位置:首页 > 蛋白库 > REF6_ARATH
REF6_ARATH
ID   REF6_ARATH              Reviewed;        1360 AA.
AC   Q9STM3;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Lysine-specific demethylase REF6 {ECO:0000303|PubMed:15377760};
DE            EC=1.14.11.- {ECO:0000269|PubMed:33107825};
DE   AltName: Full=Jumonji domain-containing protein 12 {ECO:0000303|PubMed:18713399};
DE            Short=AtJMJ12 {ECO:0000303|PubMed:18713399};
DE            Short=Protein JUMONJI 12 {ECO:0000303|PubMed:18713399};
DE   AltName: Full=Lysine-specific histone demethylase REF6 {ECO:0000303|PubMed:15377760};
DE   AltName: Full=Protein ENHANCER OF ETHYLENE INSENSITIVITY 6 {ECO:0000303|PubMed:31418686};
DE   AltName: Full=Protein ETHYLENE-INSENSITIVE 6 {ECO:0000303|PubMed:31418686};
DE   AltName: Full=Protein RELATIVE OF EARLY FLOWERING 6 {ECO:0000303|PubMed:15377760};
DE   AltName: Full=[histone H3]-trimethyl-L-lysine(27) monodemethylase JMJ12 {ECO:0000305};
DE   AltName: Full=[histone H3]-trimethyl-L-lysine(36) monodemethylase JMJ12 {ECO:0000305};
DE   AltName: Full=[histone H3]-trimethyl-L-lysine(4) monodemethylase JMJ12 {ECO:0000305};
GN   Name=REF6 {ECO:0000303|PubMed:15377760};
GN   Synonyms=EIN6 {ECO:0000303|PubMed:31418686},
GN   JMJ12 {ECO:0000303|PubMed:18713399}, PKDM9A {ECO:0000303|PubMed:18950507};
GN   OrderedLocusNames=At3g48430 {ECO:0000312|Araport:AT3G48430};
GN   ORFNames=T29H11_50 {ECO:0000312|EMBL:CAB41155.1};
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, TISSUE
RP   SPECIFICITY, AND SUBCELLULAR LOCATION.
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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   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   [5]
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   [6]
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   [7]
RP   IDENTIFICATION BY 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).
RN   [8]
RP   FUNCTION.
RX   PubMed=20711170; DOI=10.1038/emboj.2010.198;
RA   Ko J.H., Mitina I., Tamada Y., Hyun Y., Choi Y., Amasino R.M., Noh B.,
RA   Noh Y.S.;
RT   "Growth habit determination by the balance of histone methylation
RT   activities in Arabidopsis.";
RL   EMBO J. 29:3208-3215(2010).
RN   [9]
RP   FUNCTION, AND MUTAGENESIS OF HIS-246.
RX   PubMed=21642989; DOI=10.1038/ng.854;
RA   Lu F., Cui X., Zhang S., Jenuwein T., Cao X.;
RT   "Arabidopsis REF6 is a histone H3 lysine 27 demethylase.";
RL   Nat. Genet. 43:715-719(2011).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH NFYC9.
RX   PubMed=25105952; DOI=10.1038/ncomms5601;
RA   Hou X., Zhou J., Liu C., Liu L., Shen L., Yu H.;
RT   "Nuclear factor Y-mediated H3K27me3 demethylation of the SOC1 locus
RT   orchestrates flowering responses of Arabidopsis.";
RL   Nat. Commun. 5:4601-4601(2014).
RN   [12]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BRM.
RX   PubMed=27111034; DOI=10.1038/ng.3555;
RA   Li C., Gu L., Gao L., Chen C., Wei C.Q., Qiu Q., Chien C.W., Wang S.,
RA   Jiang L., Ai L.F., Chen C.Y., Yang S., Nguyen V., Qi Y., Snyder M.P.,
RA   Burlingame A.L., Kohalmi S.E., Huang S., Cao X., Wang Z.Y., Wu K., Chen X.,
RA   Cui Y.;
RT   "Concerted genomic targeting of H3K27 demethylase REF6 and chromatin-
RT   remodeling ATPase BRM in Arabidopsis.";
RL   Nat. Genet. 48:687-693(2016).
RN   [13]
RP   FUNCTION, AND DOMAIN.
RX   PubMed=27111035; DOI=10.1038/ng.3556;
RA   Cui X., Lu F., Qiu Q., Zhou B., Gu L., Zhang S., Kang Y., Cui X., Ma X.,
RA   Yao Q., Ma J., Zhang X., Cao X.;
RT   "REF6 recognizes a specific DNA sequence to demethylate H3K27me3 and
RT   regulate organ boundary formation in Arabidopsis.";
RL   Nat. Genet. 48:694-699(2016).
