FLD_ARATH
ID FLD_ARATH Reviewed; 789 AA.
AC Q9CAE3; F4J3R3; Q58T18; Q9SS50;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protein FLOWERING LOCUS D {ECO:0000303|PubMed:14593187, ECO:0000303|PubMed:15911588, ECO:0000303|PubMed:17996704};
DE EC=1.-.-.-;
DE AltName: Full=Protein SUPPRESSOR OF OVEREXPRESSED FCA 1 {ECO:0000303|PubMed:17996704};
GN Name=FLD {ECO:0000303|PubMed:14593187, ECO:0000303|PubMed:15911588,
GN ECO:0000303|PubMed:17996704}; Synonyms=SOF1 {ECO:0000303|PubMed:17996704};
GN OrderedLocusNames=At3g10390 {ECO:0000312|Araport:AT3G10390};
GN ORFNames=F13M14.34 {ECO:0000312|EMBL:AAG51395.1},
GN F14P13.1 {ECO:0000312|EMBL:AAF02805.1};
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 [GENOMIC DNA], AND VARIANTS THR-640 AND LEU-686.
RC STRAIN=cv. Landsberg erecta, and cv. Lz-0;
RX PubMed=15911588; DOI=10.1534/genetics.104.036533;
RA Werner J.D., Borevitz J.O., Uhlenhaut N.H., Ecker J.R., Chory J.,
RA Weigel D.;
RT "FRIGIDA-independent variation in flowering time of natural Arabidopsis
RT thaliana accessions.";
RL Genetics 170:1197-1207(2005).
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 FUNCTION.
RX PubMed=14593187; DOI=10.1126/science.1091109;
RA He Y., Michaels S.D., Amasino R.M.;
RT "Regulation of flowering time by histone acetylation in Arabidopsis.";
RL Science 302:1751-1754(2003).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF PRO-428.
RX PubMed=17996704; DOI=10.1016/j.molcel.2007.10.018;
RA Liu F., Quesada V., Crevillen P., Baeurle I., Swiezewski S., Dean C.;
RT "The Arabidopsis RNA-binding protein FCA requires a lysine-specific
RT demethylase 1 homolog to downregulate FLC.";
RL Mol. Cell 28:398-407(2007).
RN [6]
RP FUNCTION.
RX PubMed=17921315; DOI=10.1105/tpc.107.052373;
RA Jiang D., Yang W., He Y., Amasino R.M.;
RT "Arabidopsis relatives of the human lysine-specific demethylase1 repress
RT the expression of FWA and FLOWERING LOCUS C and thus promote the floral
RT transition.";
RL Plant Cell 19:2975-2987(2007).
RN [7]
RP SUMOYLATION AT LYS-287; LYS-693 AND LYS-770, AND MUTAGENESIS OF LYS-287;
RP LYS-693 AND LYS-770.
RX PubMed=18069938; DOI=10.1111/j.1365-313x.2007.03359.x;
RA Jin J.B., Jin Y.H., Lee J., Miura K., Yoo C.Y., Kim W.Y., Van Oosten M.,
RA Hyun Y., Somers D.E., Lee I., Yun D.J., Bressan R.A., Hasegawa P.M.;
RT "The SUMO E3 ligase, AtSIZ1, regulates flowering by controlling a salicylic
RT acid-mediated floral promotion pathway and through affects on FLC chromatin
RT structure.";
RL Plant J. 53:530-540(2008).
RN [8]
RP FUNCTION, AND INTERACTION WITH HDA6.
RX PubMed=21398257; DOI=10.1104/pp.111.174417;
RA Yu C.-W., Liu X., Luo M., Chen C., Lin X., Tian G., Lu Q., Cui Y., Wu K.;
RT "HISTONE DEACETYLASE6 interacts with FLOWERING LOCUS D and regulates
RT flowering in Arabidopsis.";
RL Plant Physiol. 156:173-184(2011).
RN [9]
RP FUNCTION.
