DOF3_ORYSJ
ID DOF3_ORYSJ Reviewed; 373 AA.
AC Q6K537; C7DQD4; Q9SXG6;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Dof zinc finger protein 3 {ECO:0000305};
DE Short=OsDof3 {ECO:0000303|Ref.1};
DE AltName: Full=Prolamin box-binding factor;
GN Name=DOF3 {ECO:0000303|Ref.1}; Synonyms=RPBF;
GN OrderedLocusNames=Os02g0252400 {ECO:0000312|EMBL:BAF08365.1},
GN LOC_Os02g15350 {ECO:0000305};
GN ORFNames=OSJNBa0009N02.17 {ECO:0000312|EMBL:BAD19767.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Yukihikari; TISSUE=Aleurone;
RA Washio K.;
RT "Molecular analysis of rice cDNAs encoding Dof proteins in germinated
RT aleurone cells.";
RL (er) Plant Gene Register PGR99-107(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 196-319.
RC STRAIN=cv. Nipponbare;
RA Gaur V.S., Singh U.S., Singh V.K., Kumar A.;
RT "Oryza sativa japonica group Dof-type zinc finger protein 03 mRNA, partial
RT cds.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DEVELOPMENTAL STAGE, AND INDUCTION BY GIBBERELLIN.
RX PubMed=11470159; DOI=10.1016/s0167-4781(01)00251-2;
RA Washio K.;
RT "Identification of Dof proteins with implication in the gibberellin-
RT regulated expression of a peptidase gene following the germination of rice
RT grains.";
RL Biochim. Biophys. Acta 1520:54-62(2001).
RN [7]
RP FUNCTION.
RX PubMed=14500792; DOI=10.1104/pp.103.027334;
RA Washio K.;
RT "Functional dissections between GAMYB and Dof transcription factors suggest
RT a role for protein-protein associations in the gibberellin-mediated
RT expression of the RAmy1A gene in the rice aleurone.";
RL Plant Physiol. 133:850-863(2003).
RN [8]
RP FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION BY GIBBERELLIN.
RX PubMed=16798940; DOI=10.1104/pp.106.082826;
RA Yamamoto M.P., Onodera Y., Touno S.M., Takaiwa F.;
RT "Synergism between RPBF Dof and RISBZ1 bZIP activators in the regulation of
RT rice seed expression genes.";
RL Plant Physiol. 141:1694-1707(2006).
RN [9]
RP FUNCTION.
RX PubMed=18980953; DOI=10.1093/jxb/ern265;
RA Kawakatsu T., Yamamoto M.P., Hirose S., Yano M., Takaiwa F.;
RT "Characterization of a new rice glutelin gene GluD-1 expressed in the
RT starchy endosperm.";
RL J. Exp. Bot. 59:4233-4245(2008).
RN [10]
RP FUNCTION, INTERACTION WITH RISBZ1/BZIP58, AND SUBCELLULAR LOCATION.
RX PubMed=19473328; DOI=10.1111/j.1365-313x.2009.03925.x;
RA Kawakatsu T., Yamamoto M.P., Touno S.M., Yasuda H., Takaiwa F.;
RT "Compensation and interaction between RISBZ1 and RPBF during grain filling
RT in rice.";
RL Plant J. 59:908-920(2009).
RN [11]
RP FUNCTION.
RX PubMed=21037241; DOI=10.1093/pcp/pcq164;
RA Kawakatsu T., Takaiwa F.;
RT "Differences in transcriptional regulatory mechanisms functioning for free
RT lysine content and seed storage protein accumulation in rice grain.";
RL Plant Cell Physiol. 51:1964-1974(2010).
CC -!- FUNCTION: Transcriptional activator that binds specifically to the DNA
CC consensus core sequence 5'-AAAG-3' also known as prolamin box
CC (PubMed:16798940). Can activate the expression of genes encoding for
CC the seed storage proteins glutelin, prolamin and globulin. Functions
CC synergistically with RISBZ/BZIP58 to positively regulate quantitatively
CC many seed storage proteins (PubMed:16798940, PubMed:19473328).
