MBD9_ARATH
ID MBD9_ARATH Reviewed; 2176 AA.
AC Q9SGH2; Q9SSA6;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Methyl-CpG-binding domain-containing protein 9;
DE Short=AtMBD9;
DE Short=MBD09;
DE EC=2.3.1.48;
DE AltName: Full=Histone acetyl transferase MBD9;
DE AltName: Full=Methyl-CpG-binding protein MBD9;
GN Name=MBD9; OrderedLocusNames=At3g01460; ORFNames=F4P13.1, T13O15.10;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 ALTERNATIVE SPLICING, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12954765; DOI=10.1093/nar/gkg735;
RA Berg A., Meza T.J., Mahic M., Thorstensen T., Kristiansen K., Aalen R.B.;
RT "Ten members of the Arabidopsis gene family encoding methyl-CpG-binding
RT domain proteins are transcriptionally active and at least one, AtMBD11, is
RT crucial for normal development.";
RL Nucleic Acids Res. 31:5291-5304(2003).
RN [4]
RP GENE FAMILY.
RX PubMed=15888682; DOI=10.1104/pp.105.060566;
RA Springer N.M., Kaeppler S.M.;
RT "Evolutionary divergence of monocot and dicot methyl-CpG-binding domain
RT proteins.";
RL Plant Physiol. 138:92-104(2005).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16623890; DOI=10.1111/j.1365-313x.2006.02691.x;
RA Peng M., Cui Y., Bi Y.-M., Rothstein S.J.;
RT "AtMBD9: a protein with a methyl-CpG-binding domain regulates flowering
RT time and shoot branching in Arabidopsis.";
RL Plant J. 46:282-296(2006).
RN [6]
RP REVIEW.
RX PubMed=17208509; DOI=10.1016/j.tplants.2006.12.004;
RA Zemach A., Grafi G.;
RT "Methyl-CpG-binding domain proteins in plants: interpreters of DNA
RT methylation.";
RL Trends Plant Sci. 12:80-85(2007).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19419532; DOI=10.1111/j.1365-313x.2009.03860.x;
RA Yaish M.W.F., Peng M., Rothstein S.J.;
RT "AtMBD9 modulates Arabidopsis development through the dual epigenetic
RT pathways of DNA methylation and histone acetylation.";
RL Plant J. 59:123-135(2009).
CC -!- FUNCTION: Probable transcriptional regulator that acts as a histone
CC acetyltransferase. Mediates the acetylation of histone H3 and H4 of
CC target loci (e.g. FLC). Involved in an auxin-independent regulation of
CC shoot branching and flowering time. {ECO:0000269|PubMed:16623890,
CC ECO:0000269|PubMed:19419532}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC -!- SUBUNIT: Interacts with histone H4.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19419532}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SGH2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SGH2-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, buds, flowers and stems.
CC {ECO:0000269|PubMed:12954765, ECO:0000269|PubMed:19419532}.
CC -!- DOMAIN: The methyl-CpG-binding domain (MBD) functions both in binding
CC to methylated DNA and in protein interactions. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Over-methylated genomic DNA. Increased shoot
CC branching and reduced transcription of FLC leading to early flowering,
CC associated with a decrease in the acetylation level in histone H3 and
CC H4 of FLC chromatin. {ECO:0000269|PubMed:16623890,
CC ECO:0000269|PubMed:19419532}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF01531.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC009325; AAF01531.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC010870; AAF24616.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73669.1; -; Genomic_DNA.
DR RefSeq; NP_186795.1; NM_111012.4. [Q9SGH2-1]
DR AlphaFoldDB; Q9SGH2; -.
DR SMR; Q9SGH2; -.
DR BioGRID; 6465; 3.
DR STRING; 3702.AT3G01460.1; -.
DR iPTMnet; Q9SGH2; -.
DR PaxDb; Q9SGH2; -.
DR PRIDE; Q9SGH2; -.
