JMJ14_ARATH
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 03-AUG-2022, entry version 136.
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},
GN PKDM7B {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};
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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.AT4G20400.1; -.
DR iPTMnet; Q8GUI6; -.
DR PaxDb; Q8GUI6; -.
DR PRIDE; Q8GUI6; -.
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; locus:2128659; AT4G20400.
DR eggNOG; KOG1246; Eukaryota.
DR InParanoid; Q8GUI6; -.
DR OMA; FEKCDIS; -.
DR PhylomeDB; Q8GUI6; -.
DR PRO; PR:Q8GUI6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GUI6; baseline and differential.
DR Genevisible; Q8GUI6; AT.
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:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0032453; F:histone H3-methyl-lysine-4 demethylase activity; IDA:TAIR.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; IBA:GO_Central.
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:0006338; P:chromatin remodeling; IBA:GO_Central.
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; IDA:CACAO.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
DR GO; GO:0062034; P:L-pipecolic acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010216; P:maintenance of DNA methylation; IMP:TAIR.
DR GO; GO:1905642; P:negative regulation of DNA methylation; 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:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0048573; P:photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:0099402; P:plant organ development; IMP:UniProtKB.
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:0044030; P:regulation of DNA methylation; IMP:UniProtKB.
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:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
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 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 PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
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
