CDF1_ARATH
ID CDF1_ARATH Reviewed; 298 AA.
AC Q8W1E3; Q4ACT9; Q9FJJ9;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cyclic dof factor 1;
DE AltName: Full=Dof zinc finger protein DOF5.5;
DE Short=AtDOF5.5;
GN Name=CDF1; Synonyms=DOF5.5; OrderedLocusNames=At5g62430;
GN ORFNames=K19B1.4, MMI9.24;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DNA-BINDING, INTERACTION
RP WITH ADO3, INDUCTION, MUTAGENESIS OF LYS-253, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=16002617; DOI=10.1126/science.1110586;
RA Imaizumi T., Schultz T.F., Harmon F.G., Ho L.A., Kay S.A.;
RT "FKF1 F-box protein mediates cyclic degradation of a repressor of CONSTANS
RT in Arabidopsis.";
RL Science 309:293-297(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12475498; DOI=10.1016/s1360-1385(02)02362-2;
RA Yanagisawa S.;
RT "The Dof family of plant transcription factors.";
RL Trends Plant Sci. 7:555-560(2002).
RN [6]
RP INTERACTION WITH GI.
RX PubMed=17872410; DOI=10.1126/science.1146994;
RA Sawa M., Nusinow D.A., Kay S.A., Imaizumi T.;
RT "FKF1 and GIGANTEA complex formation is required for day-length measurement
RT in Arabidopsis.";
RL Science 318:261-265(2007).
RN [7]
RP FUNCTION.
RX PubMed=19619493; DOI=10.1016/j.devcel.2009.06.015;
RA Fornara F., Panigrahi K.C., Gissot L., Sauerbrunn N., Ruehl M.,
RA Jarillo J.A., Coupland G.;
RT "Arabidopsis DOF transcription factors act redundantly to reduce CONSTANS
RT expression and are essential for a photoperiodic flowering response.";
RL Dev. Cell 17:75-86(2009).
RN [8]
RP FUNCTION.
RX PubMed=22628657; DOI=10.1126/science.1219644;
RA Song Y.H., Smith R.W., To B.J., Millar A.J., Imaizumi T.;
RT "FKF1 conveys timing information for CONSTANS stabilization in
RT photoperiodic flowering.";
RL Science 336:1045-1049(2012).
CC -!- FUNCTION: Transcription factor that binds specifically to a 5'-AA[AG]G-
CC 3' consensus core sequence. A flanking TGT sequence contributes to the
CC specificity of binding. Regulates a photoperiodic flowering response.
CC Transcriptional repressor of 'CONSTANS' expression. The DNA-binding
CC ability is not modulated by 'GIGANTEA' but the stability of CDF1 is
CC controlled by the proteasome-dependent pathway. Ubiquitinated by the
CC SCF(ADO3) E3 ubiquitin ligase complex. Binds to the FT promoter in the
CC morning. {ECO:0000269|PubMed:16002617, ECO:0000269|PubMed:19619493,
CC ECO:0000269|PubMed:22628657}.
CC -!- SUBUNIT: Interacts with ADO2 (via kelch repeats), ADO3 (via kelch
CC repeats) and GI (via N-terminus). {ECO:0000269|PubMed:16002617,
CC ECO:0000269|PubMed:17872410}.
CC -!- INTERACTION:
CC Q8W1E3; Q8W420: ADO2; NbExp=2; IntAct=EBI-1536051, EBI-1015688;
CC Q8W1E3; Q9C9W9: ADO3; NbExp=2; IntAct=EBI-1536051, EBI-401228;
CC Q8W1E3; Q9SQI2: GI; NbExp=3; IntAct=EBI-1536051, EBI-446380;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00071,
CC ECO:0000269|PubMed:16002617}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8W1E3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8W1E3-2; Sequence=VSP_011870;
CC -!- TISSUE SPECIFICITY: Expressed in the vascular tissues of cotyledons,
CC leaves and hypocotyls and in stomata. Not detected in roots.
CC {ECO:0000269|PubMed:16002617}.
CC -!- INDUCTION: Circadian-regulation at the protein level, but not at the
CC mRNA level. Strongly decreased expression during the dark phase.
CC Accumulates at high levels at the beginning of the day.
CC {ECO:0000269|PubMed:16002617}.
CC -!- PTM: Ubiquitinated. {ECO:0000305}.
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DR EMBL; AB231333; BAE16983.1; -; mRNA.
DR EMBL; AB015469; BAB11493.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97607.1; -; Genomic_DNA.
DR EMBL; AF446362; AAL48235.1; -; mRNA.
DR EMBL; AY143830; AAN28769.1; -; mRNA.
DR RefSeq; NP_201049.3; NM_125637.4. [Q8W1E3-1]
DR AlphaFoldDB; Q8W1E3; -.
DR BioGRID; 21608; 9.
DR IntAct; Q8W1E3; 18.
DR STRING; 3702.AT5G62430.1; -.
DR PaxDb; Q8W1E3; -.
DR PRIDE; Q8W1E3; -.
DR ProteomicsDB; 222806; -. [Q8W1E3-1]
DR EnsemblPlants; AT5G62430.1; AT5G62430.1; AT5G62430. [Q8W1E3-1]
DR GeneID; 836364; -.
DR Gramene; AT5G62430.1; AT5G62430.1; AT5G62430. [Q8W1E3-1]
DR KEGG; ath:AT5G62430; -.
DR Araport; AT5G62430; -.
DR TAIR; locus:2154079; AT5G62430.
DR eggNOG; ENOG502SJI0; Eukaryota.
DR HOGENOM; CLU_030533_1_1_1; -.
DR OMA; KTIGMTQ; -.
DR OrthoDB; 853832at2759; -.
DR PhylomeDB; Q8W1E3; -.
DR PRO; PR:Q8W1E3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8W1E3; baseline and differential.
DR Genevisible; Q8W1E3; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR InterPro; IPR045174; Dof.
DR InterPro; IPR003851; Znf_Dof.
DR PANTHER; PTHR31089; PTHR31089; 2.
DR Pfam; PF02701; zf-Dof; 1.
DR PROSITE; PS01361; ZF_DOF_1; 1.
DR PROSITE; PS50884; ZF_DOF_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Flowering; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..298
FT /note="Cyclic dof factor 1"
FT /id="PRO_0000074295"
FT ZN_FING 54..108
FT /note="Dof-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT REGION 27..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT VAR_SEQ 1..61
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_011870"
FT MUTAGEN 253
FT /note="K->A: Reduced binding to ADO3 and increased
FT stability."
FT /evidence="ECO:0000269|PubMed:16002617"
FT CONFLICT 84
FT /note="C -> Y (in Ref. 4; AAL48235/AAN28769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 33639 MW; 683CEB24D4F22D75 CRC64;
MLETKDPAIK LFGMKIPFPT VLEVADEEEE KNQNKTLTDQ SEKDKTLKKP TKILPCPRCN
SMETKFCYYN NYNVNQPRHF CKACQRYWTS GGTMRSVPIG AGRRKNKNNS PTSHYHHVTI
SETNGPVLSF SLGDDQKVSS NRFGNQKLVA RIENNDERSN NNTSNGLNCF PGVSWPYTWN
PAFYPVYPYW SMPVLSSPVS SSPTSTLGKH SRDEDETVKQ KQRNGSVLVP KTLRIDDPNE
AAKSSIWTTL GIKNEVMFNG FGSKKEVKLS NKEETETSLV LCANPAALSR SINFHEQM
