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TGA6_ARATH
ID   TGA6_ARATH              Reviewed;         330 AA.
AC   Q39140; Q9C7D1; Q9LHI1;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=Transcription factor TGA6;
DE   AltName: Full=bZIP transcription factor 45;
DE            Short=AtbZIP45;
GN   Name=TGA6; Synonyms=BZIP45; OrderedLocusNames=At3g12250;
GN   ORFNames=F28J15.6, MQC3.8;
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).
RC   STRAIN=cv. Columbia; TISSUE=Leaf;
RA   Xiang C., Miao Z.-H., Lam E.;
RT   "Isolation of TGA6, a new member of the TGA family of bZIP transcription
RT   factors in Arabidopsis thaliana.";
RL   (er) Plant Gene Register PGR95-063(1995).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
RN   [5]
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   [6]
RP   CHARACTERIZATION, AND DNA-BINDING.
RX   PubMed=9225852; DOI=10.1023/a:1005873500238;
RA   Xiang C., Miao Z.-H., Lam E.;
RT   "DNA-binding properties, genomic organization and expression pattern of
RT   TGA6, a new member of the TGA family of bZIP transcription factors in
RT   Arabidopsis thaliana.";
RL   Plant Mol. Biol. 34:403-415(1997).
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   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   [9]
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   [10]
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).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds DNA as a dimer. Interacts with NPR1, NPR3 and NPR4.
CC       Interacts with GRXC9/GRX480. {ECO:0000269|PubMed:10659709,
CC       ECO:0000269|PubMed:15634206, ECO:0000269|PubMed:17076807,
CC       ECO:0000269|PubMed:17397508}.
CC   -!- INTERACTION:
CC       Q39140; Q9ZUM0: At2g02160; NbExp=3; IntAct=EBI-541321, EBI-15206592;
CC       Q39140; Q9SGP6: GRXC9; NbExp=4; IntAct=EBI-541321, EBI-1545762;
CC       Q39140; P93002: NPR1; NbExp=5; IntAct=EBI-541321, EBI-1392127;
CC       Q39140; Q9XE58: SCL14; NbExp=3; IntAct=EBI-541321, EBI-25523217;
CC       Q39140; Q39234: TGA3; NbExp=3; IntAct=EBI-541321, EBI-541366;
CC       Q39140; Q39163: TGA5; NbExp=3; IntAct=EBI-541321, EBI-541381;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q39140-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q39140-2; Sequence=VSP_009468;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in roots and flowers.
CC   -!- DEVELOPMENTAL STAGE: Expressed primarily in roots of young seedlings
CC       and later expressed in aging cotyledons, mesophyll cells of hydathodes
CC       on leaf margins, vascular tissue and trichomes of senescing rosette
CC       leaves. Also detected in young lateral roots and in mature pollen
CC       grains.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB03134.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; L42327; AAC37470.1; -; mRNA.
DR   EMBL; AJ320540; CAC42807.1; -; mRNA.
DR   EMBL; AC069472; AAG51079.1; -; Genomic_DNA.
DR   EMBL; AP002047; BAB03134.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE75172.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75173.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75174.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM63961.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM63962.1; -; Genomic_DNA.
DR   RefSeq; NP_001326019.1; NM_001337984.1. [Q39140-1]
DR   RefSeq; NP_001326020.1; NM_001337985.1. [Q39140-1]
DR   RefSeq; NP_566415.3; NM_112061.6. [Q39140-1]
DR   RefSeq; NP_974292.1; NM_202563.3. [Q39140-1]
DR   RefSeq; NP_974293.1; NM_202564.2. [Q39140-2]
DR   AlphaFoldDB; Q39140; -.
DR   BioGRID; 5739; 16.
DR   IntAct; Q39140; 15.
DR   STRING; 3702.AT3G12250.4; -.
DR   iPTMnet; Q39140; -.
DR   PRIDE; Q39140; -.
DR   ProteomicsDB; 234213; -. [Q39140-1]
DR   EnsemblPlants; AT3G12250.1; AT3G12250.1; AT3G12250. [Q39140-1]
DR   EnsemblPlants; AT3G12250.2; AT3G12250.2; AT3G12250. [Q39140-1]
DR   EnsemblPlants; AT3G12250.3; AT3G12250.3; AT3G12250. [Q39140-2]
DR   EnsemblPlants; AT3G12250.6; AT3G12250.6; AT3G12250. [Q39140-1]
DR   EnsemblPlants; AT3G12250.7; AT3G12250.7; AT3G12250. [Q39140-1]
DR   GeneID; 820405; -.
DR   Gramene; AT3G12250.1; AT3G12250.1; AT3G12250. [Q39140-1]
DR   Gramene; AT3G12250.2; AT3G12250.2; AT3G12250. [Q39140-1]
DR   Gramene; AT3G12250.3; AT3G12250.3; AT3G12250. [Q39140-2]
DR   Gramene; AT3G12250.6; AT3G12250.6; AT3G12250. [Q39140-1]
DR   Gramene; AT3G12250.7; AT3G12250.7; AT3G12250. [Q39140-1]
DR   KEGG; ath:AT3G12250; -.
DR   Araport; AT3G12250; -.
DR   eggNOG; ENOG502QU32; Eukaryota.
DR   InParanoid; Q39140; -.
DR   PhylomeDB; Q39140; -.
DR   PRO; PR:Q39140; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q39140; baseline and differential.
DR   Genevisible; Q39140; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:UniProt.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR018524; DNA/RNA_endonuclease_AS.
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; Coiled coil; DNA-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..330
FT                   /note="Transcription factor TGA6"
FT                   /id="PRO_0000076558"
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..45
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..233
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        10..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..22
FT                   /note="MADTSSRTDVSTDGDTDHRDLG -> MHSLNETVIPDVDYMQ (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_009468"
FT   CONFLICT        74
FT                   /note="N -> D (in Ref. 1; AAC37470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82
FT                   /note="L -> V (in Ref. 1; AAC37470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        110
FT                   /note="G -> GG (in Ref. 1; AAC37470/BAB03134)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167
FT                   /note="A -> S (in Ref. 1; AAC37470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        194
FT                   /note="R -> P (in Ref. 1; AAC37470)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        272
FT                   /note="Q -> K (in Ref. 1; AAC37470)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   330 AA;  36850 MW;  2A55F2F336648A48 CRC64;
     MADTSSRTDV STDGDTDHRD LGSDRGHMHA AASDSSDRSK DKLDQKTLRR LAQNREAARK
     SRLRKKAYVQ QLENSRLKLT QLEQELQRAR QQGVFISSSG DQAHSTGGNG ALAFDAEHSR
     WLEEKNRQMN ELRSALNAHA GDTELRIIVD GVMAHYEELF RIKSNAAKND VFHLLSGMWK
     TPAERCFLWL GGFRSSELLK LLANQLEPMT ERQVMGINSL QQTSQQAEDA LSQGMESLQQ
     SLADTLSSGT LGSSSSDNVA SYMGQMAMAM GQLGTLEGFI RQADNLRLQT LQQMLRVLTT
     RQSARALLAI HDYSSRLRAL SSLWLARPRE
 
 
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