ELF6_ARATH
ID ELF6_ARATH Reviewed; 1340 AA.
AC Q6BDA0; Q56WH6; Q9FYD7;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Lysine-specific demethylase ELF6 {ECO:0000305};
DE EC=1.14.11.- {ECO:0000269|PubMed:25219852, ECO:0000269|PubMed:33107825};
DE AltName: Full=Early flowering 6 {ECO:0000303|PubMed:15377760};
DE AltName: Full=Jumonji domain-containing protein 11 {ECO:0000303|PubMed:18713399};
DE Short=AtJMJ11 {ECO:0000303|PubMed:18713399};
DE Short=Protein JUMONJI 11 {ECO:0000303|PubMed:18713399};
DE AltName: Full=Lysine-specific histone demethylase ELF6 {ECO:0000305};
DE AltName: Full=[histone H3]-trimethyl-L-lysine(27) monodemethylase JMJ11 {ECO:0000305};
GN Name=ELF6 {ECO:0000303|PubMed:15377760};
GN Synonyms=JMJ11 {ECO:0000303|PubMed:18713399}, PKDM9B;
GN OrderedLocusNames=At5g04240 {ECO:0000312|Araport:AT5G04240};
GN ORFNames=F21E1.160 {ECO:0000312|EMBL:CAC05506.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=15377760; DOI=10.1105/tpc.104.025353;
RA Noh B., Lee S.-H., Kim H.-J., Yi G., Shin E.-A., Lee M., Jung K.-J.,
RA Doyle M.R., Amasino R.M., Noh Y.-S.;
RT "Divergent roles of a pair of homologous jumonji/zinc-finger-class
RT transcription factor proteins in the regulation of Arabidopsis flowering
RT time.";
RL Plant Cell 16:2601-2613(2004).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 858-1340.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18950507; DOI=10.1186/1471-2148-8-294;
RA Zhou X., Ma H.;
RT "Evolutionary history of histone demethylase families: distinct
RT evolutionary patterns suggest functional divergence.";
RL BMC Evol. Biol. 8:294-294(2008).
RN [6]
RP GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
RX PubMed=18713399; DOI=10.1111/j.1744-7909.2008.00692.x;
RA Lu F., Li G., Cui X., Liu C., Wang X.-J., Cao X.;
RT "Comparative analysis of JmjC domain-containing proteins reveals the
RT potential histone demethylases in Arabidopsis and rice.";
RL J. Integr. Plant Biol. 50:886-896(2008).
RN [7]
RP FUNCTION, INTERACTION WITH BZR2, AND DISRUPTION PHENOTYPE.
RX PubMed=18467490; DOI=10.1073/pnas.0802254105;
RA Yu X., Li L., Li L., Guo M., Chory J., Yin Y.;
RT "Modulation of brassinosteroid-regulated gene expression by Jumonji domain-
RT containing proteins ELF6 and REF6 in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7618-7623(2008).
RN [8]
RP FUNCTION.
RX PubMed=19946624; DOI=10.1371/journal.pone.0008033;
RA Jeong J.H., Song H.R., Ko J.H., Jeong Y.M., Kwon Y.E., Seol J.H.,
RA Amasino R.M., Noh B., Noh Y.S.;
RT "Repression of FLOWERING LOCUS T chromatin by functionally redundant
RT histone H3 lysine 4 demethylases in Arabidopsis.";
RL PLoS ONE 4:E8033-E8033(2009).
