FD_ARATH
ID FD_ARATH Reviewed; 285 AA.
AC Q84JK2; O65627; Q84JC9; Q84K49; Q84K53;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein FD {ECO:0000303|PubMed:16099980};
DE AltName: Full=bZIP transcription factor 14 {ECO:0000303|PubMed:11906833};
DE Short=AtbZIP14 {ECO:0000303|PubMed:11906833};
GN Name=FD {ECO:0000303|PubMed:16099980};
GN Synonyms=BZIP14 {ECO:0000303|PubMed:11906833};
GN OrderedLocusNames=At4g35900 {ECO:0000312|Araport:AT4G35900};
GN ORFNames=F4B14.170 {ECO:0000312|EMBL:CAA21476.1},
GN T19K4.30 {ECO:0000312|EMBL:CAA18484.1};
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 / MRNA], VARIANTS VAL-13; ASN-112; CYS-141
RP AND ASP-161, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FDP/BZIP27
RP AND FT, TISSUE SPECIFICITY, AND MUTAGENESIS OF THR-282 AND
RP 279-ARG--PHE-285.
RC STRAIN=cv. Columbia, cv. Cvi-1, cv. Landsberg erecta, cv. No-0, and
RC cv. Wassilewskija;
RX PubMed=16099979; DOI=10.1126/science.1115983;
RA Abe M., Kobayashi Y., Yamamoto S., Daimon Y., Yamaguchi A., Ikeda Y.,
RA Ichinoki H., Notaguchi M., Goto K., Araki T.;
RT "FD, a bZIP protein mediating signals from the floral pathway integrator FT
RT at the shoot apex.";
RL Science 309:1052-1056(2005).
RN [2]
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 [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 IDENTIFICATION.
RX PubMed=12084834; DOI=10.1105/tpc.000869;
RA Bensmihen S., Rippa S., Lambert G., Jublot D., Pautot V., Granier F.,
RA Giraudat J., Parcy F.;
RT "The homologous ABI5 and EEL transcription factors function
RT antagonistically to fine-tune gene expression during late embryogenesis.";
RL Plant Cell 14:1391-1403(2002).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11906833; DOI=10.1016/s1360-1385(01)02223-3;
RA Jakoby M., Weisshaar B., Droege-Laser W., Vicente-Carbajosa J.,
RA Tiedemann J., Kroj T., Parcy F.;
RT "bZIP transcription factors in Arabidopsis.";
RL Trends Plant Sci. 7:106-111(2002).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH FT.
RX PubMed=16099980; DOI=10.1126/science.1114358;
RA Wigge P.A., Kim M.C., Jaeger K.-E., Busch W., Schmid M., Lohmann J.U.,
RA Weigel D.;
RT "Integration of spatial and temporal information during floral induction in
RT Arabidopsis.";
RL Science 309:1056-1059(2005).
RN [7]
RP MUTAGENESIS OF THR-276; LEU-277 AND THR-282, PHOSPHORYLATION AT THR-282,
RP INTERACTION WITH FT; CPK6; CPK33; GRF3 AND GRF4, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=25661797; DOI=10.1038/srep08341;
RA Kawamoto N., Sasabe M., Endo M., Machida Y., Araki T.;
RT "Calcium-dependent protein kinases responsible for the phosphorylation of a
RT bZIP transcription factor FD crucial for the florigen complex formation.";
RL Sci. Rep. 5:8341-8341(2015).
CC -!- FUNCTION: Transcription factor required for the transition to flowering
CC promoted by FT. {ECO:0000269|PubMed:16099979,
CC ECO:0000269|PubMed:16099980}.
CC -!- SUBUNIT: Self-interacts (PubMed:16099979). Interacts with FT and
CC FDP/BZIP27 (PubMed:16099979, PubMed:16099980, PubMed:25661797).
CC Interacts with GRF3 and GRF4, and in a calcium-independent manner, with
CC CPK6 and CPK33 (PubMed:25661797). {ECO:0000269|PubMed:16099979,
CC ECO:0000269|PubMed:16099980, ECO:0000269|PubMed:25661797}.
CC -!- INTERACTION:
CC Q84JK2; Q9SXZ2: FT; NbExp=4; IntAct=EBI-636507, EBI-636490;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:16099979, ECO:0000269|PubMed:25661797}.
CC -!- TISSUE SPECIFICITY: Highly expressed in shoot apex.
CC {ECO:0000269|PubMed:16099979, ECO:0000269|PubMed:16099980,
CC ECO:0000269|PubMed:25661797}.
CC -!- PTM: Phosphorylated at Thr-282 in a calcium-dependent manner by CPK6
CC and CPK33. {ECO:0000269|PubMed:25661797}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18484.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA21476.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81499.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB105818; BAC65864.1; -; mRNA.
DR EMBL; AB105819; BAC65865.1; -; mRNA.
DR EMBL; AB105820; BAC65866.1; -; mRNA.
DR EMBL; AB105821; BAC65867.1; -; mRNA.
DR EMBL; AB105822; BAC65868.1; -; mRNA.
DR EMBL; AB105823; BAC65869.1; -; Genomic_DNA.