RN   [14]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY HEAT.
RC   STRAIN=cv. Columbia;
RX   PubMed=30778176; DOI=10.1038/s41422-019-0145-8;
RA   Liu J., Feng L., Gu X., Deng X., Qiu Q., Li Q., Zhang Y., Wang M., Deng Y.,
RA   Wang E., He Y., Baeurle I., Li J., Cao X., He Z.;
RT   "An H3K27me3 demethylase-HSFA2 regulatory loop orchestrates
RT   transgenerational thermomemory in Arabidopsis.";
RL   Cell Res. 29:379-390(2019).
RN   [15]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH INO80.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX   PubMed=31418686; DOI=10.7554/elife.47835;
RA   Zander M., Willige B.C., He Y., Nguyen T.A., Langford A.E., Nehring R.,
RA   Howell E., McGrath R., Bartlett A., Castanon R., Nery J.R., Chen H.,
RA   Zhang Z., Jupe F., Stepanova A., Schmitz R.J., Lewsey M.G., Chory J.,
RA   Ecker J.R.;
RT   "Epigenetic silencing of a multifunctional plant stress regulator.";
RL   Elife 8:0-0(2019).
RN   [16]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=cv. Columbia;
RX   PubMed=30267471; DOI=10.1111/jipb.12726;
RA   Wang X., Gao J., Gao S., Li Z., Kuai B., Ren G.;
RT   "REF6 promotes lateral root formation through de-repression of PIN1/3/7
RT   genes.";
RL   J. Integr. Plant Biol. 61:383-387(2019).
RN   [17]
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).
RN   [18]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY DEHYDROABIETINAL.
RC   STRAIN=cv. Columbia, cv. Landsberg erecta, cv. No-0, and cv. Wassilewskija;
RX   PubMed=32392578; DOI=10.1093/jxb/eraa232;
RA   Chowdhury Z., Mohanty D., Giri M.K., Venables B.J., Chaturvedi R., Chao A.,
RA   Petros R.A., Shah J.;
RT   "Dehydroabietinal promotes flowering time and plant defense in Arabidopsis
RT   via the autonomous pathway genes FLOWERING LOCUS D, FVE, and RELATIVE OF
RT   EARLY FLOWERING 6.";
RL   J. Exp. Bot. 71:4903-4913(2020).
RN   [19]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=cv. Columbia;
RX   PubMed=33037128; DOI=10.1104/pp.20.01255;
RA   Chen H., Tong J., Fu W., Liang Z., Ruan J., Yu Y., Song X., Yuan L.,
RA   Xiao L., Liu J., Cui Y., Huang S., Li C.;
RT   "The H3K27me3 demethylase RELATIVE OF EARLY FLOWERING6 suppresses seed
RT   dormancy by inducing abscisic acid catabolism.";
RL   Plant Physiol. 184:1969-1978(2020).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1260-1360 IN COMPLEX WITH ZINC
RP   AND DNA.
RC   STRAIN=cv. Columbia;
RX   PubMed=31048693; DOI=10.1038/s41467-019-10026-1;
RA   Qiu Q., Mei H., Deng X., He K., Wu B., Yao Q., Zhang J., Lu F., Ma J.,
RA   Cao X.;
RT   "DNA methylation repels targeting of Arabidopsis REF6.";
RL   Nat. Commun. 10:2063-2063(2019).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 1223-1360 IN COMPLEX WITH ZINC
RP   AND DNA, FUNCTION, MUTAGENESIS OF LYS-1281; TYR-1282; TRP-1309; TRP-1311;
RP   GLU-1315; PHE-1339; VAL-1340; SER-1341 AND ASP-1342, DOMAIN, AND SUBUNIT.
RX   PubMed=32257379; DOI=10.1038/s41421-020-0150-6;
RA   Tian Z., Li X., Li M., Wu W., Zhang M., Tang C., Li Z., Liu Y., Chen Z.,
RA   Yang M., Ma L., Caba C., Tong Y., Lam H.-M., Dai S., Chen Z.;
RT   "Crystal structures of REF6 and its complex with DNA reveal diverse
RT   recognition mechanisms.";
RL   Cell Discov. 6:17-17(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 both tri- (H3K27me3) and di-methylated
CC       (H3K27me2) H3K27me (PubMed:21642989, PubMed:27111035, PubMed:33107825).