RN [9]
RP FUNCTION, MUTAGENESIS OF ALA-424, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY,
RP AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=25219852; DOI=10.1038/nature13722;
RA Crevillen P., Yang H., Cui X., Greeff C., Trick M., Qiu Q., Cao X.,
RA Dean C.;
RT "Epigenetic reprogramming that prevents transgenerational inheritance of
RT the vernalized state.";
RL Nature 515:587-590(2014).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=33107825; DOI=10.7554/elife.58533;
RA Antunez-Sanchez J., Naish M., Ramirez-Prado J.S., Ohno S., Huang Y.,
RA Dawson A., Opassathian K., Manza-Mianza D., Ariel F., Raynaud C.,
RA Wibowo A., Daron J., Ueda M., Latrasse D., Slotkin R.K., Weigel D.,
RA Benhamed M., Gutierrez-Marcos J.;
RT "A new role for histone demethylases in the maintenance of plant genome
RT integrity.";
RL Elife 9:E58533.1-E58533.23(2020).
CC -!- FUNCTION: Histone demethylase that demethylates 'Lys-27' (H3K27me) of
CC histone H3, thus acting as a positive regulator of gene expression
CC (PubMed:33107825). Demethylates tri-methylated (H3K27me3) and di-
CC methylated (H3K27me2) H3K27me (PubMed:33107825). Inactive on H3K27me1,
CC H3K4me3, H3K9me2 and H3K36me3 (PubMed:33107825). Acts as a repressor of
CC the photoperiodic flowering pathway and of FT (PubMed:33107825). May
CC also be active on H3K4me. Binds around the transcription start site of
CC the FT locus. Required for epigenetic reprogramming by resetting the
CC expression of the floral repressor FLC locus, thus aluviating cold-
CC mediated FLC epigenetically silencing occurring during vernalization
CC and preventing inapropriate epigenetic states inheritence
CC (PubMed:25219852, PubMed:33107825). {ECO:0000269|PubMed:15377760,
CC ECO:0000269|PubMed:18467490, ECO:0000269|PubMed:19946624,
CC ECO:0000269|PubMed:25219852, ECO:0000269|PubMed:33107825}.
CC -!- FUNCTION: Together with REF6, required for H3K27me3 resetting
CC (especially in constitutive heterochromatin within the pericentromeric
CC regions) and transgenerational inheritance of histone marks, thus
CC acting in safeguarding genome and epigenome integrity during sexual
CC reproduction. {ECO:0000269|PubMed:33107825}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone
CC H3] + O2 = CO2 + formaldehyde + N(6),N(6)-dimethyl-L-lysyl(27)-
CC [histone H3] + succinate; Xref=Rhea:RHEA:60228, Rhea:RHEA-COMP:15535,
CC Rhea:RHEA-COMP:15539, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61961, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000269|PubMed:25219852, ECO:0000269|PubMed:33107825};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60229;
CC Evidence={ECO:0000269|PubMed:25219852, ECO:0000269|PubMed:33107825};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(27)-[histone H3] +
CC O2 = CO2 + formaldehyde + N(6)-methyl-L-lysyl(27)-[histone H3] +
CC succinate; Xref=Rhea:RHEA:60232, Rhea:RHEA-COMP:15539, Rhea:RHEA-
CC COMP:15544, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929,
CC ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:25219852,
CC ECO:0000269|PubMed:33107825};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60233;
CC Evidence={ECO:0000269|PubMed:25219852, ECO:0000269|PubMed:33107825};
CC -!- SUBUNIT: Interacts with BZR2 (via N-terminus).
CC {ECO:0000269|PubMed:18467490}.
CC -!- INTERACTION:
CC Q6BDA0; Q9LN63: BZR2; NbExp=3; IntAct=EBI-1798417, EBI-617078;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537,
CC ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in seedlings, cotyledons
CC and leaves (PubMed:25219852). Detected in inflorescences, stems, roots
CC and siliques but not in shoot apical meristems or root tips.
CC Accumulates in flowers and embryos (PubMed:25219852).
CC {ECO:0000269|PubMed:15377760, ECO:0000269|PubMed:18713399,
CC ECO:0000269|PubMed:25219852}.
