DOF25_ARATH
ID DOF25_ARATH Reviewed; 369 AA.
AC Q9ZPY0; Q84WI6; Q9AR20;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Dof zinc finger protein DOF2.5;
DE Short=AtDOF2.5;
DE AltName: Full=Dof affecting germination 2;
GN Name=DOF2.5; Synonyms=DAG2; OrderedLocusNames=At2g46590;
GN ORFNames=F13A10.12;
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=12084825; DOI=10.1105/tpc.010491;
RA Gualberti G., Papi M., Bellucci L., Ricci I., Bouchez D., Camilleri C.,
RA Costantino P., Vittorioso P.;
RT "Mutations in the Dof zinc finger genes DAG2 and DAG1 influence with
RT opposite effects the germination of Arabidopsis seeds.";
RL Plant Cell 14:1253-1263(2002).
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] (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).
CC -!- FUNCTION: Transcription factor specifically involved in the maternal
CC control of seed germination. Regulates transcription by binding to a
CC 5'-AA[AG]G-3' consensus core sequence. May ensure the activation of a
CC component that would trigger germination as a consequence of red light
CC perception.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ZPY0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZPY0-2; Sequence=VSP_011775;
CC -!- TISSUE SPECIFICITY: Expressed in the vascular system of the mother
CC plant, but not present in the seed and embryo. In maturing siliques,
CC found all through the funiculus connecting the placenta to the ovule,
CC but not in the ovule.
CC -!- DEVELOPMENTAL STAGE: Turned off in siliques when they reached full
CC maturation. Not expressed in developing or mature embryos.
CC -!- MISCELLANEOUS: The regulatory role of DOF2.5/DAG2 appears to be
CC opposite to that of DOF3.7/DAG1. Both zinc finger proteins may act on a
CC maternal switch that controls seed germination, possibly by regulating
CC the same gene(s).
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD20169.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ237810; CAC36939.1; -; Genomic_DNA.
DR EMBL; AJ237811; CAC36940.1; -; mRNA.
DR EMBL; AC006418; AAD20169.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10725.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10726.1; -; Genomic_DNA.
DR EMBL; BT003328; AAO29947.1; -; mRNA.
DR EMBL; BT008842; AAP68281.1; -; mRNA.
DR PIR; G84904; G84904.
DR RefSeq; NP_001031549.1; NM_001036472.2. [Q9ZPY0-1]
DR RefSeq; NP_182182.2; NM_130224.8. [Q9ZPY0-2]
DR AlphaFoldDB; Q9ZPY0; -.
DR STRING; 3702.AT2G46590.2; -.
DR PaxDb; Q9ZPY0; -.
DR PRIDE; Q9ZPY0; -.
DR ProteomicsDB; 222110; -. [Q9ZPY0-1]
DR EnsemblPlants; AT2G46590.1; AT2G46590.1; AT2G46590. [Q9ZPY0-2]
DR EnsemblPlants; AT2G46590.2; AT2G46590.2; AT2G46590. [Q9ZPY0-1]
DR GeneID; 819271; -.
DR Gramene; AT2G46590.1; AT2G46590.1; AT2G46590. [Q9ZPY0-2]
DR Gramene; AT2G46590.2; AT2G46590.2; AT2G46590. [Q9ZPY0-1]
DR KEGG; ath:AT2G46590; -.
DR Araport; AT2G46590; -.
DR TAIR; locus:2039959; AT2G46590.
DR eggNOG; ENOG502REBY; Eukaryota.
DR HOGENOM; CLU_036438_5_1_1; -.
DR InParanoid; Q9ZPY0; -.
DR OMA; MIGEGTW; -.
DR OrthoDB; 1101510at2759; -.
DR PhylomeDB; Q9ZPY0; -.
DR PRO; PR:Q9ZPY0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZPY0; baseline and differential.
DR Genevisible; Q9ZPY0; AT.
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; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071491; P:cellular response to red light; IEP:TAIR.
DR GO; GO:0071462; P:cellular response to water stimulus; IEP:TAIR.
DR GO; GO:0010372; P:positive regulation of gibberellin biosynthetic process; IMP:TAIR.
DR GO; GO:0010030; P:positive regulation of seed germination; IMP:TAIR.
DR GO; GO:0010161; P:red light signaling pathway; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP: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 Alternative splicing; DNA-binding; Germination; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..369
FT /note="Dof zinc finger protein DOF2.5"
FT /id="PRO_0000074276"
FT ZN_FING 80..134
FT /note="Dof-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT REGION 120..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT VAR_SEQ 1..12
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_011775"
FT CONFLICT 10
FT /note="F -> L (in Ref. 1; CAC36939/CAC36940)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 40537 MW; 989DE46A2B430F58 CRC64;
MDATKWTQGF QEMMNVKPME QIMIPNNNTH QPNTTSNARP NTILTSNGVS TAGATVSGVS
NNNNNTAVVA ERKARPQEKL NCPRCNSTNT KFCYYNNYSL TQPRYFCKGC RRYWTEGGSL
RNVPVGGSSR KNKRSSSSSS SNILQTIPSS LPDLNPPILF SNQIHNKSKG SSQDLNLLSF
PVMQDQHHHH VHMSQFLQMP KMEGNGNITH QQQPSSSSSV YGSSSSPVSA LELLRTGVNV
SSRSGINSSF MPSGSMMDSN TVLYTSSGFP TMVDYKPSNL SFSTDHQGLG HNSNNRSEAL
HSDHHQQGRV LFPFGDQMKE LSSSITQEVD HDDNQQQKSH GNNNNNNNSS PNNGYWSGMF
STTGGGSSW
