TGA1_ARATH
ID TGA1_ARATH Reviewed; 368 AA.
AC Q39237; Q8LBQ9; Q9FJP4;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Transcription factor TGA1;
DE AltName: Full=DNA-binding protein TGA1a-like protein;
DE AltName: Full=bZIP transcription factor 47;
DE Short=AtbZIP47;
GN Name=TGA1; Synonyms=BZIP47; OrderedLocusNames=At5g65210; ORFNames=MQN23.15;
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].
RC STRAIN=cv. Columbia; TISSUE=Leaf, and Stem;
RX PubMed=1446171; DOI=10.2307/3869416;
RA Schindler U., Beckmann H., Cashmore A.R.;
RT "TGA1 and G-box binding factors: two distinct classes of Arabidopsis
RT leucine zipper proteins compete for the G-box-like element TGACGTGG.";
RL Plant Cell 4:1309-1319(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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].
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].
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 DNA-BINDING.
RX PubMed=7479010; DOI=10.1093/nar/23.18.3778;
RA Lam E., Lam Y.K.;
RT "Binding site requirements and differential representation of TGF factors
RT in nuclear ASF-1 activity.";
RL Nucleic Acids Res. 23:3778-3785(1995).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=8628224; DOI=10.1007/bf02174184;
RA de Pater S., Pham K., Memelink J., Kijne J.;
RT "Binding specificity and tissue-specific expression pattern of the
RT Arabidopsis bZIP transcription factor TGA2.";
RL Mol. Gen. Genet. 250:237-239(1996).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11906833; DOI=10.1016/s1360-1385(01)02223-3;
RA Jakoby M., Weisshaar B., Droege-Laser W., Vicente-Carbajosa J.,
RA Tiedemann J., Kroj T., Parcy F.;
RT "bZIP transcription factors in Arabidopsis.";
RL Trends Plant Sci. 7:106-111(2002).
RN [9]
RP INTERACTION WITH NPR1, AND MUTAGENESIS OF CYS-260 AND CYS-266.
RX PubMed=12953119; DOI=10.1105/tpc.012849;
RA Despres C., Chubak C., Rochon A., Clark R., Bethune T., Desveaux D.,
RA Fobert P.R.;
RT "The Arabidopsis NPR1 disease resistance protein is a novel cofactor that
RT confers redox regulation of DNA binding activity to the basic
RT domain/leucine zipper transcription factor TGA1.";
RL Plant Cell 15:2181-2191(2003).
CC -!- FUNCTION: Transcriptional activator that binds specifically to the DNA
CC sequence 5'-TGACG-3'. Recognizes ocs elements like the as-1 motif of
CC the cauliflower mosaic virus 35S promoter. Binding to the as-1-like cis
CC elements mediate auxin- and salicylic acid-inducible transcription. May
CC be involved in the induction of the systemic acquired resistance (SAR)
CC via its interaction with NPR1. Could also bind to the Hex-motif (5'-
CC TGACGTGG-3') another cis-acting element found in plant histone
CC promoters.
CC -!- SUBUNIT: Binds DNA as a dimer. The reduced form interacts with NPR1.
CC {ECO:0000269|PubMed:12953119}.
CC -!- INTERACTION:
CC Q39237; Q8GYE4: At2g38300; NbExp=3; IntAct=EBI-541351, EBI-4424461;
CC Q39237; O82255: GRXC13; NbExp=3; IntAct=EBI-541351, EBI-4444060;
CC Q39237; Q96305: GRXC7; NbExp=4; IntAct=EBI-541351, EBI-2257898;
CC Q39237; Q8LF89: GRXC8; NbExp=3; IntAct=EBI-541351, EBI-4434651;
CC Q39237; Q6NLU2: GRXS7; NbExp=3; IntAct=EBI-541351, EBI-25521272;
CC Q39237; O04341: GRXS9; NbExp=3; IntAct=EBI-541351, EBI-4450582;
CC Q39237; Q9STS6: LBD27; NbExp=3; IntAct=EBI-541351, EBI-15209584;
CC Q39237; P93002: NPR1; NbExp=7; IntAct=EBI-541351, EBI-1392127;
CC Q39237; Q8L746: NPR3; NbExp=3; IntAct=EBI-541351, EBI-4441365;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q39237-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in roots.
CC {ECO:0000269|PubMed:8628224}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM64610.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X68053; CAA48189.1; -; mRNA.
DR EMBL; AB013395; BAB11657.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98019.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98020.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98021.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98022.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98023.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70446.1; -; Genomic_DNA.
DR EMBL; AY099593; AAM20444.1; -; mRNA.
DR EMBL; AY128838; AAM91238.1; -; mRNA.
DR EMBL; AY087049; AAM64610.1; ALT_INIT; mRNA.