CC       Demethylates also H3K4me3/2 and H3K36me3/2 in an in vitro assay
CC       (PubMed:20711170). Involved in the transcriptional regulation of
CC       hundreds of genes regulating developmental patterning and responses to
CC       various stimuli (PubMed:18467490). Binds DNA via its four zinc fingers
CC       in a sequence-specific manner, 5'-CTCTG(C/T)T(C/T)-3' (5'-CTCTGYTY-3'),
CC       with a preference for hypo-methylated status (e.g. cytosine
CC       methylation), to promote the demethylation of H3K27me3 and recruit the
CC       chromatin remodeler BRM in order to activate gene expression
CC       (PubMed:27111034, PubMed:27111035, PubMed:32257379, PubMed:31048693).
CC       Participates in the regulation of organ boundary formation
CC       (PubMed:27111034, PubMed:27111035, PubMed:32257379, PubMed:31048693).
CC       Bind mostly motifs located in active chromatin states which are
CC       depleted for heterochromatic modifications (PubMed:31048693). Involved
CC       in the regulation of flowering time by repressing FLOWERING LOCUS C
CC       (FLC) expression (PubMed:15377760, PubMed:33107825, PubMed:32392578).
CC       Stimulates lateral roots formation (e.g. primordium initiation and
CC       emergence) via the epigenetic de-repression of PIN genes such as PIN1,
CC       PIN3 and PIN7 directly by modulating the methylation status of their
CC       loci (PubMed:30267471). Interacts with the NF-Y complex to regulate
CC       SOC1 (PubMed:25105952). Mediates the recruitment of BRM to its target
CC       loci (PubMed:27111034). Together with EEN, involved in the epigenetic
CC       chromatin-dependent regulatory mechanism that monitors the expression
CC       of the essential multifunctional plant stress regulator EIN2 via
CC       H3K27me3 repressive histone demethylation and histone variant H2A.Z
CC       eviction, thus modulating responses to ethylene (ET), especially during
CC       embryogenesis (PubMed:31418686). Eluviates seed dormancy by triggering
CC       abscisic acid (ABA) catabolism in seeds via the induction of CYP707A1
CC       and CYP707A3 expression, genes involved in ABA degradation; binds
CC       directly to CYP707A1 and CYP707A3 loci to reduce their H3K27me3 levels
CC       in developing siliques (PubMed:33037128). Required for systemic
CC       acquired resistance (SAR) toward pathogenic bacteria (e.g. Pseudomonas
CC       syringae pv tomato DC3000 (avrPto)) (PubMed:32392578). Together with
CC       FLD and MSI4/FVE, contributes to dehydroabietinal-dependent (DA, a
CC       diterpenoid tricyclic diterpene) activation of flowering ans SAR
CC       (PubMed:32392578). Binds to the HSFA2 chromatin region to alleviate
CC       H3K27me3 repressive marks and trigger its expression in response to
CC       heat in a BRM-dependent manner (PubMed:30778176). Involved in the
CC       mechanisms necessary for quick response to heat and subsequent
CC       heritable transgenerational memory of heat acclimation (global warming)
CC       such as early flowering and attenuated immunity; this process includes
CC       epigenetic regulation as well as post-transcriptional gene silencing
CC       (PTGS) (PubMed:30778176). In response to heat, HSFA2 is activated and
CC       promotes the expression of REF6 which in turn derepresses HSFA2, thus
CC       establishing an heritable feedback loop able to trigger SGIP1 and
CC       subsequent SGIP1-mediated SGS3 degradation; this prevents the
CC       biosynthesis of trans-acting siRNA (tasiRNA) and leads to the release
CC       of HTT5, which drives early flowering but attenuates immunity
CC       (PubMed:30778176). {ECO:0000269|PubMed:15377760,
CC       ECO:0000269|PubMed:18467490, ECO:0000269|PubMed:20711170,
CC       ECO:0000269|PubMed:21642989, ECO:0000269|PubMed:25105952,
CC       ECO:0000269|PubMed:27111034, ECO:0000269|PubMed:27111035,
CC       ECO:0000269|PubMed:30267471, ECO:0000269|PubMed:30778176,
CC       ECO:0000269|PubMed:31048693, ECO:0000269|PubMed:31418686,
CC       ECO:0000269|PubMed:32257379, ECO:0000269|PubMed:32392578,
CC       ECO:0000269|PubMed:33037128, ECO:0000269|PubMed:33107825}.
