ID JMJ14_ARATH Reviewed; 954 AA. AC Q8GUI6; F4JUW8; Q9SUN9; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 144. DE RecName: Full=Lysine-specific demethylase JMJ14 {ECO:0000303|PubMed:18713399}; DE EC=1.14.11.67 {ECO:0000269|PubMed:19946624, ECO:0000269|PubMed:20177424, ECO:0000269|PubMed:20202164, ECO:0000269|PubMed:29233856}; DE AltName: Full=Jumonji domain-containing protein 14 {ECO:0000303|PubMed:18713399}; DE Short=AtJMJ14 {ECO:0000303|PubMed:18713399}; DE Short=Protein JUMONJI 14 {ECO:0000303|PubMed:18713399}; DE AltName: Full=Jumonji domain-containing protein 4 {ECO:0000303|PubMed:19946624}; DE Short=AtJmj4 {ECO:0000303|PubMed:19946624}; DE AltName: Full=Lysine-specific histone demethylase JMJ14 {ECO:0000303|PubMed:18713399}; DE AltName: Full=[histone H3]-trimethyl-L-lysine(4) monodemethylase JMJ14 {ECO:0000305}; GN Name=JMJ14 {ECO:0000303|PubMed:18713399}; GN Synonyms=JMJ4 {ECO:0000303|PubMed:19946624}, PKDM7B GN {ECO:0000303|PubMed:18950507}; GN OrderedLocusNames=At4g20400 {ECO:0000312|Araport:AT4G20400}; GN ORFNames=F9F13.50 {ECO:0000312|EMBL:CAB45806.1}; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., RA Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."; RL Nature 402:769-777(1999). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). 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, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND RP SUBCELLULAR LOCATION. 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 [7] RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-397, SUBCELLULAR LOCATION, RP AND DISRUPTION PHENOTYPE. RX PubMed=20177424; DOI=10.1038/cr.2010.27; RA Lu F., Cui X., Zhang S., Liu C., Cao X.; RT "JMJ14 is an H3K4 demethylase regulating flowering time in Arabidopsis."; RL Cell Res. 20:387-390(2010). RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21052090; DOI=10.1038/embor.2010.158; RA Deleris A., Greenberg M.V., Ausin I., Law R.W., Moissiard G., Schubert D., RA Jacobsen S.E.; RT "Involvement of a Jumonji-C domain-containing histone demethylase in DRM2- RT mediated maintenance of DNA methylation."; RL EMBO Rep. 11:950-955(2010). RN [9] RP FUNCTION, AND MUTAGENESIS OF GLU-387. RX PubMed=20478993; DOI=10.1101/gad.579910; RA Searle I.R., Pontes O., Melnyk C.W., Smith L.M., Baulcombe D.C.; RT "JMJ14, a JmjC domain protein, is required for RNA silencing and cell-to- RT cell movement of an RNA silencing signal in Arabidopsis."; RL Genes Dev. 24:986-991(2010). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND RP COFACTOR. RX PubMed=20202164; DOI=10.1111/j.1365-313x.2010.04182.x; RA Yang W., Jiang D., Jiang J., He Y.; RT "A plant-specific histone H3 lysine 4 demethylase represses the floral RT transition in Arabidopsis."; RL Plant J. 62:663-673(2010). RN [11] RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH JMJ14, AND SUBCELLULAR RP LOCATION. RC STRAIN=cv. Columbia; RX PubMed=26617990; DOI=10.1038/celldisc.2015.3; RA Zhang S., Zhou B., Kang Y., Cui X., Liu A., Deleris A., Greenberg M.V.C., RA Cui X., Qiu Q., Lu F., Wohlschlegel J.A., Jacobsen S.E., Cao X.; RT "C-terminal domains of a histone demethylase interact with a pair of RT transcription factors and mediate specific chromatin association."; RL Cell Discov. 1:0-0(2015). RN [12] RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH NAC050 AND NAC051/NAC052, RP AND TISSUE SPECIFICITY. RC STRAIN=cv. Columbia; RX PubMed=25578968; DOI=10.1093/nar/gku1382; RA Ning Y.-Q., Ma Z.-Y., Huang H.-W., Mo H., Zhao T.-T., Li L., Cai T., RA Chen S., Ma L., He X.