RX PubMed=25922987; DOI=10.1111/tpj.12868;
RA Luo M., Tai R., Yu C.W., Yang S., Chen C.Y., Lin W.D., Schmidt W., Wu K.;
RT "Regulation of flowering time by the histone deacetylase HDA5 in
RT Arabidopsis.";
RL Plant J. 82:925-936(2015).
RN [10]
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).
CC -!- FUNCTION: Probable histone demethylase that promotes flowering
CC independently of the photoperiod and vernalization pathways by
CC repressing FLOWERING LOCUS C (FLC), a floral repressor that blocks the
CC transition from vegetative to reproductive development. Probably
CC mediates histone H3 'Lys-4' demethylation at FLC locus. Seems to act in
CC partial redundancy with LDL1 and LDL2 to repress FLC expression.
CC Required for histone H4 deacetylation of FLC locus. May be a component
CC of the histone deacetylase complex. Forms a histone deacetylase complex
CC with HDA5, HDA6 and MSI4/FVE that represses FLC gene expression to
CC control flowering time (PubMed:21398257, PubMed:25922987). Required for
CC systemic acquired resistance (SAR) toward pathogenic bacteria (e.g.
CC Pseudomonas syringae pv tomato DC3000 (avrPto)) (PubMed:32392578).
CC Together with FLD and MSI4/FVE, contributes to dehydroabietinal-
CC dependent (DA, a diterpenoid tricyclic diterpene) activation of
CC flowering ans SAR (PubMed:32392578). {ECO:0000269|PubMed:14593187,
CC ECO:0000269|PubMed:17921315, ECO:0000269|PubMed:17996704,
CC ECO:0000269|PubMed:21398257, ECO:0000269|PubMed:25922987,
CC ECO:0000269|PubMed:32392578}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with HDA6. {ECO:0000269|PubMed:21398257}.
CC -!- INDUCTION: Induced by dehydroabietinal-dependent (DA), a diterpenoid
CC tricyclic diterpene that promotes flowering and systemic acquired
CC resistance (SAR). {ECO:0000269|PubMed:32392578}.
CC -!- PTM: Sumoylated at Lys-287, Lys-693 and Lys-770 by SIZ1. Sumoylation
CC alters its activity and the histone H4 acetylation status of FLC locus,
CC promoting FLC expression. {ECO:0000269|PubMed:18069938}.
CC -!- DISRUPTION PHENOTYPE: Delayed flowering (PubMed:32392578). Impaired
CC systemic acquired resistance (SAR) toward pathogenic bacteria (e.g.
CC Pseudomonas syringae pv tomato DC3000 (avrPto)) (PubMed:32392578). Lost
CC ability of dehydroabietinal-dependent (DA, a diterpenoid tricyclic
CC diterpene) to trigger flowering and systemic acquired resistance (SAR)
CC (PubMed:32392578). {ECO:0000269|PubMed:32392578}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF02805.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AEE74899.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY849996; AAX51266.1; -; Genomic_DNA.
DR EMBL; AY849997; AAX51267.1; -; Genomic_DNA.
DR EMBL; AC009400; AAF02805.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC011560; AAG51395.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74899.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; ANM64276.1; -; Genomic_DNA.
DR RefSeq; NP_001326316.1; NM_001337874.1.
DR RefSeq; NP_187650.4; NM_111874.4.
DR AlphaFoldDB; Q9CAE3; -.
DR SMR; Q9CAE3; -.
DR BioGRID; 5536; 2.
DR STRING; 3702.AT3G10390.1; -.
DR PaxDb; Q9CAE3; -.
DR PRIDE; Q9CAE3; -.
DR ProteomicsDB; 230780; -.
DR EnsemblPlants; AT3G10390.4; AT3G10390.4; AT3G10390.
DR GeneID; 820202; -.
DR Gramene; AT3G10390.4; AT3G10390.4; AT3G10390.
DR KEGG; ath:AT3G10390; -.
DR Araport; AT3G10390; -.
DR TAIR; locus:2075870; AT3G10390.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_5_0_1; -.
DR InParanoid; Q9CAE3; -.