CC   -!- FUNCTION: Involved in the maintenance of H3K27me1 histone marks on
CC       euchromatin in a PRC2-dependent manner, to maintain low-level basal
CC       expression of corresponding genes (PubMed:33107825). Together with
CC       ELF6, required for H3K27me3 resetting (especially in constitutive
CC       heterochromatin within the pericentromeric regions) and
CC       transgenerational inheritance of histone marks, thus acting in
CC       safeguarding genome and epigenome integrity during sexual reproduction
CC       (PubMed:33107825). {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:33107825};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60229;
CC         Evidence={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:33107825};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60233;
CC         Evidence={ECO:0000269|PubMed:33107825};
CC   -!- SUBUNIT: Forms homooligomers (PubMed:32257379). Interacts with BZR2
CC       (via N-terminus) (PubMed:18467490). Interacts with BRM in the SWI/SNF
CC       complex (PubMed:27111034). Interacts (via N-terminus) with NFYC9
CC       (PubMed:25105952). Associates with INO80 (PubMed:31418686).
CC       {ECO:0000269|PubMed:18467490, ECO:0000269|PubMed:25105952,
CC       ECO:0000269|PubMed:27111034, ECO:0000269|PubMed:32257379,
CC       ECO:0000303|PubMed:31418686}.
CC   -!- INTERACTION:
CC       Q9STM3; Q9LN63: BZR2; NbExp=2; IntAct=EBI-1798387, EBI-617078;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537,
CC       ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:15377760,
CC       ECO:0000269|PubMed:27111034}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the shoot apical meristem and
CC       primary and secondary root tips, and lower expression in cotyledons,
CC       leaves and root axis along vascular tissues (PubMed:30267471). Detected
CC       in inflorescences, stems and siliques. Present in seeds
CC       (PubMed:33037128). {ECO:0000269|PubMed:15377760,
CC       ECO:0000269|PubMed:18713399, ECO:0000269|PubMed:30267471,
CC       ECO:0000269|PubMed:33037128}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates during seed development, seed storage,
CC       and seed germination stages (PubMed:33037128). In roots, highly
CC       expressed in the stele, but barely detectable in the cortex and
CC       epidermis (PubMed:30267471). Not observed in lateral root primordia,
CC       but detected in both young and mature lateral roots (PubMed:30267471).
CC       {ECO:0000269|PubMed:30267471, ECO:0000269|PubMed:33037128}.
CC   -!- INDUCTION: Induced by abscisic acid (ABA) during seed germination
CC       (PubMed:33037128). Induced by dehydroabietinal-dependent (DA), a
CC       diterpenoid tricyclic diterpene that promotes flowering and systemic
CC       acquired resistance (SAR) (PubMed:32392578). Up-regulated by heat
CC       stress (at 30 degrees Celsius) and remains up-regulated
CC       transgenerationally in the unstressed progeny (at 22 degrees Celsius),
CC       partly via an heritable feedback loop involving HSFA2
CC       (PubMed:30778176). {ECO:0000269|PubMed:30778176,
CC       ECO:0000269|PubMed:32392578, ECO:0000269|PubMed:33037128}.
CC   -!- DOMAIN: The 4 C2H2-type zinc fingers are required for DNA-binding, but
CC       dispensable for the H3K27me3/2 demethylase activity.
CC       {ECO:0000269|PubMed:27111035, ECO:0000269|PubMed:32257379}.
CC   -!- DISRUPTION PHENOTYPE: Late-flowering in both long and short days with
CC       an increased number of rosette leaves at bolting stage
CC       (PubMed:15377760, PubMed:33107825, PubMed:32392578). Brassinosteroid-
CC       insensitive phenotype (PubMed:18467490). Hyper-methylated genes with
CC       accumulation of H3K27me3 histone marks, but drastic reduction in
CC       H3K27me1 (PubMed:33107825). Enhanced dormancy associated with increased
CC       abscisic acid (ABA) levels as well as reduced expression of CYP707A1
CC       and CYP707A3 (due to higher H3K27me3 content at their loci), genes
CC       involved in ABA catabolism, during seed development and germination
CC       (PubMed:33037128). Suppressed expression of PIN genes (e.g. PIN1, PIN3
CC       and PIN7) due to increased levels of H3K27me3 at their loci and leading
CC       to altered lateral root formation and elongation (PubMed:30267471).
CC       Impaired systemic acquired resistance (SAR) toward pathogenic bacteria
CC       (e.g. Pseudomonas syringae pv tomato DC3000 (avrPto))
CC       (PubMed:32392578). Lost ability of dehydroabietinal-dependent (DA, a
CC       diterpenoid tricyclic diterpene) to trigger flowering and systemic
CC       acquired resistance (SAR) (PubMed:32392578). Elevated H3K27me3 levels
CC       at HSFA2 locus associated with a reduced expression of HSFA2 and
CC       altered thermo-responsiveness and thermomemory of flowering
CC       (PubMed:30778176). Plants lacking both REF6 and ELF6 have several
CC       growth defects, such as increased number of petals, reduced silique
CC       length, embryos with patterning defects, and pleiotropic defects in
CC       leaf morphology, such as serrations and downward curling; these defects
CC       are caused by epimutations arising in offspring lineage due to a lack
CC       of H3K27me3 resetting during sexual reproduction (PubMed:33107825).
