ID TGA2_ARATH Reviewed; 330 AA. AC P43273; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 24-JAN-2024, entry version 176. DE RecName: Full=Transcription factor TGA2; DE AltName: Full=HBP-1b homolog; DE Short=AHBP-1b; DE AltName: Full=bZIP transcription factor 20; DE Short=AtbZIP20; GN Name=TGA2; Synonyms=BZIP20, HBP1B; OrderedLocusNames=At5g06950; GN ORFNames=MOJ9.12; 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. Landsberg erecta; RX PubMed=1549479; DOI=10.1093/nar/20.5.1141; RA Kawata T., Imada T., Shiraishi H., Okada K., Shimura Y., Iwabuchi M.; RT "A cDNA clone encoding HBP-1b homologue in Arabidopsis thaliana."; RL Nucleic Acids Res. 20:1141-1141(1992). RN [2] 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 [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=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 [5] 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 [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 CHARACTERIZATION. 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 INTERACTION WITH NPR1. RX PubMed=10659709; DOI=10.1094/mpmi.2000.13.2.191; RA Zhou J.-M., Trifa Y., Silva H., Pontier D., Lam E., Shah J., Klessig D.F.; RT "NPR1 differentially interacts with members of the TGA/OBF family of RT transcription factors that bind an element of the PR-1 gene required for RT induction by salicylic acid."; RL Mol. Plant Microbe Interact. 13:191-202(2000). RN [9] 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 [10] RP FUNCTION. RX PubMed=12897257; DOI=10.1105/tpc.012211; RA Johnson C., Boden E., Arias J.; RT "Salicylic acid and NPR1 induce the recruitment of trans-activating TGA RT factors to a defense gene promoter in Arabidopsis."; RL Plant Cell 15:1846-1858(2003). RN [11] RP INTERACTION WITH NPR1 AND NPR4. RX PubMed=15634206; DOI=10.1111/j.1365-313x.2004.02296.x; RA Liu G., Holub E.B., Alonso J.M., Ecker J.R., Fobert P.R.; RT "An Arabidopsis NPR1-like gene, NPR4, is required for disease resistance."; RL Plant J. 41:304-318(2005). RN [12] RP INTERACTION WITH NPR3 AND NPR4. RX PubMed=17076807; DOI=10.1111/j.1365-313x.2006.02903.x; RA Zhang Y., Cheng Y.T., Qu N., Zhao Q., Bi D., Li X.; RT "Negative regulation of defense responses in Arabidopsis by two NPR1 RT paralogs."; RL Plant J. 48:647-656(2006). RN [13] RP INTERACTION WITH GRXC9/GRX480. RX PubMed=17397508; DOI=10.1111/j.1365-313x.2007.03039.x; RA Ndamukong I., Abdallat A.A., Thurow C., Fode B., Zander M., Weigel R., RA Gatz C.; RT "SA-inducible Arabidopsis glutaredoxin interacts with TGA factors and RT suppresses JA-responsive PDF1.2 transcription."; RL Plant J. 50:128-139(2007). RN [14] RP INTERACTION WITH GRXC7/ROXY1. RX PubMed=19218396; DOI=10.1105/tpc.108.064477; RA Li S., Lauri A., Ziemann M., Busch A., Bhave M., Zachgo S.; RT "Nuclear activity of ROXY1, a glutaredoxin interacting with TGA factors, is RT required for petal development in Arabidopsis thaliana."; RL Plant Cell 21:429-441(2009). 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. CC Required to induce the systemic acquired resistance (SAR) via the CC regulation of pathogenesis-related genes expression. Binding to the as- CC 1 element of PR-1 promoter is salicylic acid-inducible and mediated by CC NPR1. Could also bind to the C-boxes (5'-ATGACGTCAT-3') with high CC affinity. {ECO:0000269|PubMed:12897257}. CC -!- SUBUNIT: Binds DNA as a dimer. Interacts with NPR1, NPR3 and NPR4. CC Interacts with GRXC7/ROXY1 and GRXC9/GRX480. CC {ECO:0000269|PubMed:10659709, ECO:0000269|PubMed:15634206, CC ECO:0000269|PubMed:17076807, ECO:0000269|PubMed:17397508, CC ECO:0000269|PubMed:19218396}. CC -!- INTERACTION: CC P43273; Q8VYD2: GPL1; NbExp=6; IntAct=EBI-541307, EBI-4426914; CC P43273; Q96305: GRXC7; NbExp=3; IntAct=EBI-541307, EBI-2257898; CC P43273; Q8LF89: GRXC8; NbExp=2; IntAct=EBI-541307, EBI-4434651; CC P43273; Q9SGP6: GRXC9; NbExp=6; IntAct=EBI-541307, EBI-1545762; CC P43273; P93002: NPR1; NbExp=12; IntAct=EBI-541307, EBI-1392127; CC P43273; Q8L9W4: NPR1; NbExp=7; IntAct=EBI-541307, EBI-541093; CC P43273; Q8L746: NPR3; NbExp=9; IntAct=EBI-541307, EBI-4441365; CC P43273; Q9S7H5: SCL21; NbExp=3; IntAct=EBI-541307, EBI-1238472; CC P43273; Q39234: TGA3; NbExp=3; IntAct=EBI-541307, EBI-541366; CC P43273; Q39163: TGA5; NbExp=8; IntAct=EBI-541307, EBI-541381; CC P43273; Q93ZE2: TGA7; NbExp=3; IntAct=EBI-541307, EBI-541400; CC P43273; Q93XM6: TGA9; NbExp=4; IntAct=EBI-541307, EBI-1237844; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: Expressed in the whole plant. 