DOF11_ARATH
ID DOF11_ARATH Reviewed; 331 AA.
AC Q8L9V6; Q8W4A2; Q9LQN7; Q9XGU6;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Dof zinc finger protein DOF1.1 {ECO:0000303|PubMed:12475498};
DE Short=AtDOF1.1 {ECO:0000303|PubMed:12475498};
DE AltName: Full=OBF-binding protein 2 {ECO:0000303|PubMed:10758484};
DE AltName: Full=Protein PHLOEM EARLY DOF OBP2 {ECO:0000303|PubMed:30626969};
DE AltName: Full=Protein UAS-TAGGED ROOT PATTERNING 3 {ECO:0000303|PubMed:23057675};
GN Name=DOF1.1 {ECO:0000303|PubMed:12475498};
GN Synonyms=OBP2 {ECO:0000303|PubMed:10758484},
GN URP3 {ECO:0000303|PubMed:23057675};
GN OrderedLocusNames=At1g07640 {ECO:0000312|Araport:AT1G07640};
GN ORFNames=F24B9.30 {ECO:0000312|EMBL:AAF75094.1};
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] (ISOFORM 2), TISSUE SPECIFICITY, INDUCTION, AND
RP INTERACTION WITH OBF4.
RC STRAIN=cv. Columbia;
RX PubMed=10758484; DOI=10.1046/j.1365-313x.2000.00678.x;
RA Kang H.-G., Singh K.B.;
RT "Characterization of salicylic acid-responsive, Arabidopsis Dof domain
RT proteins: overexpression of OBP3 leads to growth defects.";
RL Plant J. 21:329-339(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP AND INDUCTION BY SPODOPTERA LITTORALIS; WOUNDING AND METHYL JASMONATE.
RX PubMed=16740150; DOI=10.1111/j.1365-313x.2006.02767.x;
RA Skirycz A., Reichelt M., Burow M., Birkemeyer C., Rolcik J., Kopka J.,
RA Zanor M.I., Gershenzon J., Strnad M., Szopa J., Mueller-Roeber B., Witt I.;
RT "DOF transcription factor AtDof1.1 (OBP2) is part of a regulatory network
RT controlling glucosinolate biosynthesis in Arabidopsis.";
RL Plant J. 47:10-24(2006).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23057675; DOI=10.1111/tpj.12049;
RA Waki T., Miyashima S., Nakanishi M., Ikeda Y., Hashimoto T., Nakajima K.;
RT "A GAL4-based targeted activation tagging system in Arabidopsis thaliana.";
RL Plant J. 73:357-367(2013).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
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. Enhances the DNA binding of OBF
CC transcription factors to OCS elements (By similarity). Involved in the
CC regulation of root development (PubMed:23057675). 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 (PubMed:30626969). Element of a regulatory network controlling indole
CC glucosinolates (IGS) biosynthesis, probably by inducing the expression
CC of accurate genes (e.g. CYP83B1). Promotes apical dominance
CC (PubMed:16740150). {ECO:0000250|UniProtKB:Q9M2U1,
CC ECO:0000269|PubMed:16740150, ECO:0000269|PubMed:23057675,
CC ECO:0000269|PubMed:30626969}.
CC -!- SUBUNIT: Interacts with OBF4. {ECO:0000269|PubMed:10758484}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8L9V6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8L9V6-2; Sequence=VSP_011776;
CC -!- TISSUE SPECIFICITY: Expressed in the vasculature (mainly in the phloem
CC and associated cell files) of cotyledons, leaves, roots, flower stalks
CC and petals (PubMed:10758484, PubMed:16740150, PubMed:23057675). The
CC PEAR proteins (e.g. DOF2.4, DOF5.1, DOF3.2, DOF1.1, DOF5.6 and DOF5.3)
CC form a short-range concentration gradient that peaks at protophloem
CC sieve elements (PSE) (PubMed:30626969). {ECO:0000269|PubMed:10758484,
CC ECO:0000269|PubMed:16740150, ECO:0000269|PubMed:23057675,
CC ECO:0000269|PubMed:30626969}.
CC -!- DEVELOPMENTAL STAGE: In roots, confined to the central cylinder
CC (vascular tissue and pericycle) of both main and lateral roots. In
CC leaves, expressed in the vasculature, mostly in phloem cells. Also
CC present in the vasculature of stems and in stamen filaments of flowers.