CC       Plants missing both EEN and REF6/EIN6 (e.g. ref6-1 een-2 and ein6-1
CC       een-1), as well as double mutants ref6-1 ino80-1 and ref6-1 arp5-1, are
CC       insensitive to ethylene (ET) and exhibit reduced levels of EIN2
CC       associated with a shift of the chromatin landscape to a repressive
CC       state at its locus (e.g. H3K27me3 and H2A.Z) (PubMed:31418686).
CC       {ECO:0000269|PubMed:15377760, ECO:0000269|PubMed:18467490,
CC       ECO:0000269|PubMed:30267471, ECO:0000269|PubMed:30778176,
CC       ECO:0000269|PubMed:31418686, ECO:0000269|PubMed:32392578,
CC       ECO:0000269|PubMed:33037128, ECO:0000269|PubMed:33107825}.
CC   -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: According to some authors, recombinant REF6 can demethylate
CC       H3K4me3/2 and H3K36me3/2 (PubMed:20711170). In contrast,
CC       PubMed:21642989 and PubMed:27111035 show that REF6 is an intrinsic
CC       H3K27me3/2-specific demethylase. The different activities seen may be
CC       caused by the presence of different cofactors.
CC       {ECO:0000305|PubMed:20711170}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY664499; AAT77779.1; -; mRNA.
DR   EMBL; AL049659; CAB41155.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78416.1; -; Genomic_DNA.
DR   PIR; T06699; T06699.
DR   RefSeq; NP_680116.2; NM_148863.4.
DR   PDB; 6A57; X-ray; 2.70 A; A=1223-1360.
DR   PDB; 6A58; X-ray; 1.57 A; A=1223-1360.
DR   PDB; 6A59; X-ray; 1.82 A; A=1223-1360.
DR   PDB; 6JNL; X-ray; 2.15 A; A=1260-1360.
DR   PDB; 6JNM; X-ray; 2.05 A; A/B=1260-1360.
DR   PDB; 6JNN; X-ray; 2.60 A; A/B/G/N=1260-1360.
DR   PDBsum; 6A57; -.
DR   PDBsum; 6A58; -.
DR   PDBsum; 6A59; -.
DR   PDBsum; 6JNL; -.
DR   PDBsum; 6JNM; -.
DR   PDBsum; 6JNN; -.
DR   AlphaFoldDB; Q9STM3; -.
DR   SMR; Q9STM3; -.
DR   BioGRID; 9321; 4.
DR   DIP; DIP-46006N; -.
DR   IntAct; Q9STM3; 1.
DR   STRING; 3702.AT3G48430.1; -.
DR   iPTMnet; Q9STM3; -.
DR   PaxDb; Q9STM3; -.
DR   PRIDE; Q9STM3; -.
DR   ProteomicsDB; 236965; -.
DR   EnsemblPlants; AT3G48430.1; AT3G48430.1; AT3G48430.
DR   GeneID; 824002; -.
DR   Gramene; AT3G48430.1; AT3G48430.1; AT3G48430.
DR   KEGG; ath:AT3G48430; -.
DR   Araport; AT3G48430; -.
DR   TAIR; locus:504955644; AT3G48430.
DR   eggNOG; KOG1246; Eukaryota.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_001687_1_0_1; -.
DR   InParanoid; Q9STM3; -.
DR   OMA; MRFREPS; -.
DR   OrthoDB; 664180at2759; -.
DR   PhylomeDB; Q9STM3; -.
DR   PRO; PR:Q9STM3; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9STM3; baseline and differential.
DR   GO; GO:0031011; C:Ino80 complex; TAS:UniProtKB.
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:0043621; F:protein self-association; IDA:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0046345; P:abscisic acid catabolic process; IMP:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0009873; P:ethylene-activated signaling pathway; IMP:TAIR.
DR   GO; GO:0010286; P:heat acclimation; IEP:UniProtKB.
DR   GO; GO:0071557; P:histone H3-K27 demethylation; IMP:UniProtKB.
DR   GO; GO:0033169; P:histone H3-K9 demethylation; IMP:TAIR.
DR   GO; GO:0048366; P:leaf development; IMP:TAIR.
DR   GO; GO:0035067; P:negative regulation of histone acetylation; IMP:TAIR.
