EBSL_ARATH
ID EBSL_ARATH Reviewed; 240 AA.
AC F4JGB7; O81451;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 2.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Chromatin remodeling protein At4g04260 {ECO:0000305};
GN OrderedLocusNames=At4g04260 {ECO:0000312|EMBL:AEE82376.1};
GN ORFNames=T27D20.8 {ECO:0000312|EMBL:AAC28226.1};
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 {ECO:0000312|Proteomes:UP000006548};
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).
CC -!- FUNCTION: Chromatin remodeling factor that binds to methylated histone
CC (e.g. H3K4me2/3) to prevent their acetylation (e.g. H3K9K14Ac), likely
CC by recruiting histone deacetylase (HDAC) complexes, and thus regulate
CC the transcription of target genes. {ECO:0000250|UniProtKB:Q9FEN9}.
CC -!- SUBUNIT: Recognizes di- and trimethylated histone H3 at lysine 4.
CC {ECO:0000250|UniProtKB:Q9FEN9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9FEN9}.
CC -!- SIMILARITY: Belongs to the SHL1/EBS protein family. {ECO:0000305}.
CC -!- CAUTION: Lacks two Cys residues in the RING-type zinc finger domain 2
CC that are conserved features of the family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC28226.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB77894.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF076274; AAC28226.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161499; CAB77894.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82376.1; -; Genomic_DNA.
DR PIR; T01813; T01813.
DR RefSeq; NP_192335.2; NM_116664.3.
DR AlphaFoldDB; F4JGB7; -.
DR SMR; F4JGB7; -.
DR STRING; 3702.AT4G04260.1; -.
DR PaxDb; F4JGB7; -.
DR PeptideAtlas; F4JGB7; -.
DR PRIDE; F4JGB7; -.
DR GeneID; 825742; -.
DR KEGG; ath:AT4G04260; -.
DR Araport; AT4G04260; -.
DR TAIR; locus:2137256; AT4G04260.
DR eggNOG; KOG1632; Eukaryota.
DR eggNOG; KOG1886; Eukaryota.
DR HOGENOM; CLU_085193_0_0_1; -.
DR InParanoid; F4JGB7; -.
DR PRO; PR:F4JGB7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JGB7; baseline and differential.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; ISS:UniProtKB.
DR GO; GO:0035067; P:negative regulation of histone acetylation; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR045205; EBS/SHL-like.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46364:SF13; PTHR46364:SF13; 1.
DR Pfam; PF01426; BAH; 1.
DR SMART; SM00439; BAH; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51038; BAH; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..240
FT /note="Chromatin remodeling protein At4g04260"
FT /id="PRO_0000434828"
FT DOMAIN 38..153
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT ZN_FING 155..205
FT /note="PHD-type; degenerate"
FT /evidence="ECO:0000305"
SQ SEQUENCE 240 AA; 27123 MW; C1B2D0B45CD770CE CRC64;
MAKTRPGVAF SSKIKLGKKD IKILGREILL GNVIVEVGFF TVGDCVLMRP SDAGKAPYVA
RVEKIEADAR NNVKVHCRWY YCPEESHGGR RQLHGAKELF LSDHFDVQSA HTIEGKCIVH
TFKNYTRLEN VGVEDYYCIF DYKAATGAFT PDRVAVYYKC EMPYNSDELM ELLLCHYRVH
LACVGVTIEE AKKLEHFVCV ECSSDEDGVK RFQNGFASST TNDLKPSAEK MIDVRASYEL