-J.; RT "Two novel NAC transcription factors regulate gene expression and flowering RT time by associating with the histone demethylase JMJ14."; RL Nucleic Acids Res. 43:1469-1484(2015). RN [13] RP SUBCELLULAR LOCATION, AND INTERACTION WITH THAL. RC STRAIN=cv. Columbia; RX PubMed=27792779; DOI=10.1371/journal.pgen.1006408; RA Chen Y.-J.C., Wang H.-J., Jauh G.-Y.; RT "Dual role of a SAS10/C1D family protein in ribosomal RNA gene expression RT and processing is essential for reproduction in Arabidopsis thaliana."; RL PLoS Genet. 12:e1006408-e1006408(2016). RN [14] RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE. RX PubMed=31826870; DOI=10.1242/dev.183905; RA Cattaneo P., Graeff M., Marhava P., Hardtke C.S.; RT "Conditional effects of the epigenetic regulator JUMONJI 14 in Arabidopsis RT root growth."; RL Development 146:0-0(2019). RN [15] RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION. RC STRAIN=cv. Columbia, and cv. Wassilewskija; RX PubMed=31429787; DOI=10.1186/s13059-019-1777-1; RA Song Q., Huang T.-Y., Yu H.H., Ando A., Mas P., Ha M., Chen Z.J.; RT "Diurnal regulation of SDG2 and JMJ14 by circadian clock oscillators RT orchestrates histone modification rhythms in Arabidopsis."; RL Genome Biol. 20:RESEARCH170.1-RESEARCH170.12(2019). RN [16] RP FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=cv. Columbia; RX PubMed=31038749; DOI=10.1111/nph.15874; RA Huang S., Zhang A., Jin J.B., Zhao B., Wang T.-J., Wu Y., Wang S., Liu Y., RA Wang J., Guo P., Ahmad R., Liu B., Xu Z.-Y.; RT "Arabidopsis histone H3K4 demethylase JMJ17 functions in dehydration stress RT response."; RL New Phytol. 223:1372-1387(2019). RN [17] RP FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=cv. Columbia; RX PubMed=31622519; DOI=10.1111/nph.16270; RA Li D., Liu R., Singh D., Yuan X., Kachroo P., Raina R.; RT "JMJ14 encoded H3K4 demethylase modulates immune responses by regulating RT defence gene expression and pipecolic acid levels."; RL New Phytol. 225:2108-2121(2020). RN [18] RP FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=cv. Columbia; RX PubMed=33986281; DOI=10.1038/s41467-021-22995-3; RA Butel N., Yu A., Le Masson I., Borges F., Elmayan T., Taochy C., RA Gursanscky N.R., Cao J., Bi S., Sawyer A., Carroll B.J., Vaucheret H.; RT "Contrasting epigenetic control of transgenes and endogenous genes promotes RT post-transcriptional transgene silencing in Arabidopsis."; RL Nat. Commun. 12:2787-2787(2021). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 35-597 IN COMPLEX WITH HISTONE RP H3K4ME3; NICKEL IONS AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, AND RP MUTAGENESIS OF PHE-171; GLU-285; SER-290; TYR-298; HIS-309; GLU-311; RP ASP-312; VAL-363; HIS-397 AND GLU-516. RX PubMed=29233856; DOI=10.1105/tpc.17.00666; RA Yang Z., Qiu Q., Chen W., Jia B., Chen X., Hu H., He K., Deng X., Li S., RA Tao W.A., Cao X., Du J.; RT "Structure of the Arabidopsis JMJ14-H3K4me3 Complex Provides Insight into RT the Substrate Specificity of KDM5 Subfamily Histone Demethylases."; RL Plant Cell 30:167-177(2018). CC -!