DOF24_ARATH
ID DOF24_ARATH Reviewed; 330 AA.
AC O80928; A2RVM3; C0SV78;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Dof zinc finger protein DOF2.4 {ECO:0000303|PubMed:12475498};
DE Short=AtDOF2.4 {ECO:0000303|PubMed:12475498};
DE AltName: Full=Protein PHLOEM EARLY DOF 1 {ECO:0000303|PubMed:30626969};
GN Name=DOF2.4 {ECO:0000303|PubMed:12475498};
GN Synonyms=PEAR1 {ECO:0000303|PubMed:30626969};
GN OrderedLocusNames=At2g37590 {ECO:0000312|Araport:AT2G37590};
GN ORFNames=F13M22.9 {ECO:0000312|EMBL:AAC23629.1};
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 [MRNA].
RA Fujita M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=17583520; DOI=10.1016/j.plaphy.2007.05.001;
RA Konishi M., Yanagisawa S.;
RT "Sequential activation of two Dof transcription factor gene promoters
RT during vascular development in Arabidopsis thaliana.";
RL Plant Physiol. Biochem. 45:623-629(2007).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION BY CYTOKININ,
RP AND SUBCELLULAR LOCATION.
RX PubMed=30626969; DOI=10.1038/s41586-018-0839-y;
RA Miyashima S., Roszak P., Sevilem I., Toyokura K., Blob B., Heo J.-O.,
RA Mellor N., Help-Rinta-Rahko H., Otero S., Smet W., Boekschoten M.,
RA Hooiveld G., Hashimoto K., Smetana O., Siligato R., Wallner E.-S.,
RA Maehoenen A.P., Kondo Y., Melnyk C.W., Greb T., Nakajima K., Sozzani R.,
RA Bishopp A., De Rybel B., Helariutta Y.;
RT "Mobile PEAR transcription factors integrate positional cues to prime
RT cambial growth.";
RL Nature 565:490-494(2019).
CC -!- FUNCTION: Transcription factor that binds specifically to a 5'-AA[AG]G-
CC 3' consensus core sequence (By similarity). Probably involved in early
CC processes for vascular development (PubMed:17583520). The PEAR proteins
CC (e.g. DOF2.4, DOF5.1, DOF3.2, DOF1.1, DOF5.6 and DOF5.3) activate gene
CC expression that promotes radial growth of protophloem sieve elements.
CC Triggers the transcription of HD-ZIP III genes, especially in the
CC central domain of vascular tissue (PubMed:30626969).
CC {ECO:0000250|UniProtKB:Q9M2U1, ECO:0000269|PubMed:17583520,
CC ECO:0000269|PubMed:30626969}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00071}.
CC Symplast {ECO:0000269|PubMed:30626969}. Note=Mobile protein observed in
CC symplastic trafficking; movements are repressed by HD-ZIP III proteins.
CC {ECO:0000269|PubMed:30626969}.
CC -!- TISSUE SPECIFICITY: Specific to the vascular tissues (PubMed:17583520).
CC The PEAR proteins (e.g. DOF2.4, DOF5.1, DOF3.2, DOF1.1, DOF5.6 and
CC DOF5.3) form a short-range concentration gradient that peaks at
CC protophloem sieve elements (PSE) (PubMed:30626969).
CC {ECO:0000269|PubMed:17583520, ECO:0000269|PubMed:30626969}.
CC -!- DEVELOPMENTAL STAGE: Specific to the midveins, containing narrow
CC procambial cell files. Expressed in procambial cells of leaf primordia,
CC roots and embryos, prior to the completion of xylem differentiation.
CC {ECO:0000269|PubMed:17583520}.
CC -!- INDUCTION: By cytokinin in procambium. Antagonized by the HD-ZIP III
CC proteins and by mobile miR165 and miR166 microRNAs.
CC {ECO:0000269|PubMed:30626969}.
CC -!- DISRUPTION PHENOTYPE: The pear1 pear2 tmo6 triple mutant variably
CC displays reduced radial growth. The pear1 pear2 dof6 tmo6 quadruple
CC mutant plants showed a greater uniform reduction in radial growth,
CC associated with compromised symplastic trafficking.
CC {ECO:0000269|PubMed:30626969}.
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DR EMBL; AB493581; BAH30419.1; -; mRNA.
DR EMBL; AC004684; AAC23629.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09422.1; -; Genomic_DNA.
DR EMBL; BT030014; ABN04752.1; -; mRNA.
DR PIR; T02525; T02525.
DR RefSeq; NP_181295.1; NM_129315.4.
DR AlphaFoldDB; O80928; -.
DR BioGRID; 3680; 1.
DR STRING; 3702.AT2G37590.1; -.
DR iPTMnet; O80928; -.
DR PaxDb; O80928; -.
DR PRIDE; O80928; -.
DR ProteomicsDB; 222109; -.
DR EnsemblPlants; AT2G37590.1; AT2G37590.1; AT2G37590.
DR GeneID; 818336; -.
DR Gramene; AT2G37590.1; AT2G37590.1; AT2G37590.
DR KEGG; ath:AT2G37590; -.
DR Araport; AT2G37590; -.
DR TAIR; locus:2040746; AT2G37590.
DR eggNOG; ENOG502QTHW; Eukaryota.
DR HOGENOM; CLU_036438_0_3_1; -.
DR InParanoid; O80928; -.
DR OMA; IHMGASG; -.
DR OrthoDB; 1130450at2759; -.
DR PhylomeDB; O80928; -.
DR PRO; PR:O80928; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80928; baseline and differential.
DR Genevisible; O80928; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0055044; C:symplast; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0010497; P:plasmodesmata-mediated intercellular transport; IDA:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0090057; P:root radial pattern formation; IGI:TAIR.
DR InterPro; IPR045174; Dof.
DR InterPro; IPR003851; Znf_Dof.
DR PANTHER; PTHR31992; PTHR31992; 1.
DR Pfam; PF02701; zf-Dof; 1.
DR PROSITE; PS01361; ZF_DOF_1; 1.
DR PROSITE; PS50884; ZF_DOF_2; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..330
FT /note="Dof zinc finger protein DOF2.4"
FT /id="PRO_0000074275"
FT ZN_FING 89..143
FT /note="Dof-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT REGION 14..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
SQ SEQUENCE 330 AA; 35331 MW; 6CECD2C0D2EB1DD3 CRC64;
MVFSSIQAYL DSSNWQQAPP SNYNHDGTGA SANGGHVLRP QLQPQQQPQQ QPHPNGSGGG
GGGGGGSIRA GSMVDRARQA NVALPEAALK CPRCESTNTK FCYFNNYSLT QPRHFCKTCR
RYWTRGGALR NVPVGGGCRR NRRTKSNSNN NNNSTATSNN TSFSSGNAST ISTILSSHYG
GNQESILSQI LSPARLMNPT YNHLGDLTSN TKTDNNMSLL NYGGLSQDLR SIHMGASGGS
LMSCVDEWRS ASYHQQSSMG GGNLEDSSNP NPSANGFYSF ESPRITSASI SSALASQFSS
VKVEDNPYKW VNVNGNCSSW NDLSAFGSSR