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; D10042; BAA00933.1; -; mRNA. DR EMBL; AB010697; BAB11153.1; -; Genomic_DNA. DR EMBL; CP002688; AED91085.1; -; Genomic_DNA. DR EMBL; CP002688; AED91086.1; -; Genomic_DNA. DR EMBL; CP002688; AED91087.1; -; Genomic_DNA. DR EMBL; CP002688; AED91088.1; -; Genomic_DNA. DR EMBL; CP002688; ANM69734.1; -; Genomic_DNA. DR EMBL; AK117686; BAC42338.1; -; mRNA. DR EMBL; BT006134; AAP04119.1; -; mRNA. DR PIR; S35439; S35439. DR RefSeq; NP_001031845.1; NM_001036768.2. DR RefSeq; NP_001078539.1; NM_001085070.2. DR RefSeq; NP_001331392.1; NM_001342913.1. DR RefSeq; NP_196312.1; NM_120777.3. DR RefSeq; NP_974744.1; NM_203015.1. DR AlphaFoldDB; P43273; -. DR SMR; P43273; -. DR BioGRID; 15865; 37. DR ComplexPortal; CPX-3572; TGA2-NPR1 complex. DR ComplexPortal; CPX-3601; TGA2 complex. DR IntAct; P43273; 24. DR STRING; 3702.P43273; -. DR PaxDb; 3702-AT5G06950-1; -. DR ProteomicsDB; 246401; -. DR EnsemblPlants; AT5G06950.1; AT5G06950.1; AT5G06950. DR EnsemblPlants; AT5G06950.2; AT5G06950.2; AT5G06950. DR EnsemblPlants; AT5G06950.3; AT5G06950.3; AT5G06950. DR EnsemblPlants; AT5G06950.4; AT5G06950.4; AT5G06950. DR EnsemblPlants; AT5G06950.5; AT5G06950.5; AT5G06950. DR GeneID; 830586; -. DR Gramene; AT5G06950.1; AT5G06950.1; AT5G06950. DR Gramene; AT5G06950.2; AT5G06950.2; AT5G06950. DR Gramene; AT5G06950.3; AT5G06950.3; AT5G06950. DR Gramene; AT5G06950.4; AT5G06950.4; AT5G06950. DR Gramene; AT5G06950.5; AT5G06950.5; AT5G06950. DR KEGG; ath:AT5G06950; -. DR Araport; AT5G06950; -. DR TAIR; AT5G06950; AHBP-1B. DR eggNOG; ENOG502QU32; Eukaryota. DR HOGENOM; CLU_024782_1_1_1; -. DR InParanoid; P43273; -. DR OMA; VFHLMSG; -. DR OrthoDB; 465017at2759; -. DR PhylomeDB; P43273; -. DR PRO; PR:P43273; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; P43273; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:TAIR. DR GO; GO:0005634; C:nucleus; IDA:TAIR. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal. DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IPI:ComplexPortal. DR GO; GO:0003677; F:DNA binding; IDA:TAIR. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:ComplexPortal. DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:TAIR. DR GO; GO:0009410; P:response to xenobiotic stimulus; IGI:TAIR. DR GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IDA:ComplexPortal. DR Gene3D; 1.20.5.170; -; 1. DR InterPro; IPR004827; bZIP. DR InterPro; IPR046347; bZIP_sf. DR InterPro; IPR025422; TGA_domain. DR PANTHER; PTHR45693:SF46; TRANSCRIPTION FACTOR TGA2-RELATED; 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; P43273; AT. PE 1: Evidence at protein level; KW Activator; Coiled coil; DNA-binding; Hypersensitive response; Nucleus; KW Plant defense; Reference proteome; Transcription; Transcription regulation. FT CHAIN 1..330 FT /note="Transcription factor TGA2" FT /id="PRO_0000076554" FT DOMAIN 44..107 FT /note="bZIP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT DOMAIN 111..327 FT /note="DOG1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01147" FT REGION 1..48 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 46..66 FT /note="Basic motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 72..86 FT /note="Leucine-zipper" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT COILED 45..142 FT /evidence="ECO:0000255" FT COILED 217..244 FT /evidence="ECO:0000255" SQ SEQUENCE 330 AA; 36684 MW; D3033153BCE932C4 CRC64; MADTSPRTDV STDDDTDHPD LGSEGALVNT AASDSSDRSK GKMDQKTLRR LAQNREAARK SRLRKKAYVQ QLENSRLKLT QLEQELQRAR QQGVFISGTG DQAHSTGGNG ALAFDAEHSR WLEEKNKQMN ELRSALNAHA GDSELRIIVD GVMAHYEELF RIKSNAAKND VFHLLSGMWK TPAERCFLWL GGFRSSELLK LLANQLEPMT ERQLMGINNL QQTSQQAEDA LSQGMESLQQ SLADTLSSGT LGSSSSGNVA SYMGQMAMAM GKLGTLEGFI RQADNLRLQT LQQMIRVLTT RQSARALLAI HDYFSRLRAL SSLWLARPRE //