- FUNCTION: Transcriptional repressor (PubMed:25578968). Histone CC demethylase that demethylates 'Lys-4' (H3K4me) of histone H3 with a CC higher activity for H3K4me3 and H3K4me2 than H3K4me1 (PubMed:29233856). CC No activity on H3K9me3/2, H3K36me3/2 and H3K27me3/2 (PubMed:29233856). CC Function as a nocturne 'eraser' to counteract the diurnal 'writer' CC methylase activity of ATXR3/SDG2 thus orchestrating the circadian rythm CC of histone modifications (e.g. H3K4me3) and modulating the rythmic CC expression of diurnal target genes; this mechanism relies also on the CC circadian clock oscillators CCA1 and LHY (PubMed:31429787). Involved in CC a negative regulation of root meristem growth upon suboptimal root CC growth conditions (PubMed:31826870). Represses FT and TSF expression to CC inhibit the floral transition. Binds around the transcription start CC site of the FT locus. Involved in the DRM2-mediated maintenance of DNA CC methylation, but not required for the de novo DNA methylation. Required CC for demethylating histone H3K4me3 at the target of RNA silencing. CC Counteracts the DNA methylation of expressed transgenes; specific CC attenuation of transgene DNA methylation enhances the production of CC aberrant RNAs (e.g. uncapped and antisense) that readily induce CC systemic RDR6-dependent post-transcriptional transgene silencing (PTGS) CC spreading (PubMed:33986281). Together with NAC051/NAC052 and NAC050, CC regulates gene expression and flowering time, probably by the promotion CC of RNA-mediated gene silencing (PubMed:25578968). Together with JMJ16 CC and JMJ17, required for plant growth and development (PubMed:31038749). CC Promotes local and systemic immunity (especially toward the bacterial CC pathogen Pseudomonas syringae Pst DC3000 avrRpt2) by regulating CC positively pathogen-induced H3K4me3 enrichment and expression of CC defense genes involved in salicylic acid (SA)- and pipecolic acid CC (Pip)-mediated defense pathways (e.g. PR1, FMO1, ALD1 and SARD4) CC (PubMed:31622519). {ECO:0000269|PubMed:19946624, CC ECO:0000269|PubMed:20177424, ECO:0000269|PubMed:20202164, CC ECO:0000269|PubMed:20478993, ECO:0000269|PubMed:21052090, CC ECO:0000269|PubMed:25578968, ECO:0000269|PubMed:26617990, CC ECO:0000269|PubMed:29233856, ECO:0000269|PubMed:31038749, CC ECO:0000269|PubMed:31429787, ECO:0000269|PubMed:31622519, CC ECO:0000269|PubMed:31826870, ECO:0000269|PubMed:33986281}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone CC H3] + O2 = CO2 + formaldehyde + N(6),N(6)-dimethyl-L-lysyl(4)- CC [histone H3] + succinate; Xref=Rhea:RHEA:60212, Rhea:RHEA-COMP:15537, CC Rhea:RHEA-COMP:15540, 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:19946624, ECO:0000269|PubMed:20177424, CC ECO:0000269|PubMed:20202164, ECO:0000269|PubMed:29233856}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60213; CC Evidence={ECO:0000269|PubMed:19946624, ECO:0000269|PubMed:20177424, CC ECO:0000269|PubMed:20202164, ECO:0000269|PubMed:29233856}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + CC O2 = CO2 + formaldehyde + N(6)-methyl-L-lysyl(4)-[histone H3] + CC succinate; Xref=Rhea:RHEA:60216, Rhea:RHEA-COMP:15540, Rhea:RHEA- CC COMP:15543, 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:19946624, CC ECO:0000269|PubMed:20177424, ECO:0000269|PubMed:20202164, CC ECO:0000269|PubMed:29233856}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60217; CC Evidence={ECO:0000269|PubMed:19946624, ECO:0000269|PubMed:20177424, CC ECO:0000269|PubMed:20202164, ECO:0000269|PubMed:29233856}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + N(6)-methyl-L-lysyl(4)-[histone H3] + O2 = CC CO2 + formaldehyde + L-lysyl(4)-[histone H3] + succinate; CC Xref=Rhea:RHEA:60220, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, CC ChEBI:CHEBI:61929; Evidence={ECO:0000269|PubMed:19946624, CC ECO:0000269|PubMed:20177424, ECO:0000269|PubMed:20202164, CC ECO:0000269|PubMed:29233856}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60221; CC