TGA10_ARATH
ID TGA10_ARATH Reviewed; 460 AA.
AC E3VNM4; F4K593; Q93XM5; Q9FL60;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Transcription factor TGA10 {ECO:0000303|PubMed:20805327};
DE AltName: Full=Protein TGACG (TGA) motif-binding protein 10 {ECO:0000303|PubMed:20805327};
DE AltName: Full=bZIP transcription factor 65 {ECO:0000303|PubMed:11906833};
DE Short=AtbZIP65 {ECO:0000303|PubMed:11906833};
GN Name=TGA10 {ECO:0000303|PubMed:20805327};
GN Synonyms=BZIP65 {ECO:0000303|PubMed:11906833};
GN OrderedLocusNames=At5g06839 {ECO:0000312|Araport:AT5G06839};
GN ORFNames=MOJ9.1 {ECO:0000312|EMBL:BAB11142.1};
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 2), 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], FUNCTION, DISRUPTION PHENOTYPE, INTERACTION
RP WITH GRXC7/ROXY1 AND GRXC8/ROXY2, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP 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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 HOMODIMERIZATION, AND INTERACTION WITH TGA1; TGA2; TGA3; TGA4; TGA5; TGA6;
RP TGA7; TGA9 AND PAN.
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 [6]
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 TGA9, basic leucine-zipper transcription factor
CC required for anther development, probably via the activation of SPL
CC expression in anthers and via the regulation of genes with functions in
CC early and middle tapetal development (PubMed:20805327). Required for
CC signaling responses to pathogen-associated molecular patterns (PAMPs)
CC such as flg22 that involves chloroplastic reactive oxygen species (ROS)
CC production and subsequent expression of H(2)O(2)-responsive genes
CC (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, TGA9 and PAN (PubMed:16731568).
CC {ECO:0000250|UniProtKB:Q39140, ECO:0000269|PubMed:16731568,
CC ECO:0000269|PubMed:20805327}.
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 Comment=Additional isoforms seem to exist. {ECO:0000305};
CC Name=1;
CC IsoId=E3VNM4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E3VNM4-2; Sequence=VSP_058777;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in inflorescence apex and
CC flowers. {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: Strongly induced by flg22 in leaves.
CC {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=BAB11142.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ314787; CAC40649.1; -; mRNA.
DR EMBL; HQ132742; ADO95299.1; -; mRNA.
DR EMBL; AB010697; BAB11142.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91072.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91074.1; -; Genomic_DNA.
DR RefSeq; NP_001190244.1; NM_001203315.2. [E3VNM4-1]
DR RefSeq; NP_850784.1; NM_180453.2. [E3VNM4-2]
DR AlphaFoldDB; E3VNM4; -.
DR SMR; E3VNM4; -.
DR STRING; 3702.AT5G06839.3; -.
DR iPTMnet; E3VNM4; -.
DR PaxDb; E3VNM4; -.
DR PRIDE; E3VNM4; -.
DR ProteomicsDB; 246399; -. [E3VNM4-1]
DR EnsemblPlants; AT5G06839.1; AT5G06839.1; AT5G06839. [E3VNM4-2]
DR EnsemblPlants; AT5G06839.3; AT5G06839.3; AT5G06839. [E3VNM4-1]
DR GeneID; 830575; -.
DR Gramene; AT5G06839.1; AT5G06839.1; AT5G06839. [E3VNM4-2]
DR Gramene; AT5G06839.3; AT5G06839.3; AT5G06839. [E3VNM4-1]
DR KEGG; ath:AT5G06839; -.
DR Araport; AT5G06839; -.
DR TAIR; locus:1005716824; AT5G06839.
DR eggNOG; ENOG502QRKF; Eukaryota.
DR HOGENOM; CLU_024782_0_2_1; -.
DR InParanoid; E3VNM4; -.
DR OrthoDB; 722501at2759; -.
DR PRO; PR:E3VNM4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; E3VNM4; 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..460
FT /note="Transcription factor TGA10"
FT /id="PRO_0000438994"
FT DOMAIN 159..203
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT DOMAIN 236..455
FT /note="DOG1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01147"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..181
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 187..201
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOTIF 163..170
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 97..139
FT /note="Missing (in isoform 2)"
FT /id="VSP_058777"
FT CONFLICT 395
FT /note="S -> F (in Ref. 1; CAC40649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 460 AA; 51167 MW; F01C4E663FE7AD28 CRC64;
MQGHHQNHHQ HLSSSSATSS HGNFMNKDGY DIGEIDPSLF LYLDGQGHHD PPSTAPSPLH
HHHTTQNLAM RPPTSTLNIF PSQPMHIEPP PSSTHNTDNT RLVPAAQPSG STRPASDPSM
DLTNHSQFHQ PPQGSKSIKK EGNRKGLASS DHDIPKSSDP KTLRRLAQNR EAARKSRLRK
KAYVQQLESC RIKLTQLEQE IQRARSQGVF FGGSLIGGDQ QQGGLPIGPG NISSEAAVFD
MEYARWLEEQ QRLLNELRVA TQEHLSENEL RMFVDTCLAH YDHLINLKAM VAKTDVFHLI
SGAWKTPAER CFLWMGGFRP SEIIKVIVNQ IEPLTEQQIV GICGLQQSTQ EAEEALSQGL
EALNQSLSDS IVSDSLPPAS APLPPHLSNF MSHMSLALNK LSALEGFVLQ ADNLRHQTIH
RLNQLLTTRQ EARCLLAVAE YFHRLQALSS LWLARPRQDG
