DOF37_ARATH
ID DOF37_ARATH Reviewed; 296 AA.
AC Q43385; Q8GYW3; Q9SAF9;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Dof zinc finger protein DOF3.7;
DE Short=AtDOF3.7;
DE AltName: Full=Dof affecting germination 1;
DE AltName: Full=RolB domain B factor a;
DE AltName: Full=Transcription factor BBFa;
DE Short=AtBBFa;
GN Name=DOF3.7; Synonyms=BBFA, DAG1; OrderedLocusNames=At3g61850;
GN ORFNames=F21F14.20;
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 / MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=8771779; DOI=10.1046/j.1365-313x.1996.10020215.x;
RA de Paolis A., Sabatini S., de Pascalis L., Costantino P., Capone I.;
RT "A rolB regulatory factor belongs to a new class of single zinc finger
RT plant proteins.";
RL Plant J. 10:215-223(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC STRAIN=cv. Wassilewskija;
RX PubMed=10640273;
RA Papi M., Sabatini S., Bouchez D., Camilleri C., Costantino P.,
RA Vittorioso P.;
RT "Identification and disruption of an Arabidopsis zinc finger gene
RT controlling seed germination.";
RL Genes Dev. 14:28-33(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP CHARACTERIZATION.
RX PubMed=11842145; DOI=10.1104/pp.010488;
RA Papi M., Sabatini S., Altamura M.M., Hennig L., Schaefer E., Costantino P.,
RA Vittorioso P.;
RT "Inactivation of the phloem-specific Dof zinc finger gene DAG1 affects
RT response to light and integrity of the testa of Arabidopsis seeds.";
RL Plant Physiol. 128:411-417(2002).
RN [7]
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 inactivity of a
CC component that would be activated to trigger germination as a
CC consequence of red light perception.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q43385-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q43385-2; Sequence=VSP_008898;
CC -!- TISSUE SPECIFICITY: Expressed in the phloem of the mother plant,
CC including in roots, stem, leaves and flowers, but not present in the
CC seed and embryo. In maturing siliques, found all through the funiculus
CC connecting the placenta to the ovule, 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 DOF3.7/DAG1 appears to be
CC opposite to that of DOF2.5/DAG2. Both zinc finger proteins may act on a
CC maternal switch that controls seed germination, possibly by regulating
CC the same gene(s).
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DR EMBL; X97941; CAA66600.2; -; mRNA.
DR EMBL; AJ224122; CAB40190.1; -; Genomic_DNA.
DR EMBL; AL138642; CAB71892.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80266.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80267.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80268.1; -; Genomic_DNA.
DR EMBL; AK117352; BAC42022.1; -; mRNA.
DR PIR; T47977; T47977.
DR RefSeq; NP_001078327.1; NM_001084858.1. [Q43385-2]
DR RefSeq; NP_191744.1; NM_116050.4. [Q43385-1]
DR RefSeq; NP_850734.1; NM_180403.2. [Q43385-2]
DR AlphaFoldDB; Q43385; -.
DR BioGRID; 10672; 1.
DR STRING; 3702.AT3G61850.4; -.
DR ProteomicsDB; 222116; -. [Q43385-1]
DR EnsemblPlants; AT3G61850.1; AT3G61850.1; AT3G61850. [Q43385-1]
DR EnsemblPlants; AT3G61850.2; AT3G61850.2; AT3G61850. [Q43385-2]
DR EnsemblPlants; AT3G61850.3; AT3G61850.3; AT3G61850. [Q43385-2]
DR GeneID; 825358; -.
DR Gramene; AT3G61850.1; AT3G61850.1; AT3G61850. [Q43385-1]
DR Gramene; AT3G61850.2; AT3G61850.2; AT3G61850. [Q43385-2]
DR Gramene; AT3G61850.3; AT3G61850.3; AT3G61850. [Q43385-2]
DR KEGG; ath:AT3G61850; -.
DR Araport; AT3G61850; -.
DR eggNOG; ENOG502REBY; Eukaryota.
DR InParanoid; Q43385; -.
DR PhylomeDB; Q43385; -.
DR PRO; PR:Q43385; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q43385; baseline and differential.
DR Genevisible; Q43385; 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 InterPro; IPR045174; Dof.
DR InterPro; IPR003851; Znf_Dof.
DR PANTHER; PTHR31992; PTHR31992; 2.
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; Germination; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..296
FT /note="Dof zinc finger protein DOF3.7"
FT /id="PRO_0000074283"
FT ZN_FING 74..128
FT /note="Dof-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT REGION 41..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00071"
FT BINDING 101
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 VAR_SEQ 1..12
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_008898"
SQ SEQUENCE 296 AA; 32966 MW; 0D733352776272EB CRC64;
MDATKWTQGF QEMINVKPME QMISSTNNNT PQQQPTFIAT NTRPNATASN GGSGGNTNNT
ATMETRKARP QEKVNCPRCN STNTKFCYYN NYSLTQPRYF CKGCRRYWTE GGSLRNVPVG
GSSRKNKRSS TPLASPSNPK LPDLNPPILF SSQIPNKSNK DLNLLSFPVM QDHHHHALEL
LRSNGVSSRG MNTFLPGQMM DSNSVLYSSL GFPTMPDYKQ SNNNLSFSID HHQGIGHNTI
NSNQRAQDNN DDMNGASRVL FPFSDMKELS STTQEKSHGN NTYWNGMFSN TGGSSW
