TGA9_ARATH
ID TGA9_ARATH Reviewed; 481 AA.
AC Q93XM6; Q0WT94; Q56W43; Q9SGC7; Q9SJF8;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Transcription factor TGA9 {ECO:0000303|PubMed:20805327};
DE AltName: Full=Protein TGACG (TGA) motif-binding protein 9 {ECO:0000303|PubMed:20805327};
DE AltName: Full=bZIP transcription factor 21 {ECO:0000303|PubMed:11906833};
DE Short=AtbZIP21 {ECO:0000303|PubMed:11906833};
GN Name=TGA9 {ECO:0000303|PubMed:20805327};
GN Synonyms=BZIP21 {ECO:0000303|PubMed:11906833};
GN OrderedLocusNames=At1g08320 {ECO:0000312|Araport:AT1G08320};
GN ORFNames=T23G18.19 {ECO:0000312|EMBL:AAF18246.1},
GN T23G18.22 {ECO:0000312|EMBL:AAF18246.1},
GN T27G7.2 {ECO:0000312|EMBL:AAF22906.1};
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 1), GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE,
RP INTERACTION WITH GRXC7/ROXY1 AND GRXC8/ROXY2, DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=20805327; DOI=10.1104/pp.110.159111;
RA Murmu J., Bush M.J., Delong C., Li S., Xu M., Khan M., Malcolmson C.,
RA Fobert P.R., Zachgo S., Hepworth S.R.;
RT "Arabidopsis basic leucine-zipper transcription factors TGA9 and TGA10
RT interact with floral glutaredoxins ROXY1 and ROXY2 and are redundantly
RT required for anther development.";
RL Plant Physiol. 154:1492-1504(2010).
RN [3]
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 [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] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY.
RX PubMed=15226410; DOI=10.1093/nar/gkh653;
RA Deppmann C.D., Acharya A., Rishi V., Wobbes B., Smeekens S.,
RA Taparowsky E.J., Vinson C.;
RT "Dimerization specificity of all 67 B-ZIP motifs in Arabidopsis thaliana: a
RT comparison to Homo sapiens B-ZIP motifs.";
RL Nucleic Acids Res. 32:3435-3445(2004).
RN [7]
RP INTERACTION WITH TGA1; TGA2; TGA3; TGA4; TGA5; TGA6; TGA7; TGA10 AND PAN,
RP AND SUBUNIT.
RX PubMed=16731568; DOI=10.1093/molbev/msl022;
RA Deppmann C.D., Alvania R.S., Taparowsky E.J.;
RT "Cross-species annotation of basic leucine zipper factor interactions:
RT Insight into the evolution of closed interaction networks.";
RL Mol. Biol. Evol. 23:1480-1492(2006).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY FLG22.
RC STRAIN=cv. Columbia;
RX PubMed=27717447; DOI=10.1016/j.plantsci.2016.06.019;
RA Noshi M., Mori D., Tanabe N., Maruta T., Shigeoka S.;
RT "Arabidopsis clade IV TGA transcription factors, TGA10 and TGA9, are
RT involved in ROS-mediated responses to bacterial PAMP flg22.";
RL Plant Sci. 252:12-21(2016).
CC -!- FUNCTION: Together with TGA10, basic leucine-zipper transcription
CC factor required for anther development, probably via the activation of
CC SPL expression in anthers and via the regulation of genes with
CC functions in early and middle tapetal development (PubMed:20805327).
CC Required for signaling responses to pathogen-associated molecular
CC patterns (PAMPs) such as flg22 that involves chloroplastic reactive
CC oxygen species (ROS) production and subsequent expression of H(2)O(2)-
CC responsive genes (PubMed:27717447). {ECO:0000269|PubMed:20805327,
CC ECO:0000269|PubMed:27717447}.
CC -!- SUBUNIT: Homodimer (PubMed:16731568). Binds DNA as a dimer (By
CC similarity). Interacts with floral glutaredoxins GRXC7/ROXY1 and
CC GRXC8/ROXY2 in the nucleus (PubMed:20805327). Interacts with TGA1,
CC TGA2, TGA3, TGA4, TGA5, TGA6, TGA7, TGA10 and PAN (PubMed:16731568).
CC {ECO:0000250|UniProtKB:Q39140, ECO:0000269|PubMed:16731568,
CC ECO:0000269|PubMed:20805327}.
CC -!- INTERACTION:
CC Q93XM6; Q8L746: NPR3; NbExp=3; IntAct=EBI-1237844, EBI-4441365;
CC Q93XM6; Q8LPR5: TCP4; NbExp=3; IntAct=EBI-1237844, EBI-15192325;
CC Q93XM6; P43273: TGA2; NbExp=4; IntAct=EBI-1237844, EBI-541307;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:20805327}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q93XM6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q93XM6-2; Sequence=VSP_058776;
CC -!- TISSUE SPECIFICITY: Mostly expressed in stems, inflorescence apex and
CC flowers, and, to a lower extent, in seedlings, leaves and siliques.
CC {ECO:0000269|PubMed:20805327}.
CC -!- DEVELOPMENTAL STAGE: During anther development, accumulates in anther
CC primordia during archesporial cell specification and later present in a
CC horseshoe pattern associated with the lateral and adaxial portion of
CC primordia, prior to the emergence of distinct locules. Expressed
CC throughout sporogenic tissue and surrounding cells layers in adaxial
CC and adaxial locules. Localized to the tapetum and middle layers,
CC gradually fading postmeiosis with degeneration of these cell layers.
CC {ECO:0000269|PubMed:20805327}.
CC -!- INDUCTION: Induced by flg22 in leaves. {ECO:0000269|PubMed:27717447}.