DR ProteomicsDB; 238318; -. [Q9SGH2-1]
DR EnsemblPlants; AT3G01460.1; AT3G01460.1; AT3G01460. [Q9SGH2-1]
DR GeneID; 821132; -.
DR Gramene; AT3G01460.1; AT3G01460.1; AT3G01460. [Q9SGH2-1]
DR KEGG; ath:AT3G01460; -.
DR Araport; AT3G01460; -.
DR TAIR; locus:2096672; AT3G01460.
DR eggNOG; ENOG502QW8S; Eukaryota.
DR HOGENOM; CLU_234476_0_0_1; -.
DR InParanoid; Q9SGH2; -.
DR OMA; FEDFFVL; -.
DR PhylomeDB; Q9SGH2; -.
DR PRO; PR:Q9SGH2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SGH2; baseline and differential.
DR Genevisible; Q9SGH2; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0000812; C:Swr1 complex; IDA:TAIR.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008327; F:methyl-CpG binding; ISS:TAIR.
DR GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IMP:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IMP:UniProtKB.
DR GO; GO:0048573; P:photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0010223; P:secondary shoot formation; IMP:TAIR.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF05965; FYRC; 1.
DR Pfam; PF05964; FYRN; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF15612; WHIM1; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF54171; SSF54171; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Bromodomain; Coiled coil; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..2176
FT /note="Methyl-CpG-binding domain-containing protein 9"
FT /id="PRO_0000405285"
FT DOMAIN 258..327
FT /note="MBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT DOMAIN 403..456
FT /note="FYR N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00875"
FT DOMAIN 550..698
FT /note="FYR C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00876"
FT REPEAT 1098..1137
FT /note="Pumilio"
FT DOMAIN 1157..1228
FT /note="Bromo"
FT ZN_FING 83..133
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 86..131
FT /note="RING-type 1; degenerate"
FT ZN_FING 1287..1337
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1290..1335
FT /note="RING-type 2; degenerate"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 28..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1472..1553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1565..1595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2136..2176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 491..511
FT /evidence="ECO:0000255"
FT COILED 1251..1273
FT /evidence="ECO:0000255"
FT COILED 1410..1437
FT /evidence="ECO:0000255"
FT COILED 1588..1628
FT /evidence="ECO:0000255"
FT MOTIF 914..921
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 1124..1131
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 1256..1263
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 1337..1344
