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MBD12_ARATH
ID   MBD12_ARATH             Reviewed;         155 AA.
AC   Q9FZP6;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Putative methyl-CpG-binding domain protein 12;
DE            Short=AtMBD12;
DE            Short=MBD12;
DE   AltName: Full=Methyl-CpG-binding protein MBD12;
GN   Name=MBD12; OrderedLocusNames=At5g35338; ORFNames=MVP2, T26D22;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [3]
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   [4]
RP   MAD MOTIF, 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   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}.
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DR   EMBL; AB025636; BAB11482.1; -; Genomic_DNA.
DR   EMBL; AF058826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED93955.1; -; Genomic_DNA.
DR   RefSeq; NP_974851.1; NM_203122.2.
DR   AlphaFoldDB; Q9FZP6; -.
DR   SMR; Q9FZP6; -.
DR   STRING; 3702.AT5G35338.2; -.
DR   PaxDb; Q9FZP6; -.
DR   PRIDE; Q9FZP6; -.
DR   EnsemblPlants; AT5G35338.2; AT5G35338.2; AT5G35338.
DR   GeneID; 833492; -.
DR   Gramene; AT5G35338.2; AT5G35338.2; AT5G35338.
DR   KEGG; ath:AT5G35338; -.
DR   Araport; AT5G35338; -.
DR   TAIR; locus:504954793; AT5G35338.
DR   eggNOG; KOG4161; Eukaryota.
DR   HOGENOM; CLU_109577_0_0_1; -.
DR   InParanoid; Q9FZP6; -.
DR   OMA; WRLIPSM; -.
DR   OrthoDB; 377499at2759; -.
DR   PhylomeDB; Q9FZP6; -.
DR   PRO; PR:Q9FZP6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FZP6; baseline and differential.
DR   GO; GO:0005634; C:nucleus; ISS: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   3: Inferred from homology;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..155
FT                   /note="Putative methyl-CpG-binding domain protein 12"
FT                   /id="PRO_0000405288"
FT   DOMAIN          53..126
FT                   /note="MBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT   ZN_FING         1..53
FT                   /note="CW-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   REGION          130..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           3..45
FT                   /note="MBD-associated domain (MAD)"
FT   MOTIF           140..147
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   BINDING         4
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   BINDING         7
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   BINDING         33
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   BINDING         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
SQ   SEQUENCE   155 AA;  17889 MW;  B421496F54549A84 CRC64;
     MVQCTDCKKW RLIPSMQHYN IIKETQLQTP FVCGTTSGWT PNMSCNVPQD GTTCDTWPSI
     PPIPTGWSRS VHIRSESTKF ADVYYFPPSG ERLRSSAEVQ SFLDNHPEYV REGVNRSQFS
     FQIPKPLDDN YVKKRTRPVK RRKSSKDNNC EKGKK
 
 
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