CC -!- DISRUPTION PHENOTYPE: In the double mutant tga9 tga10, reduced male
CC fertility due to defects in male gametogenesis, with early steps in
CC anther development blocked in adaxial lobes and later steps affected in
CC abaxial lobes. Microspore development in abaxial anther lobes leads to
CC the production of inviable pollen grains contained within nondehiscent
CC anthers. In addition, multiple defects in the anther dehiscence program
CC are observed, including abnormal stability and lignification of the
CC middle layer and defects in septum and stomium function. Reduced SPL
CC levels in anthers (PubMed:20805327). Increased sensitivity to flg22
CC treatment associated with a lack of chloroplastic H(2)O(2)-responsive
CC genes; this phenotype is enhanced in the double mutant tga9 tga10
CC (PubMed:27717447). {ECO:0000269|PubMed:20805327,
CC ECO:0000269|PubMed:27717447}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF18246.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF22906.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ314757; CAC40022.1; -; mRNA.
DR EMBL; HQ132743; ADO95300.1; -; mRNA.
DR EMBL; AC006932; AAF22906.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011438; AAF18246.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28275.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28276.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28277.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59112.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59113.1; -; Genomic_DNA.
DR EMBL; AK222204; BAD95356.1; -; mRNA.
DR EMBL; AK227667; BAE99654.1; -; mRNA.
DR RefSeq; NP_001030998.1; NM_001035921.3. [Q93XM6-2]
DR RefSeq; NP_001030999.1; NM_001035922.1. [Q93XM6-1]
DR RefSeq; NP_001318954.1; NM_001331769.1. [Q93XM6-2]
DR RefSeq; NP_001321503.1; NM_001331770.1. [Q93XM6-1]
DR RefSeq; NP_563810.2; NM_100705.4. [Q93XM6-1]
DR AlphaFoldDB; Q93XM6; -.
DR IntAct; Q93XM6; 37.
DR STRING; 3702.AT1G08320.3; -.
DR iPTMnet; Q93XM6; -.
DR PaxDb; Q93XM6; -.
DR PRIDE; Q93XM6; -.
DR ProteomicsDB; 234230; -. [Q93XM6-1]
DR EnsemblPlants; AT1G08320.1; AT1G08320.1; AT1G08320. [Q93XM6-1]
DR EnsemblPlants; AT1G08320.2; AT1G08320.2; AT1G08320. [Q93XM6-2]
DR EnsemblPlants; AT1G08320.3; AT1G08320.3; AT1G08320. [Q93XM6-1]
DR EnsemblPlants; AT1G08320.4; AT1G08320.4; AT1G08320. [Q93XM6-1]
DR EnsemblPlants; AT1G08320.5; AT1G08320.5; AT1G08320. [Q93XM6-2]
DR GeneID; 837353; -.
DR Gramene; AT1G08320.1; AT1G08320.1; AT1G08320. [Q93XM6-1]
DR Gramene; AT1G08320.2; AT1G08320.2; AT1G08320. [Q93XM6-2]
DR Gramene; AT1G08320.3; AT1G08320.3; AT1G08320. [Q93XM6-1]
DR Gramene; AT1G08320.4; AT1G08320.4; AT1G08320. [Q93XM6-1]
DR Gramene; AT1G08320.5; AT1G08320.5; AT1G08320. [Q93XM6-2]
DR KEGG; ath:AT1G08320; -.
DR Araport; AT1G08320; -.
DR TAIR; locus:2199968; AT1G08320.
DR eggNOG; ENOG502QRFK; Eukaryota.
DR HOGENOM; CLU_024782_0_2_1; -.
DR InParanoid; Q93XM6; -.
DR OMA; DNSCQTI; -.
DR OrthoDB; 823978at2759; -.
DR PhylomeDB; Q93XM6; -.
DR PRO; PR:Q93XM6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93XM6; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0048653; P:anther development; IMP:UniProtKB.
DR GO; GO:0071588; P:hydrogen peroxide mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IMP:UniProtKB.
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; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..481
FT /note="Transcription factor TGA9"
FT /id="PRO_0000438993"
FT DOMAIN 176..220
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT DOMAIN 242..450
FT /note="DOG1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01147"
FT REGION 91..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..198
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 204..218
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOTIF 165..172
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 91..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..124
FT /note="Missing (in isoform 2)"
FT /id="VSP_058776"
FT CONFLICT 402
FT /note="F -> L (in Ref. 5; BAE99654)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 53514 MW; E80974FF665DCD57 CRC64;
MANHRMSEAT NHNHNHHLPY SLIHGLNNNH PSSGFINQDG SSSFDFGELE EAIVLQGVKY
RNEEAKPPLL GGGGGATTLE MFPSWPIRTH QTLPTESSKS GGESSDSGSA NFSGKAESQQ
PESPMSSKHH LMLQPHHNNM ANSSSTSGLP STSRTLAPPK PSEDKRKATT SGKQLDAKTL
RRLAQNREAA RKSRLRKKAY VQQLESSRIK LSQLEQELQR ARSQGLFMGG CGPPGPNITS
GAAIFDMEYG RWLEDDNRHM SEIRTGLQAH LSDNDLRLIV DGYIAHFDEI FRLKAVAAKA
DVFHLIIGTW MSPAERCFIW MAGFRPSDLI KILVSQMDLL TEQQLMGIYS LQHSSQQAEE
ALSQGLEQLQ QSLIDTLAAS PVIDGMQQMA VALGKISNLE GFIRQADNLR QQTVHQLRRI
LTVRQAARCF LVIGEYYGRL RALSSLWLSR PRETLMSDET SCQTTTDLQI VQSSRNHFSN
F
