MBD11_ARATH
ID MBD11_ARATH Reviewed; 254 AA.
AC Q9LW00; Q0WUS8;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Methyl-CpG-binding domain-containing protein 11;
DE Short=AtMBD11;
DE Short=MBD11;
DE AltName: Full=Methyl-CpG-binding protein MBD11;
GN Name=MBD11; OrderedLocusNames=At3g15790; ORFNames=MSJ11.19;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP 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 [6]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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 [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).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Transcriptional regulator that binds DNA independently of its
CC methylation status. Required during plant organogenesis and
CC development. {ECO:0000269|PubMed:12954765,
CC ECO:0000269|PubMed:15010609}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12954765,
CC ECO:0000269|PubMed:15010609}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves (around hydathodes), buds,
CC flowers (carpels and pollen grains), stems (around nodes), siliques,
CC mature seeds and roots. {ECO:0000269|PubMed:12954765,
CC 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 -!- DISRUPTION PHENOTYPE: Variety of phenotypic effects, including aerial
CC rosettes, serrated leaves, abnormal position of flowers, fertility
CC problems and late flowering. {ECO:0000269|PubMed:12954765}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE99120.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB017071; BAB02310.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75727.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64124.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64125.1; -; Genomic_DNA.
DR EMBL; AK227060; BAE99120.1; ALT_FRAME; mRNA.
DR EMBL; BT015051; AAT71923.1; -; mRNA.
DR EMBL; BT033124; ACF22900.1; -; mRNA.
DR RefSeq; NP_001319562.1; NM_001338188.1.
DR RefSeq; NP_001326173.1; NM_001338189.1.
DR RefSeq; NP_188200.1; NM_112449.6.
DR PDB; 6ACV; NMR; -; A=4-74.
DR PDBsum; 6ACV; -.
DR AlphaFoldDB; Q9LW00; -.
DR SMR; Q9LW00; -.
DR BioGRID; 6156; 6.
DR IntAct; Q9LW00; 4.
DR STRING; 3702.AT3G15790.1; -.
DR iPTMnet; Q9LW00; -.
DR PaxDb; Q9LW00; -.
DR PRIDE; Q9LW00; -.
DR ProteomicsDB; 238846; -.
DR EnsemblPlants; AT3G15790.1; AT3G15790.1; AT3G15790.
DR EnsemblPlants; AT3G15790.2; AT3G15790.2; AT3G15790.
DR EnsemblPlants; AT3G15790.3; AT3G15790.3; AT3G15790.
DR GeneID; 820822; -.
DR Gramene; AT3G15790.1; AT3G15790.1; AT3G15790.
DR Gramene; AT3G15790.2; AT3G15790.2; AT3G15790.
DR Gramene; AT3G15790.3; AT3G15790.3; AT3G15790.
DR KEGG; ath:AT3G15790; -.
DR Araport; AT3G15790; -.
DR TAIR; locus:2093197; AT3G15790.
DR eggNOG; ENOG502RYIM; Eukaryota.
DR HOGENOM; CLU_051759_0_1_1; -.
DR InParanoid; Q9LW00; -.
DR OMA; EENSHVK; -.
DR OrthoDB; 992644at2759; -.
DR PhylomeDB; Q9LW00; -.
DR PRO; PR:Q9LW00; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LW00; baseline and differential.
DR Genevisible; Q9LW00; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008327; F:methyl-CpG binding; ISS:TAIR.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR039622; MBD10/11.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR PANTHER; PTHR33729; PTHR33729; 1.
DR Pfam; PF01429; MBD; 1.
DR SUPFAM; SSF54171; SSF54171; 1.
DR PROSITE; PS50982; MBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..254
FT /note="Methyl-CpG-binding domain-containing protein 11"
FT /id="PRO_0000405287"
FT DOMAIN 4..74
FT /note="MBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT REGION 56..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:6ACV"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:6ACV"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:6ACV"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6ACV"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:6ACV"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:6ACV"
SQ SEQUENCE 254 AA; 27642 MW; 633CFE2429C9E92A CRC64;
MGGEEEVVSV ELPAPSSWKK LFYPNKVGSV KKTEVVFVAP TGEEISNRKQ LEQYLKSHPG
NPAIAEFDWT TSGTPRRSAR ISEKTKATPS PDKEPPKKRG RTKSPVSKKD AEGEKSEGGG
EENSHVKDTE MNPPEGIAEN ENVTDKNGSG ETERVNDAKE NIVAEETPNA APVQEEGESM
KEKALDSVDD KSKETDKEKD TGSIEKNSVD VEKKTVEASD EKKNSEAETR NHEENGLTTE
AEGKEKTAEG EATG
