MBD13_ARATH
ID MBD13_ARATH Reviewed; 746 AA.
AC Q9LTJ8; Q0WLQ6; Q8L791;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Methyl-CpG-binding domain-containing protein 13;
DE Short=AtMBD13;
DE Short=MBD13;
DE AltName: Full=Methyl-CpG-binding protein MBD13;
GN Name=MBD13; OrderedLocusNames=At5g52230; ORFNames=F17P19.13;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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;
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] OF 186-746.
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 [5]
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 [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).
CC -!- FUNCTION: Probable transcriptional regulator. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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=BAF01951.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB025603; BAA97466.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96188.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96189.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69599.1; -; Genomic_DNA.
DR EMBL; AY136403; AAM97069.1; -; mRNA.
DR EMBL; BT000226; AAN15545.1; -; mRNA.
DR EMBL; AK230136; BAF01951.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001190520.1; NM_001203591.2.
DR RefSeq; NP_001331264.1; NM_001344990.1.
DR RefSeq; NP_200036.1; NM_124602.4.
DR AlphaFoldDB; Q9LTJ8; -.
DR BioGRID; 20544; 2.
DR IntAct; Q9LTJ8; 2.
DR STRING; 3702.AT5G52230.2; -.
DR iPTMnet; Q9LTJ8; -.
DR PaxDb; Q9LTJ8; -.
DR PRIDE; Q9LTJ8; -.
DR ProteomicsDB; 238518; -.
DR EnsemblPlants; AT5G52230.1; AT5G52230.1; AT5G52230.
DR EnsemblPlants; AT5G52230.2; AT5G52230.2; AT5G52230.
DR EnsemblPlants; AT5G52230.3; AT5G52230.3; AT5G52230.
DR GeneID; 835299; -.
DR Gramene; AT5G52230.1; AT5G52230.1; AT5G52230.
DR Gramene; AT5G52230.2; AT5G52230.2; AT5G52230.
DR Gramene; AT5G52230.3; AT5G52230.3; AT5G52230.
DR KEGG; ath:AT5G52230; -.
DR Araport; AT5G52230; -.
DR TAIR; locus:2145091; AT5G52230.
DR eggNOG; ENOG502QS50; Eukaryota.
DR HOGENOM; CLU_443036_0_0_1; -.
DR InParanoid; Q9LTJ8; -.
DR OMA; KVQRIVP; -.
DR OrthoDB; 1305422at2759; -.
DR PhylomeDB; Q9LTJ8; -.
DR PRO; PR:Q9LTJ8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LTJ8; baseline and differential.
DR Genevisible; Q9LTJ8; AT.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0008327; F:methyl-CpG binding; ISS:TAIR.
DR InterPro; IPR038945; MBD13-like.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR PANTHER; PTHR34067; PTHR34067; 1.
DR PROSITE; PS50982; MBD; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..746
FT /note="Methyl-CpG-binding domain-containing protein 13"
FT /id="PRO_0000405289"
FT DOMAIN 29..104
FT /note="MBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT REGION 131..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 13..20
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 44..51
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 256..263
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 131..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 8
FT /note="D -> G (in Ref. 3; AAM97069/AAN15545)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 746 AA; 82656 MW; A0EACB409EB5953A CRC64;
MNGEGISDGL SAERKVEIRV RKNGRKDKVI VEKSAAQGLP EGWIKKLEIT NRSGRKTRRD
PFFIDPKSEY IFQSFKDASR YVETGNIGHY ARKLKESDIE DDDSGNGKTV LRLEYVDKRS
ADDVLEKEKT IDDVRRSKRR NLSSSDEHSK NCKMTSDLSI VTSQVLEDLG KKEEVKDPIE
KQLIAKRVTR SQTKASTTEE VVVDLKRNLS SSNAKSEKDS VNSSVRSQKP KKEAVMKEEE
EQDSSEKRIT RSKVEEKKNE LSNSVARRTS KRLAGIELEP TPELKTRAKV QRIVPLDDEP
TPELKTRTKV QRVVPPDDEP TPELKTRTKI QRIVPPDDEP TLELKTRTKV QRILPPDDEL
TPELKSRTKV QRIVPPDDEL TPEFKTRTKV QQRIPPDDGR AGKCKQPVNH VTTSGSKKTE
IPLNKEVAQS CNEQSSQKPH AAAATSNNRV SADSAVGIQN IGKAVGRKPS KDKKTLKSPL
IVYELNPVFH LDGYKQKEEM SPVSPLSCQT SATKCEKTAA GKRVGRSSPK ANLTTSVKPT
QISPLRSPNK GKQPHPSDSG SAIQRRNKLA NEYSNSSVVR GTCSEVMEKS TNSFSSAFDS
TLADLCKDPC IAFAIKTLTG ESLCLLNTPA ISSNPINNHT KQKGVSFTPE TPGNVNTCSE
KLVFPSPPPG ANIWQDPCID FAIKTLTGAI PIGLDEPDTK SKSQGMTSTT AATQEAKGRQ
NNCDYMTNKT VGKPDDLRFT QSFSKD
