TGA5_ARATH
ID TGA5_ARATH Reviewed; 330 AA.
AC Q39163; Q9FL50;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Transcription factor TGA5;
DE AltName: Full=Ocs element-binding factor 5;
DE Short=OBF5;
DE AltName: Full=bZIP transcription factor 26;
DE Short=AtbZIP26;
GN Name=TGA5; Synonyms=BZIP26, OBF5; OrderedLocusNames=At5g06960;
GN ORFNames=MOJ9.13;
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-330.
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 [5]
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 [6]
RP INTERACTION WITH OBP1.
RX PubMed=8718629; DOI=10.2307/3870165;
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 [7]
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 [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 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 [10]
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).
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 protein
CC OBP1 enhances the binding to the ocs element. Interacts with NPR1, NPR3
CC and NPR4. {ECO:0000269|PubMed:10659709, ECO:0000269|PubMed:15634206,
CC ECO:0000269|PubMed:17076807, ECO:0000269|PubMed:8718629}.
CC -!- INTERACTION:
CC Q39163; P93002: NPR1; NbExp=8; IntAct=EBI-541381, EBI-1392127;
CC Q39163; Q8L9W4: NPR1; NbExp=4; IntAct=EBI-541381, EBI-541093;
CC Q39163; Q8L746: NPR3; NbExp=4; IntAct=EBI-541381, EBI-4441365;
CC Q39163; P43273: TGA2; NbExp=8; IntAct=EBI-541381, EBI-541307;
CC Q39163; Q39234: TGA3; NbExp=7; IntAct=EBI-541381, EBI-541366;
CC Q39163; Q39163: TGA5; NbExp=2; IntAct=EBI-541381, EBI-541381;
CC Q39163; Q39140: TGA6; NbExp=3; IntAct=EBI-541381, EBI-541321;
CC Q39163; Q93ZE2: TGA7; NbExp=7; IntAct=EBI-541381, EBI-541400;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in roots.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; AB010697; BAB11154.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91089.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91090.1; -; Genomic_DNA.
DR EMBL; AY058830; AAL24218.1; -; mRNA.
DR EMBL; AY143864; AAN28803.1; -; mRNA.
DR EMBL; X69900; CAA49525.1; -; mRNA.
DR PIR; S48122; S48122.
DR RefSeq; NP_196313.1; NM_120778.4.
DR RefSeq; NP_974745.1; NM_203016.2.
DR AlphaFoldDB; Q39163; -.
DR SMR; Q39163; -.
DR BioGRID; 15866; 20.
DR IntAct; Q39163; 17.
DR STRING; 3702.AT5G06960.1; -.
DR PaxDb; Q39163; -.
DR PRIDE; Q39163; -.
DR ProteomicsDB; 234410; -.
DR EnsemblPlants; AT5G06960.1; AT5G06960.1; AT5G06960.
DR EnsemblPlants; AT5G06960.2; AT5G06960.2; AT5G06960.
DR GeneID; 830587; -.
DR Gramene; AT5G06960.1; AT5G06960.1; AT5G06960.
DR Gramene; AT5G06960.2; AT5G06960.2; AT5G06960.
DR KEGG; ath:AT5G06960; -.
DR Araport; AT5G06960; -.
DR TAIR; locus:2169409; AT5G06960.
DR eggNOG; ENOG502QU32; Eukaryota.
DR HOGENOM; CLU_024782_1_1_1; -.
DR InParanoid; Q39163; -.
DR OrthoDB; 1018848at2759; -.
DR PhylomeDB; Q39163; -.
DR PRO; PR:Q39163; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39163; baseline and differential.
DR Genevisible; Q39163; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0098542; P:defense response to other organism; TAS:TAIR.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IGI:TAIR.
DR GO; GO:0009863; P:salicylic acid mediated signaling pathway; IPI: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; Coiled coil; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..330
FT /note="Transcription factor TGA5"
FT /id="PRO_0000076557"
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..64
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..98
FT /evidence="ECO:0000255"
FT COILED 211..244
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 204
FT /note="S -> C (in Ref. 4; CAA49525)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="S -> T (in Ref. 4; CAA49525)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 36890 MW; 645062F0F3351869 CRC64;
MGDTSPRTSV STDGDTDHNN LMFDEGHLGI GASDSSDRSK SKMDQKTLRR LAQNREAARK
SRLRKKAYVQ QLENSRLKLT QLEQELQRAR QQGVFISSSG DQAHSTAGDG AMAFDVEYRR
WQEDKNRQMK ELSSAIDSHA TDSELRIIVD GVIAHYEELY RIKGNAAKSD VFHLLSGMWK
TPAERCFLWL GGFRSSELLK LIASQLEPLT EQQSLDINNL QQSSQQAEDA LSQGMDNLQQ
SLADTLSSGT LGSSSSGNVA SYMGQMAMAM GKLGTLEGFI RQADNLRLQT YQQMVRLLTT
RQSARALLAV HNYTLRLRAL SSLWLARPRE