DR OMA; IVHTIRY; -.
DR PhylomeDB; Q9CAE3; -.
DR PRO; PR:Q9CAE3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9CAE3; baseline and differential.
DR Genevisible; Q9CAE3; AT.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IMP:TAIR.
DR GO; GO:2000028; P:regulation of photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IMP:UniProtKB.
DR GO; GO:1904629; P:response to diterpene; IMP:UniProtKB.
DR GO; GO:0009627; P:systemic acquired resistance; IMP:UniProtKB.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF04433; SWIRM; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; FAD; Flavoprotein; Isopeptide bond; Oxidoreductase;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..789
FT /note="Protein FLOWERING LOCUS D"
FT /id="PRO_0000342895"
FT DOMAIN 76..177
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 195
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT BINDING 214
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT BINDING 216
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT BINDING 222
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT BINDING 240..243
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT BINDING 595
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT BINDING 604..605
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT BINDING 607..612
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 693
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT CROSSLNK 770
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT VARIANT 640
FT /note="A -> T (in strain: cv. Lz-0)"
FT VARIANT 686
FT /note="R -> L (in strain: cv. Lz-0)"
FT /evidence="ECO:0000269|PubMed:15911588"
FT MUTAGEN 287
FT /note="K->R: Loss of sumoylation; when associated with R-
FT 693 and R-770."
FT /evidence="ECO:0000269|PubMed:15911588"
FT MUTAGEN 428
FT /note="P->L: In sof1/fld-6; weak allele that suppresses the
FT down-regulation of FLC by FCA."
FT /evidence="ECO:0000269|PubMed:18069938"
FT MUTAGEN 693
FT /note="K->R: Loss of sumoylation; when associated with R-
FT 287 and R-770."
FT /evidence="ECO:0000269|PubMed:17996704"
FT MUTAGEN 770
FT /note="K->R: Loss of sumoylation; when associated with R-
FT 287 and R-693."
FT /evidence="ECO:0000269|PubMed:18069938"
SQ SEQUENCE 789 AA; 86037 MW; 937FCFCF0E7A8EFF CRC64;
MVSFSAPKKR RRGRSQRSMS SLNSLPVPNV GLLPGNSNFV SSSASSSGRF NVEVVNGSNQ
TVKSYPGIGD EIITINKEAT TEALLALTAG FPADSLTEEE IEFGVVPIVG GIEQVNYILI
RNHIISKWRE NISSWVTKEM FLNSIPKHCS SLLDSAYNYL VTHGYINFGI AQAIKDKFPA
QSSKSSVIIV GAGLSGLAAA RQLMRFGFKV TVLEGRKRPG GRVYTKKMEA NRVGAAADLG
GSVLTGTLGN PLGIIARQLG SSLYKVRDKC PLYRVDGKPV DPDVDIKVEV AFNQLLDKAS
KLRQLMGDVS MDVSLGAALE TFRQVSGNDV ATEEMGLFNW HLANLEYANA GLVSKLSLAF
WDQDDPYDMG GDHCFLPGGN GRLVQALAEN VPILYEKTVQ TIRYGSNGVK VTAGNQVYEG
DMVLCTVPLG VLKNGSIKFV PELPQRKLDC IKRLGFGLLN KVAMLFPYVF WSTDLDTFGH
LTEDPNYRGE FFLFYSYAPV AGGALLIALV AGEAAHKFET MPPTDAVTRV LHILRGIYEP
QGINVPDPLQ TVCTRWGGDP FSLGSYSNVA VGASGDDYDI LAESVGDGRL FFAGEATTRR
YPATMHGAFV TGLREAANMA QSAKARGIRK RIDRNPSRNA HSCAILLADL FRDPDLEFGS
FCIIFSRRNP DPKSPAILRV TLSEPRKRNE DPKADQHSNK ILFQQLQSHF NQQQQIQVYT
LLTRQQALDL REVRGGDEKR LYYLCETLGV KLVGRKGLGV GADSVIASIK AERTGRKLPS
SSTSGTKSG