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 1761..1768
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1487..1532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2158..2176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2176 AA; 240431 MW; 05DBD955D895C3D5 CRC64;
MEPTDSTNEQ LGDTKTAAVK EESRSFLGID LNEIPTGATL GGGCTAGQDD DGEYEPVEVV
RSIHDNPDPA PGAPAEVPEP DRDASCGACG RPESIELVVV CDACERGFHM SCVNDGVEAA
PSADWMCSDC RTGGERSKLW PLGVKSKLIL DMNASPPSDA EGYGAEETSD SRKHMLASSS
CIGNSFDYAM MHSSFSSLGR GHASLEASGL MSRNTKMSMD ALGSHNLGFG FPLNLNNSSL
PMRFPSLDPS ELFLQNLRHF ISERHGVLED GWRVEFRQPL NGYQLCAVYC APNGKTFSSI
QEVACYLGLA INGNYSCMDA EIRNENSLLQ ERLHTPKRRK TSRWPNNGFP EQKGSSVSAQ
LRRFPFNGQT MSPFAVKSGT HFQAGGSLSS GNNGCGCEEA KNGCPMQFED FFVLSLGRID
IRQSYHNVNV IYPIGYKSCW HDKITGSLFT CEVSDGNSGP IFKVTRSPCS KSFIPAGSTV
FSCPKIDEMV EQNSDKLSNR RDSTQERDDD ASVEILLSEH CPPLGDDILS CLREKSFSKT
VNSLRSEVDS SRVDFDKNLS YDQDHGVEIG DIVVEEDSLS DAWKKVSQKL VDACSIVLKQ
KGTLNFLCKH VDRETSEINW DTMNEKDNVI LSLSKFCCSL APCSVTCGEK DKSEFAAVVD
ALSRWLDQNR FGLDADFVQE MIEHMPGAES CTNYRTLKSR SSSSVPITVA EGALVVKPKG
GENVKDEVFG EISRKAKKPK LNGGHGVRNL HPPPGRPMCL RLPPGLVGDF LQVSEVFWRF
HEILGFEEAF SPENLEQELI NPVFDGLFLD KPGKDDKRSE INFTDKDSTA TKLFSLFDES
RQPFPAKNTS ASELKEKKAG DSSDFKISDS SRGSCVGALL TRAHISLLQV LICELQSKVA
AFVDPNFDSG ESRSRRGRKK DDSTLSAKRN KLHMLPVNEF TWPELARRYI LSLLSMDGNL
ESAEIAARES GKVFRCLQGD GGLLCGSLTG VAGMEADSML LAEAIKKISG SLTSENDVLS
VEDDDSDGLD ATETNTCSGD IPEWAQVLEP VKKLPTNVGT RIRKCVYEAL ERNPPEWAKK
ILEHSISKEI YKGNASGPTK KAVLSLLADI RGGDLVQRSI KGTKKRTYIS VSDVIMKKCR
AVLRGVAAAD EDKVLCTLLG RKLLNSSDND DDGLLGSPAM VSRPLDFRTI DLRLAAGAYD
GSTEAFLEDV LELWSSIRVM YADQPDCVDL VATLSEKFKS LYEAEVVPLV QKLKDYRKLE
CLSAEMKKEI KDIVVSVNKL PKAPWDEGVC KVCGVDKDDD SVLLCDTCDA EYHTYCLNPP
LIRIPDGNWY CPSCVIAKRM AQEALESYKL VRRRKGRKYQ GELTRASMEL TAHLADVMEE
KDYWEFSAEE RILLLKLLCD ELLSSSLVHQ HLEQCAEAII EMQQKLRSLS SEWKNAKMRQ
EFLTAKLAKV EPSILKEVGE PHNSSYFADQ MGCDPQPQEG VGDGVTRDDE TSSTAYLNKN
QGKSPLETDT QPGESHVNFG ESKISSPETI SSPGRHELPI ADTSPLVTDN LPEKDTSETL
LKSVGRNHET HSPNSNAVEL PTAHDASSQA SQELQACQQD LSATSNEIQN LQQSIRSIES
QLLKQSIRRD FLGTDASGRL YWGCCFPDEN PRILVDGSIS LQKPVQADLI GSKVPSPFLH
TVDHGRLRLS PWTYYETETE ISELVQWLHD DDLKERDLRE SILWWKRLRY GDVQKEKKQA
QNLSAPVFAT GLETKAAMSM EKRYGPCIKL EMETLKKRGK KTKVAEREKL CRCECLESIL
PSMIHCLICH KTFASDDEFE DHTESKCIPY SLATEEGKDI SDSSKAKESL KSDYLNVKSS
AGKDVAEISN VSELDSGLIR YQEEESISPY HFEEICSKFV TKDCNRDLVK EIGLISSNGI
PTFLPSSSTH LNDSVLISAK SNKPDGGDSG DQVIFAGPET NVEGLNSESN MSFDRSVTDS
HGGPLDKPSG LGFGFSEQKN KKSSGSGLKS CCVVPQAALK RVTGKALPGF RFLKTNLLDM
DVALPEEALR PSKSHPNRRR AWRVFVKSSQ SIYELVQATI VVEDMIKTEY LKNEWWYWSS
LSAAAKISTL SALSVRIFSL DAAIIYDKPI TPSNPIDETK PIISLPDQKS QPVSDSQERS
SRVRRSGKKR KEPEGS