DR   GO; GO:1902465; P:negative regulation of histone H3-K27 trimethylation; IMP:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; IMP:UniProtKB.
DR   GO; GO:1901333; P:positive regulation of lateral root development; IMP:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR   GO; GO:0097355; P:protein localization to heterochromatin; IDA:UniProtKB.
DR   GO; GO:0010104; P:regulation of ethylene-activated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0040029; P:regulation of gene expression, epigenetic; IDA:UniProtKB.
DR   GO; GO:2000028; P:regulation of photoperiodism, flowering; IMP:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0048838; P:release of seed from dormancy; IMP:UniProtKB.
DR   GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR   GO; GO:0009741; P:response to brassinosteroid; IMP:TAIR.
DR   GO; GO:1904629; P:response to diterpene; IMP:UniProtKB.
DR   GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEP:TAIR.
DR   GO; GO:0010182; P:sugar mediated signaling pathway; TAS:TAIR.
DR   GO; GO:0009627; P:systemic acquired resistance; IMP:UniProtKB.
DR   GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; 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   3D-structure; Abscisic acid signaling pathway; Acetylation; Activator;
KW   Chromatin regulator; Dioxygenase; DNA-binding; Ethylene signaling pathway;
KW   Germination; Iron; Metal-binding; Nucleus; Oxidoreductase; Plant defense;
KW   Reference proteome; Repeat; Stress response; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..1360
FT                   /note="Lysine-specific demethylase REF6"
FT                   /id="PRO_0000412631"
FT   DOMAIN          20..61
FT                   /note="JmjN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT   DOMAIN          203..369
FT                   /note="JmjC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   ZN_FING         1243..1266
FT                   /note="C2H2-type 1; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1266..1290
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1296..1320
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1326..1352
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          652..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          955..1012
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1044..1081
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1133..1155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1172..1238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1275..1348
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000269|PubMed:31048693,
FT                   ECO:0000269|PubMed:32257379, ECO:0007744|PDB:6A57,
FT                   ECO:0007744|PDB:6JNL, ECO:0007744|PDB:6JNM,
FT                   ECO:0007744|PDB:6JNN"
FT   MOTIF           944..951
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   COMPBIAS        677..695
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        958..983
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        984..1010
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1056..1073
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1133..1148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1172..1205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1224..1238
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         246
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         248
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         337
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         1245
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:32257379,
FT                   ECO:0007744|PDB:6A57, ECO:0007744|PDB:6A58,
FT                   ECO:0007744|PDB:6A59"
FT   BINDING         1250
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:32257379,
FT                   ECO:0007744|PDB:6A57, ECO:0007744|PDB:6A58,
FT                   ECO:0007744|PDB:6A59"
FT   BINDING         1263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:32257379,
FT                   ECO:0007744|PDB:6A57, ECO:0007744|PDB:6A58,
FT                   ECO:0007744|PDB:6A59"
FT   BINDING         1268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:31048693,
FT                   ECO:0000269|PubMed:32257379, ECO:0007744|PDB:6A57,
FT                   ECO:0007744|PDB:6A58, ECO:0007744|PDB:6A59,
FT                   ECO:0007744|PDB:6JNL, ECO:0007744|PDB:6JNN"
FT   BINDING         1273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:31048693,
FT                   ECO:0000269|PubMed:32257379, ECO:0007744|PDB:6A57,
FT                   ECO:0007744|PDB:6A58, ECO:0007744|PDB:6A59,
FT                   ECO:0007744|PDB:6JNL, ECO:0007744|PDB:6JNN"
FT   BINDING         1280
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:32257379,