Evidence={ECO:0000269|PubMed:19946624, ECO:0000269|PubMed:20177424, CC ECO:0000269|PubMed:20202164, ECO:0000269|PubMed:29233856}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)- CC [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone CC H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537, CC Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67; CC Evidence={ECO:0000269|PubMed:19946624, ECO:0000269|PubMed:20177424, CC ECO:0000269|PubMed:20202164, ECO:0000269|PubMed:29233856}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60209; CC Evidence={ECO:0000269|PubMed:19946624, ECO:0000269|PubMed:20177424, CC ECO:0000269|PubMed:20202164, ECO:0000269|PubMed:29233856}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000269|PubMed:20202164, ECO:0000269|PubMed:29233856}; CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:20202164, CC ECO:0000269|PubMed:29233856}; CC -!- SUBUNIT: Interacts with NAC050 and NAC051/NAC052 (PubMed:25578968, CC PubMed:26617990). Interacts with THAL in the nucleus (PubMed:27792779). CC {ECO:0000269|PubMed:25578968, ECO:0000269|PubMed:26617990, CC ECO:0000269|PubMed:27792779}. CC -!- INTERACTION: CC Q8GUI6; Q9SQX9: NAC050; NbExp=4; IntAct=EBI-4429826, EBI-4428214; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm CC {ECO:0000269|PubMed:19946624, ECO:0000269|PubMed:20177424, CC ECO:0000269|PubMed:21052090}. Nucleus {ECO:0000255|PROSITE- CC ProRule:PRU00537, ECO:0000255|PROSITE-ProRule:PRU00768, CC ECO:0000269|PubMed:26617990, ECO:0000269|PubMed:27792779}. Note=Not CC detected in the nucleolus and the chromocenters. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8GUI6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8GUI6-2; Sequence=VSP_041728; CC -!- TISSUE SPECIFICITY: Expressed in shoot apex, primary root tip, CC trichomes of young leaves, leaf vascular tissues, anther filaments and CC styles. Detected in inflorescences, leaves, stems, roots and siliques. CC Mostly expressed in floral organs, and, at low levels, in other organs CC (PubMed:25578968). {ECO:0000269|PubMed:18713399, CC ECO:0000269|PubMed:19946624, ECO:0000269|PubMed:20202164, CC ECO:0000269|PubMed:25578968}. CC -!- DEVELOPMENTAL STAGE: Expressed in mature root vasculature and CC throughout root meristem. {ECO:0000269|PubMed:31826870}. CC -!- INDUCTION: Circadian-regulation with peak levels occurring at night and CC lower levels after dawn under both diurnal and constant light CC conditions in a CCA1- and LHY-dependent manner. CC {ECO:0000269|PubMed:31429787}. CC -!- DISRUPTION PHENOTYPE: Early flowering (especially in long day CC conditions), but normal development of all organs (PubMed:31038749). CC Partially redundant with ELF6. Increased H3K4 methylation on specific CC genes, thus leading to their derepression (PubMed:25578968, CC PubMed:31826870). Slightly increased levels of CCA1 and LHY circadian CC oscillators transcription factors as well as of other clock genes such CC as TOC1, PRR5, PRR7, PRR9, GI, ELF3, ELF4, and LUX associated with CC higher H3K4me3 levels near their promoters (PubMed:31429787). Impaired CC systemic RDR6-dependent post-transcriptional transgene silencing (PTGS) CC associated with reduced production of aberrant RNAs (e.g. uncapped and CC antisense) (PubMed:33986281). Abnormal root meristem size as well as CC partial suppression of reduced root meristem size and growth vigor CC observed in brx mutants (PubMed:31826870). Compromised in both local CC and systemic