ID   TGA4_ARATH              Reviewed;         364 AA.
AC   Q39162; Q9LX25;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=Transcription factor TGA4;
DE   AltName: Full=Ocs element-binding factor 4;
DE            Short=OBF4;
DE   AltName: Full=bZIP transcription factor 57;
DE            Short=AtbZIP57;
GN   Name=TGA4; Synonyms=BZIP57, OBF4; OrderedLocusNames=At5g10030;
GN   ORFNames=T31P16_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 [MRNA], AND CHARACTERIZATION.
RC   STRAIN=cv. Columbia; TISSUE=Root;
RX   PubMed=8252072; DOI=10.1046/j.1365-313x.1993.04040711.x;
RA   Zhang B., Foley R.C., Singh K.B.;
RT   "Isolation and characterization of two related Arabidopsis ocs-element bZIP
RT   binding proteins.";
RL   Plant J. 4:711-716(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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   INTERACTION WITH OBP1.
RX   PubMed=8718629; DOI=10.1105/tpc.7.12.2241;
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   [5]
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   [6]
RP   INTERACTION WITH EBP.
RX   PubMed=9159183; DOI=10.1073/pnas.94.11.5961;
RA   Buettner M., Singh K.B.;
RT   "Arabidopsis thaliana ethylene-responsive element binding protein (AtEBP),
RT   an ethylene-inducible, GCC box DNA-binding protein interacts with an ocs
RT   element binding protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:5961-5966(1997).
RN   [7]
RP   INTERACTION WITH OBP2 AND OBP3.
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   [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-256 AND CYS-262.
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. Interaction with the Dof domain proteins
CC       OBP1, OBP2 or OBP3 enhances the binding to the ocs element. Interacts
CC       with RAP2-3/EPB, an ethylene-responsive element binding protein. The
CC       reduced form interacts with NPR1. {ECO:0000269|PubMed:10758484,
CC       ECO:0000269|PubMed:12953119, ECO:0000269|PubMed:8718629,
CC       ECO:0000269|PubMed:9159183}.
CC   -!- INTERACTION:
CC       Q39162; Q39057: CO; NbExp=3; IntAct=EBI-541600, EBI-1639724;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in roots.
CC       {ECO:0000269|PubMed:8628224}.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X69899; CAA49524.1; -; mRNA.
DR   EMBL; AL356332; CAB92044.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91484.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91485.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM68900.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM68901.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM68902.1; -; Genomic_DNA.
DR   PIR; S48121; S48121.
DR   PIR; T50007; T50007.
DR   RefSeq; NP_001190270.1; NM_001203341.1.
DR   RefSeq; NP_001330616.1; NM_001343084.1.
DR   RefSeq; NP_001330617.1; NM_001343085.1.
DR   RefSeq; NP_001330618.1; NM_001343086.1.
DR   RefSeq; NP_196565.1; NM_121041.5.
DR   AlphaFoldDB; Q39162; -.
DR   SMR; Q39162; -.
DR   BioGRID; 16144; 7.
DR   IntAct; Q39162; 7.
DR   STRING; 3702.Q39162; -.
DR   PaxDb; 3702-AT5G10030-1; -.
DR   ProteomicsDB; 234409; -.
DR   EnsemblPlants; AT5G10030.1; AT5G10030.1; AT5G10030.
DR   EnsemblPlants; AT5G10030.2; AT5G10030.2; AT5G10030.
DR   EnsemblPlants; AT5G10030.3; AT5G10030.3; AT5G10030.
DR   EnsemblPlants; AT5G10030.4; AT5G10030.4; AT5G10030.
DR   EnsemblPlants; AT5G10030.5; AT5G10030.5; AT5G10030.
DR   GeneID; 830866; -.
DR   Gramene; AT5G10030.1; AT5G10030.1; AT5G10030.
DR   Gramene; AT5G10030.2; AT5G10030.2; AT5G10030.
DR   Gramene; AT5G10030.3; AT5G10030.3; AT5G10030.
DR   Gramene; AT5G10030.4; AT5G10030.4; AT5G10030.
DR   Gramene; AT5G10030.5; AT5G10030.5; AT5G10030.
DR   KEGG; ath:AT5G10030; -.
DR   Araport; AT5G10030; -.
DR   TAIR; AT5G10030; TGA4.
DR   eggNOG; ENOG502QS1H; Eukaryota.
DR   HOGENOM; CLU_024782_1_0_1; -.
DR   InParanoid; Q39162; -.
DR   OMA; IGMWEES; -.
DR   OrthoDB; 452329at2759; -.
DR   PhylomeDB; Q39162; -.
DR   PRO; PR:Q39162; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q39162; baseline and differential.
DR   GO; GO:0005634; C:nucleus; HDA: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:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 1.20.5.170; -; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR025422; TGA_domain.
DR   PANTHER; PTHR45693:SF70; TRANSCRIPTION FACTOR TGA4; 1.
DR   PANTHER; PTHR45693; TRANSCRIPTION FACTOR TGA9; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   Pfam; PF14144; DOG1; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
DR   PROSITE; PS51806; DOG1; 1.
DR   Genevisible; Q39162; AT.
PE   1: Evidence at protein level;
KW   Activator; Coiled coil; Disulfide bond; DNA-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..364
FT                   /note="Transcription factor TGA4"
FT                   /id="PRO_0000076556"
FT   DOMAIN          78..141
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   DOMAIN          149..359
FT                   /note="DOG1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01147"
FT   REGION          39..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          80..100
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          106..120
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COILED          79..127
FT                   /evidence="ECO:0000255"
FT   COILED          257..277
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        52..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        256..262
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         256
FT                   /note="C->N: Gain of interaction with NPR1; when associated
FT                   with S-262."
FT                   /evidence="ECO:0000269|PubMed:12953119"
FT   MUTAGEN         262
FT                   /note="C->S: Gain of interaction with NPR1; when associated
FT                   with N-256."
FT                   /evidence="ECO:0000269|PubMed:12953119"
FT   CONFLICT        265
FT                   /note="A -> S (in Ref. 1; CAA49524)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   364 AA;  41751 MW;  08225A91F4CA20ED CRC64;
     MNTTSTHFVP PRRFEVYEPL NQIGMWEESF KNNGDMYTPG SIIIPTNEKP DSLSEDTSHG
     TEGTPHKFDQ EASTSRHPDK IQRRLAQNRE AARKSRLRKK AYVQQLETSR LKLIHLEQEL
     DRARQQGFYV GNGVDTNALS FSDNMSSGIV AFEMEYGHWV EEQNRQICEL RTVLHGQVSD
     IELRSLVENA MKHYFQLFRM KSAAAKIDVF YVMSGMWKTS AERFFLWIGG FRPSELLKVL
     LPHFDPLTDQ QLLDVCNLRQ SCQQAEDALS QGMEKLQHTL AESVAAGKLG EGSYIPQMTC
     AMERLEALVS FVNQADHLRH ETLQQMHRIL TTRQAARGLL ALGEYFQRLR ALSSSWAARQ
     REPT
//