CC -!- DISRUPTION PHENOTYPE: Early flowering a reduced number of rosette
CC leaves at bolting stage, but normal development of all other organs
CC (PubMed:33107825, PubMed:25219852). Hyper-methylated genes with
CC accumulation of H3K27me3 histone marks (PubMed:33107825). Reduced FLC
CC expression (PubMed:25219852). Partially redundant with JMJ14.
CC Brassinosteroid-insensitive phenotype. Plants lacking both REF6 and
CC ELF6 have several growth defects, such as increased number of petals,
CC reduced silique length, embryos with patterning defects, and
CC pleiotropic defects in leaf morphology, such as serrations and downward
CC curling; these defects are caused by epimutations arising in offspring
CC lineage due to a lack of H3K27me3 resetting during sexual reproduction
CC (PubMed:33107825). {ECO:0000269|PubMed:15377760,
CC ECO:0000269|PubMed:18467490, ECO:0000269|PubMed:25219852,
CC ECO:0000269|PubMed:33107825}.
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94870.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAC05506.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY664500; AAT77780.1; -; mRNA.
DR EMBL; AL391716; CAC05506.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90717.1; -; Genomic_DNA.
DR EMBL; AK222064; BAD94870.1; ALT_INIT; mRNA.
DR RefSeq; NP_196044.2; NM_120506.5.
DR AlphaFoldDB; Q6BDA0; -.
DR SMR; Q6BDA0; -.
DR BioGRID; 15583; 1.
DR DIP; DIP-46102N; -.
DR IntAct; Q6BDA0; 1.
DR STRING; 3702.AT5G04240.1; -.
DR PaxDb; Q6BDA0; -.
DR PRIDE; Q6BDA0; -.
DR ProMEX; Q6BDA0; -.
DR ProteomicsDB; 222231; -.
DR EnsemblPlants; AT5G04240.1; AT5G04240.1; AT5G04240.
DR GeneID; 830303; -.
DR Gramene; AT5G04240.1; AT5G04240.1; AT5G04240.
DR KEGG; ath:AT5G04240; -.
DR Araport; AT5G04240; -.
DR TAIR; locus:2146653; AT5G04240.
DR eggNOG; KOG1246; Eukaryota.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_001687_1_0_1; -.
DR InParanoid; Q6BDA0; -.
DR OMA; PFKCPWD; -.
DR OrthoDB; 664180at2759; -.
DR PhylomeDB; Q6BDA0; -.
DR PRO; PR:Q6BDA0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6BDA0; baseline and differential.
DR Genevisible; Q6BDA0; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0071558; F:histone H3-tri/di-methyl-lysine-27 demethylase activity; IDA:UniProtKB.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0071557; P:histone H3-K27 demethylation; IDA:UniProtKB.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IMP:TAIR.
DR GO; GO:0061086; P:negative regulation of histone H3-K27 methylation; IMP:UniProtKB.
DR GO; GO:1902465; P:negative regulation of histone H3-K27 trimethylation; IMP:UniProtKB.
DR GO; GO:0048579; P:negative regulation of long-day photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0048577; P:negative regulation of short-day photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0010219; P:regulation of vernalization response; IMP:UniProtKB.
DR GO; GO:0009741; P:response to brassinosteroid; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Activator; Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1340
FT /note="Lysine-specific demethylase ELF6"
FT /id="PRO_0000412632"
FT DOMAIN 16..57
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 262..428
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 1228..1250
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1251..1275
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1281..1305
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1311..1337
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 195..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1333
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9STM3"
FT MOTIF 818..825
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 1248..1255
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 227..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 305
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 307
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 396
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 1230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9STM3"
FT BINDING 1235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9STM3"
FT BINDING 1248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9STM3"
FT BINDING 1253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9STM3"
FT BINDING 1258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9STM3"
FT BINDING 1265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9STM3"
FT BINDING 1271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9STM3"
FT BINDING 1275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9STM3"
FT BINDING 1283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9STM3"
FT BINDING 1288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9STM3"
FT BINDING 1301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9STM3"
FT BINDING 1305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9STM3"
FT BINDING 1313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9STM3"
FT BINDING 1318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9STM3"
FT BINDING 1331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9STM3"
FT BINDING 1337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q9STM3"
FT MUTAGEN 424
FT /note="A->V: In elf6-5; reduced the H3K27 demethylase
FT activity, defective in the reactivation of FLC after
FT vernalization due to H3K4me accumulation at its locus, and
FT reduced FLC levels, especially in flowers and siliques."
