DOF34_ARATH
ID DOF34_ARATH Reviewed; 253 AA.
AC Q39088; Q9M2R8;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Dof zinc finger protein DOF3.4;
DE Short=AtDOF3.4;
DE AltName: Full=OBF-binding protein 1;
GN Name=DOF3.4; Synonyms=OBP1; OrderedLocusNames=At3g50410;
GN ORFNames=F11C1_250;
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], TISSUE SPECIFICITY, AND INTERACTION WITH OBF4
RP AND OBF5.
RC STRAIN=cv. Columbia;
RX PubMed=8718629; DOI=10.2307/3870165;
RA Zhang B., Chen W., Foley R.C., Buettner M., Singh K.B.;
RT "Interactions between distinct types of DNA binding proteins enhance
RT binding to ocs element promoter sequences.";
RL Plant Cell 7:2241-2252(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 TISSUE SPECIFICITY, AND INDUCTION.
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 [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 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.
CC -!- SUBUNIT: Interacts with OBF4 or OBF5. {ECO:0000269|PubMed:8718629}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in the whole plant.
CC {ECO:0000269|PubMed:10758484, ECO:0000269|PubMed:8718629}.
CC -!- INDUCTION: By auxin and salicylic acid (SA).
CC {ECO:0000269|PubMed:10758484}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA61485.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X89192; CAA61485.1; ALT_FRAME; mRNA.
DR EMBL; AL132976; CAB88324.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78664.1; -; Genomic_DNA.
DR PIR; T46072; T46072.
DR RefSeq; NP_190610.1; NM_114901.4.
DR AlphaFoldDB; Q39088; -.
DR BioGRID; 9523; 1.
DR IntAct; Q39088; 1.
DR STRING; 3702.AT3G50410.1; -.
DR PaxDb; Q39088; -.
DR PRIDE; Q39088; -.
DR ProteomicsDB; 222113; -.
DR EnsemblPlants; AT3G50410.1; AT3G50410.1; AT3G50410.
DR GeneID; 824205; -.
DR Gramene; AT3G50410.1; AT3G50410.1; AT3G50410.
DR KEGG; ath:AT3G50410; -.
DR Araport; AT3G50410; -.
DR TAIR; locus:2074850; AT3G50410.
DR eggNOG; ENOG502QUV1; Eukaryota.
DR HOGENOM; CLU_036438_6_0_1; -.
DR InParanoid; Q39088; -.
DR OMA; GNTWQVE; -.
DR OrthoDB; 1353534at2759; -.
DR PhylomeDB; Q39088; -.
DR PRO; PR:Q39088; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q39088; baseline and differential.
DR Genevisible; Q39088; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IDA:TAIR.
DR GO; GO:0042545; P:cell wall modification; IMP:TAIR.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IEP: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 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..253
FT /note="Dof zinc finger protein DOF3.4"
FT /id="PRO_0000074280"
FT ZN_FING 30..84
FT /note="Dof-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT REGION 73..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT CONFLICT 155
FT /note="A -> R (in Ref. 1; CAA61485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 253 AA; 26382 MW; 3A64EA3F6CF0A5D1 CRC64;
MPTSDSGEPR RIAMKPNGVT VPISDQQEQL PCPRCDSSNT KFCYYNNYNF SQPRHFCKAC
RRYWTHGGTL RDVPVGGGTR KSAKRSRTCS NSSSSSVSGV VSNSNGVPLQ TTPVLFPQSS
ISNGVTHTVT ESDGKGSALS LCGSFTSTLL NHNAAATATH GSGSVIGIGG FGIGLGSGFD
DVSFGLGRAM WPFSTVGTAT TTNVGSNGGH HAVPMPATWQ FEGLESNAGG GFVSGEYFAW
PDLSITTPGN SLK