FT                   ECO:0007744|PDB:6A57, ECO:0007744|PDB:6A58,
FT                   ECO:0007744|PDB:6A59"
FT   BINDING         1286
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:31048693,
FT                   ECO:0000269|PubMed:32257379, ECO:0007744|PDB:6A57,
FT                   ECO:0007744|PDB:6A58, ECO:0007744|PDB:6A59,
FT                   ECO:0007744|PDB:6JNL, ECO:0007744|PDB:6JNN"
FT   BINDING         1290
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:31048693,
FT                   ECO:0000269|PubMed:32257379, ECO:0007744|PDB:6A57,
FT                   ECO:0007744|PDB:6A58, ECO:0007744|PDB:6A59,
FT                   ECO:0007744|PDB:6JNL, ECO:0007744|PDB:6JNN"
FT   BINDING         1298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:31048693,
FT                   ECO:0000269|PubMed:32257379, ECO:0007744|PDB:6A57,
FT                   ECO:0007744|PDB:6A58, ECO:0007744|PDB:6A59,
FT                   ECO:0007744|PDB:6JNL, ECO:0007744|PDB:6JNN"
FT   BINDING         1303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:31048693,
FT                   ECO:0000269|PubMed:32257379, ECO:0007744|PDB:6A57,
FT                   ECO:0007744|PDB:6A58, ECO:0007744|PDB:6A59,
FT                   ECO:0007744|PDB:6JNL, ECO:0007744|PDB:6JNN"
FT   BINDING         1316
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:31048693,
FT                   ECO:0000269|PubMed:32257379, ECO:0007744|PDB:6A57,
FT                   ECO:0007744|PDB:6A58, ECO:0007744|PDB:6A59,
FT                   ECO:0007744|PDB:6JNL, ECO:0007744|PDB:6JNN"
FT   BINDING         1320
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:31048693,
FT                   ECO:0000269|PubMed:32257379, ECO:0007744|PDB:6A57,
FT                   ECO:0007744|PDB:6A58, ECO:0007744|PDB:6A59,
FT                   ECO:0007744|PDB:6JNL, ECO:0007744|PDB:6JNN"
FT   BINDING         1328
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000269|PubMed:31048693,
FT                   ECO:0000269|PubMed:32257379, ECO:0007744|PDB:6A57,
FT                   ECO:0007744|PDB:6A58, ECO:0007744|PDB:6A59,
FT                   ECO:0007744|PDB:6JNL, ECO:0007744|PDB:6JNM,
FT                   ECO:0007744|PDB:6JNN"
FT   BINDING         1333
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000269|PubMed:31048693,
FT                   ECO:0000269|PubMed:32257379, ECO:0007744|PDB:6A57,
FT                   ECO:0007744|PDB:6A58, ECO:0007744|PDB:6A59,
FT                   ECO:0007744|PDB:6JNL, ECO:0007744|PDB:6JNM,
FT                   ECO:0007744|PDB:6JNN"
FT   BINDING         1346
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000269|PubMed:31048693,
FT                   ECO:0000269|PubMed:32257379, ECO:0007744|PDB:6A57,
FT                   ECO:0007744|PDB:6A58, ECO:0007744|PDB:6A59,
FT                   ECO:0007744|PDB:6JNL, ECO:0007744|PDB:6JNM,
FT                   ECO:0007744|PDB:6JNN"
FT   BINDING         1352
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000269|PubMed:31048693,
FT                   ECO:0000269|PubMed:32257379, ECO:0007744|PDB:6A57,
FT                   ECO:0007744|PDB:6A58, ECO:0007744|PDB:6A59,
FT                   ECO:0007744|PDB:6JNL, ECO:0007744|PDB:6JNM,
FT                   ECO:0007744|PDB:6JNN"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MUTAGEN         246
FT                   /note="H->A: Loss of demethylase activity."
FT                   /evidence="ECO:0000269|PubMed:21642989"
FT   MUTAGEN         1281
FT                   /note="K->A: Reduced binding affinity to DNA."
FT                   /evidence="ECO:0000269|PubMed:32257379"
FT   MUTAGEN         1282
FT                   /note="Y->A: Reduced binding affinity to DNA."
FT                   /evidence="ECO:0000269|PubMed:32257379"
FT   MUTAGEN         1309
FT                   /note="W->A: Impaired binding affinity to DNA."
FT                   /evidence="ECO:0000269|PubMed:32257379"
FT   MUTAGEN         1311
FT                   /note="W->A: Reduced binding affinity to DNA."
FT                   /evidence="ECO:0000269|PubMed:32257379"
FT   MUTAGEN         1315
FT                   /note="E->A: Reduced binding affinity to DNA."
FT                   /evidence="ECO:0000269|PubMed:32257379"
FT   MUTAGEN         1339
FT                   /note="F->A: Reduced binding affinity to DNA."
FT                   /evidence="ECO:0000269|PubMed:32257379"
FT   MUTAGEN         1340
FT                   /note="V->A: Reduced binding affinity to DNA."
FT                   /evidence="ECO:0000269|PubMed:32257379"
FT   MUTAGEN         1341
FT                   /note="S->W: Reduced binding affinity to DNA."
FT                   /evidence="ECO:0000269|PubMed:32257379"
FT   MUTAGEN         1342
FT                   /note="D->A: Reduced binding affinity to DNA."