DR EMBL; AB105824; BAC65870.1; -; Genomic_DNA.
DR EMBL; AB105825; BAC65871.1; -; Genomic_DNA.
DR EMBL; AB105826; BAC65872.1; -; Genomic_DNA.
DR EMBL; AB105827; BAC65873.1; -; Genomic_DNA.
DR EMBL; AL022373; CAA18484.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL031986; CAA21476.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161588; CAB81499.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86586.1; -; Genomic_DNA.
DR EMBL; BN000021; CAD29860.1; -; Genomic_DNA.
DR PIR; T04700; T04700.
DR RefSeq; NP_001329774.1; NM_001342379.1.
DR RefSeq; NP_195315.3; NM_119756.5.
DR AlphaFoldDB; Q84JK2; -.
DR SMR; Q84JK2; -.
DR BioGRID; 15026; 11.
DR IntAct; Q84JK2; 4.
DR STRING; 3702.AT4G35900.1; -.
DR iPTMnet; Q84JK2; -.
DR PaxDb; Q84JK2; -.
DR PRIDE; Q84JK2; -.
DR EnsemblPlants; AT4G35900.1; AT4G35900.1; AT4G35900.
DR GeneID; 829744; -.
DR Gramene; AT4G35900.1; AT4G35900.1; AT4G35900.
DR KEGG; ath:AT4G35900; -.
DR Araport; AT4G35900; -.
DR TAIR; locus:2125349; AT4G35900.
DR eggNOG; ENOG502RZGX; Eukaryota.
DR HOGENOM; CLU_085189_0_0_1; -.
DR InParanoid; Q84JK2; -.
DR OrthoDB; 1354639at2759; -.
DR PhylomeDB; Q84JK2; -.
DR PRO; PR:Q84JK2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q84JK2; baseline and differential.
DR Genevisible; Q84JK2; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0009648; P:photoperiodism; IMP:TAIR.
DR GO; GO:0009911; P:positive regulation of flower development; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0009909; P:regulation of flower development; IGI:TAIR.
DR GO; GO:2000028; P:regulation of photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR043452; BZIP46-like.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR22952; PTHR22952; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..285
FT /note="Protein FD"
FT /id="PRO_0000245359"
FT DOMAIN 214..277
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..235
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 242..263
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 257..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 282
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:25661797"
FT VARIANT 13
FT /note="L -> V (in strain: cv. No-0)"
FT /evidence="ECO:0000269|PubMed:16099979"
FT VARIANT 112
FT /note="K -> N (in strain: cv. Cvi-1 and cv. No-0)"
FT /evidence="ECO:0000269|PubMed:16099979"
FT VARIANT 141
FT /note="Y -> C (in strain: cv. Cvi-1, cv. Landsberg erecta,
FT cv. No-0 and cv. Wassilewskija)"
FT /evidence="ECO:0000269|PubMed:16099979"
FT VARIANT 161
FT /note="E -> D (in strain: cv. Cvi-1 and cv. No-0)"
FT /evidence="ECO:0000269|PubMed:16099979"
FT MUTAGEN 276
FT /note="T->A: No effect on phosphorylation. Loss of
FT phosphorylation; when associated with A-282."
FT /evidence="ECO:0000269|PubMed:25661797"
FT MUTAGEN 277
FT /note="L->Q: Loss of phosphorylation and loss of
FT interaction with FD, GRF3 and GRF4. No effect on
FT interaction with FD, GRF3 and GRF4; when associated with E-
FT 282."
FT /evidence="ECO:0000269|PubMed:25661797"
FT MUTAGEN 279..285
FT /note="Missing: Loss of interaction with FT."
FT /evidence="ECO:0000269|PubMed:16099979"
FT MUTAGEN 282
FT /note="T->A: Loss of phosphorylation and loss of
FT interaction with FT. Loss of phosphorylation; when
FT associated with A-276."
FT /evidence="ECO:0000269|PubMed:16099979,
FT ECO:0000269|PubMed:25661797"
FT MUTAGEN 282
FT /note="T->E: Normal interaction with FT. No effect on
FT interaction with FD, GRF3 and GRF4; when associated with Q-
FT 277."
FT /evidence="ECO:0000269|PubMed:25661797"
FT MUTAGEN 282
FT /note="T->S: Normal interaction with FT."
FT /evidence="ECO:0000269|PubMed:16099979"
SQ SEQUENCE 285 AA; 31377 MW; 9F50BE3364C89D54 CRC64;
MLSSAKHQRN HRLSATNKNQ TLTKVSSISS SSPSSSSSSS STSSSSPLPS QDSQAQKRSL
VTMEEVWNDI NLASIHHLNR HSPHPQHNHE PRFRGQNHHN QNPNSIFQDF LKGSLNQEPA
PTSQTTGSAP NGDSTTVTVL YSSPFPPPAT VLSLNSGAGF EFLDNQDPLV TSNSNLHTHH
HLSNAHAFNT SFEALVPSSS FGKKRGQDSN EGSGNRRHKR MIKNRESAAR SRARKQAYTN
ELELEVAHLQ AENARLKRQQ DQLKMAAAIQ QPKKNTLQRS STAPF