defense responses to the bacterial pathogen Pseudomonas CC syringae Pst DC3000 avrRpt2 due to abnormal H3K4me3 enrichment and CC reduced expression of defense genes involved in salicylic acid CC (SA)- and pipecolic acid (Pip)-mediated defense pathways (e.g. PR1, CC FMO1, ALD1 and SARD4) (PubMed:31622519). The double mutant jmj17-1 CC jmj14-1 has an early flowering phenotype (especially in long day CC conditions) (PubMed:31038749). The triple mutant jmj17-1 jmj14-1 jmj16- CC 1 flowers even earlier (PubMed:31038749). {ECO:0000269|PubMed:19946624, CC ECO:0000269|PubMed:20177424, ECO:0000269|PubMed:20202164, CC ECO:0000269|PubMed:25578968, ECO:0000269|PubMed:26617990, CC ECO:0000269|PubMed:31038749, ECO:0000269|PubMed:31429787, CC ECO:0000269|PubMed:31622519, ECO:0000269|PubMed:31826870, CC ECO:0000269|PubMed:33986281}. CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB45806.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAB79040.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; 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; AL080253; CAB45806.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL161553; CAB79040.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002687; AEE84324.1; -; Genomic_DNA. DR EMBL; CP002687; AEE84325.1; -; Genomic_DNA. DR EMBL; BT002486; AAO00846.1; -; mRNA. DR EMBL; BT010548; AAQ65171.1; -; mRNA. DR PIR; T10582; T10582. DR RefSeq; NP_001031681.1; NM_001036604.1. [Q8GUI6-2] DR RefSeq; NP_193773.2; NM_118159.3. [Q8GUI6-1] DR PDB; 5YKN; X-ray; 2.30 A; A=35-597. DR PDB; 5YKO; X-ray; 2.90 A; A=35-597. DR PDBsum; 5YKN; -. DR PDBsum; 5YKO; -. DR AlphaFoldDB; Q8GUI6; -. DR SMR; Q8GUI6; -. DR BioGRID; 13079; 4. DR IntAct; Q8GUI6; 3. DR STRING; 3702.Q8GUI6; -. DR iPTMnet; Q8GUI6; -. DR PaxDb; 3702-AT4G20400-1; -. DR ProteomicsDB; 232294; -. [Q8GUI6-1] DR EnsemblPlants; AT4G20400.1; AT4G20400.1; AT4G20400. [Q8GUI6-1] DR EnsemblPlants; AT4G20400.2; AT4G20400.2; AT4G20400. [Q8GUI6-2] DR GeneID; 827788; -. DR Gramene; AT4G20400.1; AT4G20400.1; AT4G20400. [Q8GUI6-1] DR Gramene; AT4G20400.2; AT4G20400.2; AT4G20400. [Q8GUI6-2] DR KEGG; ath:AT4G20400; -. DR Araport; AT4G20400; -. DR TAIR; AT4G20400; JMJ14. DR eggNOG; KOG1246; Eukaryota. DR InParanoid; Q8GUI6; -. DR OMA; FEKCDIS; -. DR OrthoDB; 1205686at2759; -. DR PhylomeDB; Q8GUI6; -. DR PRO; PR:Q8GUI6; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; Q8GUI6; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR. DR GO; GO:0032453; F:histone H3K4 demethylase activity; IDA:TAIR. DR GO; GO:0034647; F:histone H3K4me/H3K4me2/H3K4me3 demethylase activity; IEA:RHEA. DR GO; GO:0042054; F:histone methyltransferase activity; IDA:TAIR. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:TAIR. DR GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB. DR GO; GO:0048589; P:developmental growth; IMP:UniProtKB. DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW. DR GO; GO:0034720; P:histone H3-K4 demethylation; IMP:TAIR. DR GO; GO:0062034; P:L-pipecolic acid biosynthetic process; IMP:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0009910; P:negative regulation of flower development; IMP:TAIR. DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IMP:UniProtKB. DR GO; GO:0048579; P:negative regulation of long-day photoperiodism, flowering; IMP:CACAO. