MBD1_ARATH
ID MBD1_ARATH Reviewed; 204 AA.
AC Q5XEN5; O49655;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Methyl-CpG-binding domain-containing protein 1;
DE Short=AtMBD1;
DE Short=MBD01;
DE AltName: Full=Methyl-CpG-binding protein MBD1;
GN Name=MBD1; OrderedLocusNames=At4g22745; ORFNames=T12H17.130;
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=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;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP MAD MOTIF, 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 [5]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=15010609; DOI=10.1023/b:plan.0000019118.56822.a9;
RA Scebba F., Bernacchia G., De Bastiani M., Evangelista M., Cantoni R.M.,
RA Cella R., Locci M.T., Pitto L.;
RT "Arabidopsis MBD proteins show different binding specificities and nuclear
RT localization.";
RL Plant Mol. Biol. 53:715-731(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=14605234; DOI=10.1104/pp.103.026708;
RA Ito M., Koike A., Koizumi N., Sano H.;
RT "Methylated DNA-binding proteins from Arabidopsis.";
RL Plant Physiol. 133:1747-1754(2003).
RN [7]
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 [8]
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).
CC -!- FUNCTION: Probable transcriptional regulator. {ECO:0000250}.
CC -!- INTERACTION:
CC Q5XEN5; Q9CAV7: At3g04930; NbExp=3; IntAct=EBI-4445335, EBI-15198431;
CC Q5XEN5; O81793: At4g35610; NbExp=3; IntAct=EBI-4445335, EBI-15191765;
CC Q5XEN5; Q17TI5: BRX; NbExp=3; IntAct=EBI-4445335, EBI-4426649;
CC Q5XEN5; O81801: DAZ3; NbExp=3; IntAct=EBI-4445335, EBI-4447483;
CC Q5XEN5; P93830: IAA17; NbExp=7; IntAct=EBI-4445335, EBI-632243;
CC Q5XEN5; P49678: IAA2; NbExp=7; IntAct=EBI-4445335, EBI-632343;
CC Q5XEN5; Q9LJW5: MIF2; NbExp=4; IntAct=EBI-4445335, EBI-15191779;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14605234}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers and buds.
CC {ECO:0000269|PubMed:12954765, ECO:0000269|PubMed:15010609}.
CC -!- DOMAIN: The methyl-CpG-binding domain (MBD) functions both in binding
CC to methylated DNA and in protein interactions. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16559.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79229.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021635; CAA16559.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161557; CAB79229.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84648.1; -; Genomic_DNA.
DR EMBL; BT015931; AAV31161.1; -; mRNA.
DR EMBL; BT020548; AAW70394.1; -; mRNA.
DR PIR; T04569; T04569.
DR RefSeq; NP_567667.2; NM_118401.6.
DR AlphaFoldDB; Q5XEN5; -.
DR SMR; Q5XEN5; -.
DR BioGRID; 13660; 17.
DR IntAct; Q5XEN5; 17.
DR STRING; 3702.AT4G22745.1; -.
DR iPTMnet; Q5XEN5; -.
DR PaxDb; Q5XEN5; -.
DR PRIDE; Q5XEN5; -.
DR ProteomicsDB; 238361; -.
DR EnsemblPlants; AT4G22745.1; AT4G22745.1; AT4G22745.
DR GeneID; 828371; -.
DR Gramene; AT4G22745.1; AT4G22745.1; AT4G22745.
DR KEGG; ath:AT4G22745; -.
DR Araport; AT4G22745; -.
DR TAIR; locus:505006513; AT4G22745.
DR eggNOG; KOG4161; Eukaryota.
DR HOGENOM; CLU_109577_1_1_1; -.
DR InParanoid; Q5XEN5; -.
DR OMA; AVQCEKC; -.
DR OrthoDB; 986130at2759; -.
DR PhylomeDB; Q5XEN5; -.
DR PRO; PR:Q5XEN5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q5XEN5; baseline and differential.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008327; F:methyl-CpG binding; ISS:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR011124; Znf_CW.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF07496; zf-CW; 1.
DR SMART; SM00391; MBD; 1.
DR SUPFAM; SSF54171; SSF54171; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS51050; ZF_CW; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..204
FT /note="Methyl-CpG-binding domain-containing protein 1"
FT /id="PRO_0000405277"
FT DOMAIN 110..180
FT /note="MBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT ZN_FING 49..104
FT /note="CW-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 58..96
FT /note="MBD-associated domain (MAD)"
FT COMPBIAS 10..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
SQ SEQUENCE 204 AA; 23152 MW; E03DADF5CD15E284 CRC64;
MLPFPAMNLK KSRSENSSVA SSGSKIEEQT EKSAEPTTIK VQKKAGTPGR SIDVFAVQCE
KCMKWRKIDT QDEYEDIRSR VQEDPFFCKT KEGVSCEDVG DLNYDSSRTW VIDKPGLPRT
PRGFKRSLIL RKDYSKMDAY YITPTGKKLK SRNEIAAFID ANQDYKYALL GDFNFTVPKV
MEETVPSGIL SDRTPKPSRK VTID