FT /evidence="ECO:0000269|PubMed:25219852"
SQ SEQUENCE 1340 AA; 150072 MW; 40CB360D273989DC CRC64;
MGNVEIPNWL KALPLAPVFR PTDTEFADPI AYISKIEKEA SAFGICKIIP PLPKPSKKYV
FYNLNKSLLK CPELVSDVDI SKVCKEDRAV FTTRQQELGQ TVKKNKGEKG KSNSQRSGVK
QVWQSGGVYT LDQFEAKSKA FYKTQLGTVK ELAPVVIEAL FWKAALEKPI YIEYANDVPG
SAFGEPEDHF RHFRQRKRRG RGFYQRKTEN NDPSGKNGEK SSPEVEKAPL ASTSLSSQDS
SKQKNMDIVD EMEGTAGWKL SNSSWNLQMI ARSPGSVTRF MPDDIPGVTS PMVYIGMLFS
WFAWHVEDHE LHSMNYLHTG SPKTWYAVPC DYALDFEEVI RKNSYGRNID QLAALTQLGE
KTTLVSPEMI VASGIPCCRL VQNPGEFVVT FPRSYHVGFS HGFNCGEAAN FGTPQWLNVA
KEAAVRRAAM NYLPMLSHQQ LLYLLTMSFV SRVPRSLLPG GRSSRLRDRQ REEREFLVKR
AFVEDILNEN KNLSVLLREP GSRLVMWDPD LLPRHSALAL AAAGVAGASA VSPPAVAKKE
LEEGHSELQN KEKTSLLEEL SLFMEKLNDV YYDDDDGLLN DFQVDTGTLP CVACGVLGFP
FMSVVQPSEK ALKDLSERQG ETDAQEIMTL SSEKSDCEWK TSSRYIRPRI FCLEHTIELQ
RLLQSRGGLK FLVICHKDFQ KFKAHAAIVA EEVKVPFSYD DVLLESASQE ELSLIDLAIE
DEEKYEHSVD WTSELGINLR YCVKVRKNSP TKKIQHALSL GGLFSDTSQM LDFTTIRWLQ
RKSRSKAKPS STSSFTPCEH LEVKADGKLR DNLDSQTGKK EEKIIQYSRK KKLNPKPSAE
QVQELATLAK SKDFDKTCKN FSSRSHLDSA IRSEMNSEIG DSGRVIGVSF SINPCSSSFT
VGHGQEHPEI TVKFGSDLDG NVTNSLSMVN GDSADLTLTS ISREQHQGHS MTSNNNGSNS
GSHVVASQTI LVSTGDNHDG PRKLSGDYVC SDVSVRGIQE AVEMSDQEFG EPRSTVTNIE
DEQQSQIVKP TQREAVFGDH EQVEGAEAVS TRENLCSEII LHTEHSSAHV GMEIPDINTA
SENLVVDMTH DGEPLESSDI LSSSNGDEAS SNGLQVLNDE LSMESEVSSS ENTEVIEAPN
SMGEAKKKRK IESESETNDN PESSIGFIRS PCEGLRSRGK RKATCETSLK HTETSDEEKK
PIAKRLKKTP KACSGSRQQE VPTTTHPNRC YLEGCKMTFE SKAKLQTHKR NRCTHEGCGK
KFRAHKYLVL HQRVHKDERP FECSWKGCSM TFKWQWARTE HLRLHTGERP YICKVDGCGL
SFRFVSDYSR HRRKTMHYVT
