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}.
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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