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0048573; P:photoperiodism, flowering; IMP:UniProtKB. DR GO; GO:0099402; P:plant organ development; IMP:UniProtKB. DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW. DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB. DR GO; GO:1901672; P:positive regulation of systemic acquired resistance; IMP:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:TAIR. DR GO; GO:0060147; P:regulation of post-transcriptional gene silencing; IMP:UniProtKB. DR GO; GO:2000280; P:regulation of root development; IMP:UniProtKB. DR GO; GO:0010082; P:regulation of root meristem growth; IMP:UniProtKB. DR GO; GO:0009627; P:systemic acquired resistance; IMP:GO_Central. DR Gene3D; 3.30.160.360; -; 1. DR Gene3D; 2.60.120.650; Cupin; 1. DR InterPro; IPR003889; FYrich_C. DR InterPro; IPR003888; FYrich_N. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR003349; JmjN. DR InterPro; IPR004198; Znf_C5HC2. DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1. DR PANTHER; PTHR10694:SF105; LYSINE-SPECIFIC DEMETHYLASE JMJ14; 1. DR Pfam; PF05965; FYRC; 1. DR Pfam; PF05964; FYRN; 1. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF02375; JmjN; 1. DR Pfam; PF02928; zf-C5HC2; 1. DR SMART; SM00542; FYRC; 1. DR SMART; SM00541; FYRN; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00545; JmjN; 1. DR SUPFAM; SSF51197; Clavaminate synthase-like; 1. DR PROSITE; PS51543; FYRC; 1. DR PROSITE; PS51542; FYRN; 1. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS51183; JMJN; 1. DR Genevisible; Q8GUI6; AT. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromatin regulator; Dioxygenase; KW Flowering; Hypersensitive response; Iron; Metal-binding; Nucleus; KW Oxidoreductase; Plant defense; Reference proteome; Repressor; KW Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..954 FT /note="Lysine-specific demethylase JMJ14" FT /id="PRO_0000412633" FT DOMAIN 56..97 FT /note="JmjN" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537" FT DOMAIN 263..429 FT /note="JmjC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538" FT DOMAIN 726..784 FT /note="FYR N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00875" FT DOMAIN 786..876 FT /note="FYR C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00876" FT ZN_FING 519..571 FT /note="C5HC2" FT /evidence="ECO:0000255" FT REGION 1..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 148..170 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 641..671 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 884..905 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 136..143 FT /note="Nuclear localization signal 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768" FT MOTIF 470..477 FT /note="Nuclear localization signal 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768" FT COMPBIAS 26..42 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 645..671 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 309 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538, FT ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN, FT ECO:0007744|PDB:5YKO" FT BINDING 311 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538, FT ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN, FT ECO:0007744|PDB:5YKO" FT BINDING 397 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538, FT ECO:0000269|PubMed:29233856, ECO:0007744|PDB:5YKN, FT ECO:0007744|PDB:5YKO" FT BINDING 519 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:29233856, FT ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO" FT BINDING 522 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:29233856, FT ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO" FT BINDING 533 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:29233856, FT ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO" FT BINDING 535 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:29233856, FT ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO" FT BINDING 542 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:29233856, FT ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO" FT BINDING 545 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:29233856, FT ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO" FT BINDING 550 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:29233856, FT ECO:0007744|PDB:5YKO" FT BINDING 552 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:29233856, FT ECO:0007744|PDB:5YKN" FT SITE 171 FT /note="Involved in histone H3A7 recognition" FT /evidence="ECO:0000269|PubMed:29233856, FT ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO" FT SITE 285 FT /note="Involved in histone H3R2 recognition" FT /evidence="ECO:0000269|PubMed:29233856, FT ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO" FT SITE 290 FT /note="Involved in histone H3K4me3 recognition" FT /evidence="ECO:0000269|PubMed:29233856, FT ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO" FT SITE 298 FT /note="Involved in histone H3K4me3 recognition" FT /evidence="ECO:0000269|PubMed:29233856, FT ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO" FT SITE 312 FT /note="Involved in histone H3Q5 recognition" FT /evidence="ECO:0000269|PubMed:29233856, FT ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO" FT SITE 363 FT /note="Involved in histone H3A7 recognition" FT /evidence="ECO:0000269|PubMed:29233856, FT ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO" FT SITE 516 FT /note="Involved in histone H3R2 recognition" FT /evidence="ECO:0000269|PubMed:29233856, FT ECO:0007744|PDB:5YKN, ECO:0007744|PDB:5YKO" FT VAR_SEQ 1..64 FT /note="MDQLASLAESVAMEEDSEKQSIKGESSLEPDSTPSSPKITARWNPSEACRPL FT VDDAPIFYPTNE -> MILLHGQ (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_041728" FT MUTAGEN 171 FT /note="F->K: Decreased demethylation activity." FT /evidence="ECO:0000269|PubMed:29233856" FT MUTAGEN 285 FT /note="E->A: Decreased demethylation activity." FT /evidence="ECO:0000269|PubMed:29233856" FT MUTAGEN 290 FT /note="S->A: Decreased demethylation activity." FT /evidence="ECO:0000269|PubMed:29233856" FT MUTAGEN 298 FT /note="Y->A: Decreased demethylation activity." FT /evidence="ECO:0000269|PubMed:29233856" FT MUTAGEN 309 FT /note="H->A: Loss of demethylation activity." FT /evidence="ECO:0000269|PubMed:29233856" FT MUTAGEN 311 FT /note="E->A: Loss of demethylation activity." FT /evidence="ECO:0000269|PubMed:29233856" FT MUTAGEN 312 FT /note="D->A: Decreased demethylation activity." FT /evidence="ECO:0000269|PubMed:29233856" FT MUTAGEN 363 FT /note="V->A: Decreased demethylation activity." FT /evidence="ECO:0000269|PubMed:29233856" FT MUTAGEN 387 FT /note="E->K: In jmj14-3; loss of transgenic photobleaching FT phenotype due to RNA silencing." FT /evidence="ECO:0000269|PubMed:20478993" FT MUTAGEN 397 FT /note="H->A: Loss of demethylation activity." FT /evidence="ECO:0000269|PubMed:20177424, FT ECO:0000269|PubMed:29233856" FT MUTAGEN 516 FT /note="E->A: Decreased activity." FT /evidence="ECO:0000269|PubMed:29233856" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 63..66 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 69..80 FT /evidence="ECO:0007829|PDB:5YKN" FT TURN 81..83 FT /evidence="ECO:0007829|PDB:5YKN" FT STRAND 84..88 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 