DR PIR; JQ1678; JQ1678.
DR RefSeq; NP_001032147.1; NM_001037070.1. [Q39237-1]
DR RefSeq; NP_001032148.1; NM_001037071.1. [Q39237-1]
DR RefSeq; NP_001032149.1; NM_001037072.2. [Q39237-1]
DR RefSeq; NP_001318881.1; NM_001345675.1. [Q39237-1]
DR RefSeq; NP_201324.1; NM_125919.3. [Q39237-1]
DR RefSeq; NP_851273.1; NM_180942.3. [Q39237-1]
DR AlphaFoldDB; Q39237; -.
DR SMR; Q39237; -.
DR BioGRID; 21888; 161.
DR IntAct; Q39237; 128.
DR STRING; 3702.AT5G65210.2; -.
DR PaxDb; Q39237; -.
DR PRIDE; Q39237; -.
DR ProteomicsDB; 234268; -. [Q39237-1]
DR EnsemblPlants; AT5G65210.1; AT5G65210.1; AT5G65210. [Q39237-1]
DR EnsemblPlants; AT5G65210.2; AT5G65210.2; AT5G65210. [Q39237-1]
DR EnsemblPlants; AT5G65210.3; AT5G65210.3; AT5G65210. [Q39237-1]
DR EnsemblPlants; AT5G65210.4; AT5G65210.4; AT5G65210. [Q39237-1]
DR EnsemblPlants; AT5G65210.5; AT5G65210.5; AT5G65210. [Q39237-1]
DR EnsemblPlants; AT5G65210.7; AT5G65210.7; AT5G65210. [Q39237-1]
DR GeneID; 836646; -.
DR Gramene; AT5G65210.1; AT5G65210.1; AT5G65210. [Q39237-1]
DR Gramene; AT5G65210.2; AT5G65210.2; AT5G65210. [Q39237-1]
DR Gramene; AT5G65210.3; AT5G65210.3; AT5G65210. [Q39237-1]
DR Gramene; AT5G65210.4; AT5G65210.4; AT5G65210. [Q39237-1]
DR Gramene; AT5G65210.5; AT5G65210.5; AT5G65210. [Q39237-1]
DR Gramene; AT5G65210.7; AT5G65210.7; AT5G65210. [Q39237-1]
DR KEGG; ath:AT5G65210; -.
DR Araport; AT5G65210; -.
DR TAIR; locus:2171820; AT5G65210.
DR eggNOG; ENOG502QS1H; Eukaryota.
DR InParanoid; Q39237; -.
DR PhylomeDB; Q39237; -.
DR PRO; PR:Q39237; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39237; baseline and differential.
DR Genevisible; Q39237; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR025422; TGA_domain.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF14144; DOG1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
DR PROSITE; PS51806; DOG1; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; Disulfide bond; DNA-binding;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..368
FT /note="Transcription factor TGA1"
FT /id="PRO_0000076553"
FT DOMAIN 82..145
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT DOMAIN 153..363
FT /note="DOG1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01147"
FT REGION 53..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..104
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 110..124
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COILED 83..131
FT /evidence="ECO:0000255"
FT COILED 261..281
FT /evidence="ECO:0000255"
FT COMPBIAS 53..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 260..266
FT /evidence="ECO:0000255"
FT MUTAGEN 260
FT /note="C->N: Gain of interaction with NPR1; when associated
FT with S-266."
FT /evidence="ECO:0000269|PubMed:12953119"
FT MUTAGEN 266
FT /note="C->S: Gain of interaction with NPR1; when associated
FT with N-260."
FT /evidence="ECO:0000269|PubMed:12953119"
FT CONFLICT 285..287
FT /note="ADC -> RT (in Ref. 1; CAA48189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 42064 MW; 8EB9CD75E1E1EF39 CRC64;
MNSTSTHFVP PRRVGIYEPV HQFGMWGESF KSNISNGTMN TPNHIIIPNN QKLDNNVSED
TSHGTAGTPH MFDQEASTSR HPDKIQRRLA QNREAARKSR LRKKAYVQQL ETSRLKLIQL
EQELDRARQQ GFYVGNGIDT NSLGFSETMN PGIAAFEMEY GHWVEEQNRQ ICELRTVLHG
HINDIELRSL VENAMKHYFE LFRMKSSAAK ADVFFVMSGM WRTSAERFFL WIGGFRPSDL
LKVLLPHFDV LTDQQLLDVC NLKQSCQQAE DALTQGMEKL QHTLADCVAA GQLGEGSYIP
QVNSAMDRLE ALVSFVNQAD HLRHETLQQM YRILTTRQAA RGLLALGEYF QRLRALSSSW
ATRHREPT
