-homolog 4 {ECO:0000303|PubMed:19704828};
DE Short=CRT1-h4 {ECO:0000303|PubMed:19704828};
GN Name=MORC4 {ECO:0000303|PubMed:24799676};
GN Synonyms=CRH4 {ECO:0000303|PubMed:19704828};
GN OrderedLocusNames=At5g50780 {ECO:0000312|Araport:AT5G50780};
GN ORFNames=MFB16.18 {ECO:0000312|EMBL:BAA96991.2};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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 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 [4]
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).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, AND SUBCELLULAR LOCATION.
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).
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. Together with MORC7, acts to suppress a wide set of non-
CC methylated protein-coding genes, especially involved in pathogen
CC response. Positive regulator of defense against the oomycete
CC Hyaloperonospora arabidopsidis (Hpa) (PubMed:27171361).
CC {ECO:0000250|UniProtKB:Q84WV6, ECO:0000269|PubMed:27171361}.
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. Forms homomeric complexes
CC (PubMed:27171361). {ECO:0000250|UniProtKB:Q84WV6,
CC ECO:0000269|PubMed:27171361}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:27171361}. Note=Accumulates in discrete nuclear
CC bodies adjacent to chromocenters. {ECO:0000269|PubMed:27171361}.
CC -!- DISRUPTION PHENOTYPE: The double mutant atmorc4 atmorc7 exhibits a
CC pathogen response phenotype with abnormal up-regulation of several
CC genes involved in plant defense. {ECO:0000269|PubMed:27171361}.
CC -!- SIMILARITY: Belongs to the MORC ATPase protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AED95991.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA96991.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB023037; BAA96991.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95991.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_199891.4; NM_124456.4.
DR AlphaFoldDB; F4KAF2; -.
DR SMR; F4KAF2; -.
DR STRING; 3702.AT5G50780.1; -.
DR PaxDb; F4KAF2; -.
DR PRIDE; F4KAF2; -.
DR GeneID; 835150; -.
DR KEGG; ath:AT5G50780; -.
DR Araport; AT5G50780; -.
DR TAIR; locus:2163320; AT5G50780.
DR eggNOG; KOG1845; Eukaryota.
DR HOGENOM; CLU_011516_6_0_1; -.
DR InParanoid; F4KAF2; -.
DR OrthoDB; 144359at2759; -.
DR PRO; PR:F4KAF2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KAF2; baseline and differential.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:TAIR.
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:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1902290; P:positive regulation of defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0044030; P:regulation of DNA methylation; IMP:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; Coiled coil; DNA damage; DNA repair;
KW DNA-binding; Endonuclease; Hydrolase; Kinase; Nuclease; Nucleotide-binding;
KW Nucleus; Plant defense; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Transferase.
FT CHAIN 1..800
FT /note="Protein MICRORCHIDIA 4"
FT /id="PRO_0000434979"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 699..766
FT /evidence="ECO:0000255"
FT MOTIF 716..723
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 735..742
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 7..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 800 AA; 89695 MW; 7C608C2C20805922 CRC64;
MEPIVKQENP VTTSTLSTWK PAARNKTIPP PESVIELSSS NEGSELGENL DEIAEIQSVD
RTGGDDVSGT KRARSDSIAS PAKRLAVMIP DDDEEFLLST TSGQAILALP ATPCNVVAAP
SSWGSCKQFW KAGDYEGTSG GDWEVSAGGF DHVRVHPKFL HSNATSHKWS LGAFAELLDN
ALDEVRSGAT FVNVDMIQNR KDGSKMILIE DNGGGMNPEK MRHCMSLGYS AKSKLADTIG
QYGNGFKTST MRLGADVIVF SRCLGKDGKS STQSIGLLSY TFLKSTGKED IVVPMLDYER
RDSEWCPITR SSVSDWEKNV ETVVQWSPYA TEEELLCQFN LMKKHGTRII IYNLWEDDEG
MLELDFDTDP HDIQLRGVNR DDKNIVMASQ FPNSRHYLTY KHSLRSYASI LYLKISHEFR
IILRGKDVEH HNIVNDMMQT EKITYRPKEA ADVSQLSAVV TIGFVKDAKH HVDVQGFNVY
HKNRLIKPFW RIWNAAGSDG RGVIGVLEAN FVEPAHDKQG FERTTVLSRL EARLLHMQKD
YWRSKCHKIG YAKRQGRKSA KDTEKDTEDR ESSPEFDPKG SASSRKRTVP SSFKTPTAAP
RFNTPTAASE KFNPRSNVNG GGKGSVKVSK DIGYKSSEKG GKLGNSFSKS NKRAKPQGAR
AVEVTNSDDD YDCDSSPERN VTELPGKSSE LPKPQSGPRT LSQLEQENNE LRERLDKKEE
VFLLLQKDLR RERELRKTLE AEVETLKNKL KEMDKEQASL IDVFAEDRDR RDKEEENLRI
KLEEASNTIQ KLIDGKARGR