CC Detected at low levels in the vasculature of petals and carpels.
CC {ECO:0000269|PubMed:16740150}.
CC -!- INDUCTION: By auxin and salicylic acid (SA) (PubMed:10758484). Induced
CC transiently in response to the generalist herbivore S.littoralis.
CC Triggered by methyl jasmonate (MeJA) and wounding (PubMed:16740150).
CC {ECO:0000269|PubMed:10758484, ECO:0000269|PubMed:16740150}.
CC -!- DISRUPTION PHENOTYPE: Reduced expression of CYP83B1. Longer hypocotyls
CC and increased lateral root formation. {ECO:0000269|PubMed:16740150}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD38986.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF75094.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF155816; AAD38986.1; ALT_FRAME; mRNA.
DR EMBL; AC007583; AAF75094.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28152.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28153.1; -; Genomic_DNA.
DR EMBL; AY062715; AAL32793.1; -; mRNA.
DR EMBL; AY093351; AAM13350.1; -; mRNA.
DR EMBL; AY088198; AAM65740.1; -; mRNA.
DR PIR; H86210; H86210.
DR RefSeq; NP_001030988.1; NM_001035911.2.
DR RefSeq; NP_563792.3; NM_100637.4. [Q8L9V6-1]
DR RefSeq; NP_850938.1; NM_180607.2. [Q8L9V6-2]
DR AlphaFoldDB; Q8L9V6; -.
DR BioGRID; 22518; 2.
DR STRING; 3702.AT1G07640.3; -.
DR iPTMnet; Q8L9V6; -.
DR PaxDb; Q8L9V6; -.
DR PRIDE; Q8L9V6; -.
DR EnsemblPlants; AT1G07640.1; AT1G07640.1; AT1G07640. [Q8L9V6-2]
DR EnsemblPlants; AT1G07640.2; AT1G07640.2; AT1G07640. [Q8L9V6-1]
DR GeneID; 837277; -.
DR Gramene; AT1G07640.1; AT1G07640.1; AT1G07640. [Q8L9V6-2]
DR Gramene; AT1G07640.2; AT1G07640.2; AT1G07640. [Q8L9V6-1]
DR KEGG; ath:AT1G07640; -.
DR Araport; AT1G07640; -.
DR eggNOG; ENOG502RPNM; Eukaryota.
DR InParanoid; Q8L9V6; -.
DR OrthoDB; 1130450at2759; -.
DR PhylomeDB; Q8L9V6; -.
DR PRO; PR:Q8L9V6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L9V6; baseline and differential.
DR Genevisible; Q8L9V6; 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; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010439; P:regulation of glucosinolate biosynthetic process; IMP:UniProtKB.
DR GO; GO:2000280; P:regulation of root development; IMP:UniProtKB.
DR GO; GO:0009625; P:response to insect; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
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 Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..331
FT /note="Dof zinc finger protein DOF1.1"
FT /id="PRO_0000074263"
FT ZN_FING 77..131
FT /note="Dof-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT REGION 121..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 104
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 VAR_SEQ 1..56
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10758484,
FT ECO:0000303|PubMed:14593172"
FT /id="VSP_011776"
FT CONFLICT 102
FT /note="H -> Y (in Ref. 5; AAM65740)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="L -> I (in Ref. 5; AAM65740)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 35589 MW; D13ED8009A1A8996 CRC64;
MPTNSNHQHH LQHQLNENGS IISGHGLVLS HQLPPLQANP NPNHHHVATS AGLPSRMGGS
MAERARQANI PPLAGPLKCP RCDSSNTKFC YYNNYNLTQP RHFCKGCRRY WTQGGALRNV
PVGGGCRRNN KKGKNGNLKS SSSSSKQSSS VNAQSPSSGQ LRTNHQFPFS PTLYNLTQLG
GIGLNLAATN GNNQAHQIGS SLMMSDLGFL HGRNTSTPMT GNIHENNNNN NNENNLMASV
GSLSPFALFD PTTGLYAFQN DGNIGNNVGI SGSSTSMVDS RVYQTPPVKM EEQPNLANLS
RPVSGLTSPG NQTNQYFWPG SDFSGPSNDL L
