ID MBD10_ARATH Reviewed; 384 AA.
AC Q9XI36; Q0WLE9;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE RecName: Full=Methyl-CpG-binding domain-containing protein 10;
DE Short=AtMBD10;
DE Short=MBD10;
DE AltName: Full=Methyl-CpG-binding protein MBD10;
GN Name=MBD10; OrderedLocusNames=At1g15340; ORFNames=F9L1.28;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 1).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP 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 [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 FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=19061642; DOI=10.1016/j.molcel.2008.11.009;
RA Preuss S.B., Costa-Nunes P., Tucker S., Pontes O., Lawrence R.J.,
RA Mosher R., Kasschau K.D., Carrington J.C., Baulcombe D.C., Viegas W.,
RA Pikaard C.S.;
RT "Multimegabase silencing in nucleolar dominance involves siRNA-directed DNA
RT methylation and specific methylcytosine-binding proteins.";
RL Mol. Cell 32:673-684(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, 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: Probable transcriptional regulator (By similarity). Required
CC for nucleolar dominance that consist in the silencing of rRNA genes
CC inherited from one progenitor in genetic hybrids. {ECO:0000250,
CC ECO:0000269|PubMed:19061642}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19061642}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9XI36-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9XI36-2; Sequence=VSP_040661;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, buds, flowers, stems and
CC siliques. {ECO:0000269|PubMed:12954765}.
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: Impaired nucleolar dominance.
CC {ECO:0000269|PubMed:19061642}.
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DR EMBL; AC007591; AAD39661.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29305.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29306.1; -; Genomic_DNA.
DR EMBL; AY094439; AAM19811.1; -; mRNA.
DR EMBL; BT020367; AAV85722.1; -; mRNA.
DR EMBL; AK230256; BAF02058.1; -; mRNA.
DR PIR; G86287; G86287.
DR RefSeq; NP_001185003.1; NM_001198074.1. [Q9XI36-2]
DR RefSeq; NP_563971.1; NM_101403.4. [Q9XI36-1]
DR AlphaFoldDB; Q9XI36; -.
DR SMR; Q9XI36; -.
DR BioGRID; 23343; 2.
DR IntAct; Q9XI36; 2.
DR STRING; 3702.Q9XI36; -.
DR iPTMnet; Q9XI36; -.
DR MetOSite; Q9XI36; -.
DR PaxDb; 3702-AT1G15340-1; -.
DR ProMEX; Q9XI36; -.
DR ProteomicsDB; 238869; -. [Q9XI36-1]
DR EnsemblPlants; AT1G15340.1; AT1G15340.1; AT1G15340. [Q9XI36-1]
DR EnsemblPlants; AT1G15340.2; AT1G15340.2; AT1G15340. [Q9XI36-2]
DR GeneID; 838103; -.
DR Gramene; AT1G15340.1; AT1G15340.1; AT1G15340. [Q9XI36-1]
DR Gramene; AT1G15340.2; AT1G15340.2; AT1G15340. [Q9XI36-2]
DR KEGG; ath:AT1G15340; -.
DR Araport; AT1G15340; -.
DR TAIR; AT1G15340; MBD10.
DR eggNOG; ENOG502RYIM; Eukaryota.
DR HOGENOM; CLU_051759_0_0_1; -.
DR InParanoid; Q9XI36; -.
DR OMA; SEFEWTT; -.
DR OrthoDB; 622866at2759; -.
DR PRO; PR:Q9XI36; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XI36; baseline and differential.
DR Genevisible; Q9XI36; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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; METHYL-CPG BINDING DOMAIN CONTAINING PROTEIN, EXPRESSED; 1.
DR PANTHER; PTHR33729:SF6; METHYL-CPG-BINDING DOMAIN-CONTAINING PROTEIN 10; 1.
DR Pfam; PF01429; MBD; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR PROSITE; PS50982; MBD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..384
FT /note="Methyl-CpG-binding domain-containing protein 10"
FT /id="PRO_0000405286"
FT DOMAIN 4..74
FT /note="MBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT REGION 65..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 100..224
FT /evidence="ECO:0000255"
FT COILED 310..356
FT /evidence="ECO:0000255"
FT COMPBIAS 67..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 56..107
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_040661"
SQ SEQUENCE 384 AA; 42358 MW; 29CA77B564341023 CRC64;
MENTDELVSI ELPAPASWKK LFYPKRAGTP RKTEIVFVAP TGEEISSRKQ LEQYLKAHPG
NPVISEFEWT TGETPRRSSR ISQKVKATTP TPDKEPLLKK RRSSLTKKDN KEAAEKNEEA
AVKENMDVDK DGKTENAEAE KEKEKEGVTE IAEAEKENNE GEKTEAEKVN KEGEKTEAGK
EGQTEIAEAE KEKEGEKAEA ENKEAEVVRD KKESMEVDTS ELEKKAGSGE GAEEPSKVEG
LKDTEMKEAQ EVVTEADVEK KPAEEKTENK GSVTTEANGE QNVTLGEPNL DADAEADKGK
ESKEYDEKTT EAEANKENDT QESDEKKTEA AANKENETQE SDVKKTEAAV AEEKSNDMKA
EDTNRSLEAN QVQQQQGAAA SVSC
//