CC Functions synergistically with RISBZ1/BZIP58 to positively regulate
CC some metabolic enzymes, such as alanine aminotransferase and pyruvate
CC phosphate dikinase, that are expressed in developing seeds
CC (PubMed:16798940). Functions synergistically with RISBZ1/BZIP58 to
CC positively regulate genes that are key players in the development of
CC aleurone layers (PubMed:19473328). Functions synergistically with
CC RISBZ1/BZIP58 to positively regulate the glutelin GLUD-1 gene in
CC endosperm of developing seeds (PubMed:18980953). Can activate the
CC expression of the bifunctional lysine-degrading enzyme, lysine
CC ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH), one of
CC the key regulators determining free lysine content in plants
CC (PubMed:21037241). In germinating seeds, involved in the gibberellin-
CC mediated activation of the alpha-amylase AMY1.1/AMY1A gene
CC (PubMed:14500792). {ECO:0000269|PubMed:14500792,
CC ECO:0000269|PubMed:16798940, ECO:0000269|PubMed:18980953,
CC ECO:0000269|PubMed:19473328, ECO:0000269|PubMed:21037241}.
CC -!- SUBUNIT: Interacts with RISBZ1/BZIP58. {ECO:0000269|PubMed:19473328}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00071,
CC ECO:0000269|PubMed:19473328}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing seeds from 5 to 30 days
CC after flowering (DAF) (PubMed:16798940). Expressed in germinating seeds
CC up to 5 days after imbibition (PubMed:11470159).
CC {ECO:0000269|PubMed:11470159, ECO:0000269|PubMed:16798940}.
CC -!- INDUCTION: Induced by gibberellin. {ECO:0000269|PubMed:11470159,
CC ECO:0000269|PubMed:16798940}.
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DR EMBL; AB028131; BAA78574.2; -; mRNA.
DR EMBL; AP005510; BAD19767.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF08365.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS77920.1; -; Genomic_DNA.
DR EMBL; GQ183530; ACT31340.1; -; mRNA.
DR RefSeq; XP_015623741.1; XM_015768255.1.
DR AlphaFoldDB; Q6K537; -.
DR STRING; 4530.OS02T0252400-01; -.
DR PaxDb; Q6K537; -.
DR PRIDE; Q6K537; -.
DR EnsemblPlants; Os02t0252400-01; Os02t0252400-01; Os02g0252400.
DR GeneID; 4328903; -.
DR Gramene; Os02t0252400-01; Os02t0252400-01; Os02g0252400.
DR KEGG; osa:4328903; -.
DR eggNOG; ENOG502RB9Y; Eukaryota.
DR HOGENOM; CLU_058543_0_0_1; -.
DR InParanoid; Q6K537; -.
DR OMA; PRYFCRE; -.
DR OrthoDB; 1723828at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW DNA-binding; Germination; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..373
FT /note="Dof zinc finger protein 3"
FT /id="PRO_0000441229"
FT ZN_FING 45..99
FT /note="Dof-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
SQ SEQUENCE 373 AA; 36843 MW; 55B88568858A409B CRC64;
MASGGALSPV EEKPTVVKTT KAEQHEEEAA VAVKSAAEMM KKSSPCCPRC NSIKTKFCYY
NNYSMAQPRY FCRECRRYWT QGGSLRNVPV GGGCRKSKRS SASSASASAA SPPAPAVGAA
PPVVPALSSA ISKLLQSEPM AAPCADFPNV LPTFVSTGFE LPAAAGDRLS LGSFGAFGNL
SAAVAAPGGG GGSSTTTSFM DMLRGVGGLF DGVGNSHQMG GNGGGGGSYY APLITGAGNG
MLMPPPPLPP FSGSLMQHGM QGLFANHAMG GGGGGVMNAG EDGSVMAGLG GGQWPPALGG
ADEQQGGGDG GEAVMTKDTG GGASSSASRP DYFYGWNSAA GGVVAGGGIG GNAAAATGAT
PWQGLIDSSS AMM