FT                   /evidence="ECO:0000269|PubMed:32257379"
FT   STRAND          1235..1238
FT                   /evidence="ECO:0007829|PDB:6A57"
FT   TURN            1239..1241
FT                   /evidence="ECO:0007829|PDB:6A58"
FT   STRAND          1242..1244
FT                   /evidence="ECO:0007829|PDB:6A58"
FT   TURN            1247..1249
FT                   /evidence="ECO:0007829|PDB:6A57"
FT   STRAND          1253..1256
FT                   /evidence="ECO:0007829|PDB:6A58"
FT   HELIX           1257..1264
FT                   /evidence="ECO:0007829|PDB:6A58"
FT   TURN            1271..1273
FT                   /evidence="ECO:0007829|PDB:6A58"
FT   STRAND          1276..1278
FT                   /evidence="ECO:0007829|PDB:6JNL"
FT   HELIX           1280..1290
FT                   /evidence="ECO:0007829|PDB:6A58"
FT   STRAND          1306..1309
FT                   /evidence="ECO:0007829|PDB:6A58"
FT   HELIX           1310..1321
FT                   /evidence="ECO:0007829|PDB:6A58"
FT   TURN            1331..1333
FT                   /evidence="ECO:0007829|PDB:6A58"
FT   STRAND          1336..1339
FT                   /evidence="ECO:0007829|PDB:6A58"
FT   HELIX           1340..1349
FT                   /evidence="ECO:0007829|PDB:6A58"
SQ   SEQUENCE   1360 AA;  152629 MW;  A45A5801285EBA16 CRC64;
     MAVSEQSQDV FPWLKSLPVA PEFRPTLAEF QDPIAYILKI EEEASRYGIC KILPPLPPPS
     KKTSISNLNR SLAARAAARV RDGGFGACDY DGGPTFATRQ QQIGFCPRKQ RPVQRPVWQS
     GEEYSFGEFE FKAKNFEKNY LKKCGKKSQL SALEIETLYW RATVDKPFSV EYANDMPGSA
     FIPLSLAAAR RRESGGEGGT VGETAWNMRA MSRAEGSLLK FMKEEIPGVT SPMVYVAMMF
     SWFAWHVEDH DLHSLNYLHM GAGKTWYGVP KDAALAFEEV VRVHGYGEEL NPLVTFSTLG
     EKTTVMSPEV FVKAGIPCCR LVQNPGEFVV TFPGAYHSGF SHGFNFGEAS NIATPEWLRM
     AKDAAIRRAA INYPPMVSHL QLLYDFVLAL GSRVPTSINP KPRSSRLKDK ARSEGERLTK
     KLFVQNIIHN NELLSSLGKG SPVALLPQSS SDISVCSDLR IGSHLITNQE NPIQLKCEDL
     SSDSVVVDLS NGLKDTVSVK EKFTSLCERS RNHLASTEKD TQETLSDAER RKNDAAVALS
     DQRLFSCVTC GVLSFDCVAI VQPKEAAARY LMSADCSFFN DWTAASGSAN LGQAARSLHP
     QSKEKHDVNY FYNVPVQTMD HSVKTGDQKT STTSPTIAHK DNDVLGMLAS AYGDSSDSEE
     EDQKGLVTPS SKGETKTYDQ EGSDGHEEAR DGRTSDFNCQ RLTSEQNGLS KGGKSSLLEI
     ALPFIPRSDD DSCRLHVFCL EHAAEVEQQL RPFGGINLML LCHPEYPRIE AEAKIVAEEL
     VINHEWNDTE FRNVTREDEE TIQAALDNVE AKGGNSDWTV KLGVNLSYSA ILSRSPLYSK
     QMPYNSIIYK AFGRSSPVAS SPSKPKVSGK RSSRQRKYVV GKWCGKVWMS HQVHPFLLEQ
     DLEGEESERS CHLRVAMDED ATGKRSFPNN VSRDSTTMFG RKYCRKRKIR AKAVPRKKLT
     SFKREDGVSD DTSEDHSYKQ QWRASGNEEE SYFETGNTAS GDSSNQMSDP HKGIIRHKGY
     KEFESDDEVS DRSLGEEYTV RACAASESSM ENGSQHSMYD HDDDDDDIDR QPRGIPRSQQ
     TRVFRNPVSY ESEDNGVYQQ SGRISISNRQ ANRMVGEYDS AENSLEERGF CSTGKRQTRS
     TAKRIAKTKT VQSSRDTKGR FLQEFASGKK NEELDSYMEG PSTRLRVRHQ KPSRGSLETK
     PKKIGKKRSG NASFSRVATE KDVEEKEEEE EEEENEEEEC AAYQCNMEGC TMSFSSEKQL
     MLHKRNICPI KGCGKNFFSH KYLVQHQRVH SDDRPLKCPW KGCKMTFKWA WSRTEHIRVH
     TGARPYVCAE PDCGQTFRFV SDFSRHKRKT GHSVKKTNKR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024