99..101 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 103..106 FT /evidence="ECO:0007829|PDB:5YKN" FT STRAND 114..117 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 118..120 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 179..194 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 214..226 FT /evidence="ECO:0007829|PDB:5YKN" FT STRAND 233..241 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 242..245 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 260..266 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 271..274 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 281..284 FT /evidence="ECO:0007829|PDB:5YKN" FT TURN 291..293 FT /evidence="ECO:0007829|PDB:5YKN" FT STRAND 296..300 FT /evidence="ECO:0007829|PDB:5YKN" FT STRAND 305..309 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 312..314 FT /evidence="ECO:0007829|PDB:5YKN" FT STRAND 316..325 FT /evidence="ECO:0007829|PDB:5YKN" FT STRAND 327..331 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 334..336 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 337..347 FT /evidence="ECO:0007829|PDB:5YKN" FT STRAND 351..354 FT /evidence="ECO:0007829|PDB:5YKN" FT TURN 359..361 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 368..373 FT /evidence="ECO:0007829|PDB:5YKN" FT STRAND 379..383 FT /evidence="ECO:0007829|PDB:5YKN" FT STRAND 388..391 FT /evidence="ECO:0007829|PDB:5YKN" FT STRAND 397..412 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 415..417 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 418..431 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 439..458 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 465..471 FT /evidence="ECO:0007829|PDB:5YKN" FT STRAND 475..477 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 479..497 FT /evidence="ECO:0007829|PDB:5YKN" FT STRAND 504..506 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 509..511 FT /evidence="ECO:0007829|PDB:5YKO" FT STRAND 512..515 FT /evidence="ECO:0007829|PDB:5YKO" FT TURN 520..522 FT /evidence="ECO:0007829|PDB:5YKN" FT STRAND 527..536 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 543..545 FT /evidence="ECO:0007829|PDB:5YKN" FT TURN 554..556 FT /evidence="ECO:0007829|PDB:5YKN" FT STRAND 557..563 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 565..575 FT /evidence="ECO:0007829|PDB:5YKN" FT HELIX 579..586 FT /evidence="ECO:0007829|PDB:5YKN" SQ SEQUENCE 954 AA; 108156 MW; 551B17E4D6FF336A CRC64; MDQLASLAES VAMEEDSEKQ SIKGESSLEP DSTPSSPKIT ARWNPSEACR PLVDDAPIFY PTNEDFDDPL GYIEKLRSKA ESYGICRIVP PVAWRPPCPL KEKKIWENSK FPTRIQFIDL LQNREPIKKS TKTKKRKRRR ISKIGYTRRK RDSGCDTASS GSSDSEGKFG FQTGPDFTLE EFQKYDEYFK ECYFQSEDHP GSKASENKKF KPKVKDLEGE YWRIVEQATD EVEVYYGADL ETKKFGSGFP KYKPGYPISE ADQYSQCGWN LNNLSRLPGS VLAFESCDIS GVIVPWLYVG MCFSTFCWHV EDHHLYSMNY LHTGDPKVWY GIPGNHAESF ENVMKKRLPD LFEEQPDLLH QLVTQLSPRI LKEEGVPVYR AVQRSGEFIL TFPKAYHSGF NCGFNCAEAV NVAPVDWLVH GQNAVEGYSK QRRKSSLSHD KLLLGAAMEA TYCLWELSLS KKKTPVIARW KRVCSEDGLL TKAVKKRVQM EEERLNHLQD GFSLRKMEGD FDNKRERECF LCFYDLHMSA SSCKCSPNRF ACLIHAKDLC SCESKDRYIL IRHTLDELWA LVRALEGDLD AIDLWASKCR DQYPSQHPRA REYAYLKSAP CIKSRGSSKV QQREQNNLQL VSERLQSDLT SNKEVQLKQD GDSDVNRHGH ESERNHVHGI TDKSAVTDVK LGVGGKFDEK KISVESQNPH SVSDVGCSEL AKKVDGCLGG KDQNAATNRL SLSVELLSSG SLVVKKLWCS KQAIYPKGFK SRVKFLSVLD PTNLTNYISE VLDAGLLGPL FRVSVEDYPT ENFSNVSAEK CWQMVTQRLK LEIIKKCDQP VSSLTSLQPL ESINGLEMFG FLSPHVIKVV EALDPKHQLE EYWNQKAVKL FGAEPIKEGE KDDTEKGGAS DPSLDRDTRL LRGLLKKATP EELVMMHGLL CGETRNTELK EELSTLVDKM EISP //