TGT1_ARATH
ID TGT1_ARATH Reviewed; 406 AA.
AC Q9FX53; B3H720; Q2L6T7; Q39116;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Trihelix transcription factor GT-1;
DE AltName: Full=Trihelix DNA-binding protein GT-1;
GN Name=GT-1; OrderedLocusNames=At1g13450; ORFNames=T6J4.18;
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), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF GLN-89; GLN-118 AND LEU-143.
RC STRAIN=cv. Columbia;
RX PubMed=7866025; DOI=10.2307/3869909;
RA Hiratsuka K., Wu X., Fukuzawa H., Chua N.H.;
RT "Molecular dissection of GT-1 from Arabidopsis.";
RL Plant Cell 6:1805-1813(1994).
RN [2]
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 [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] (ISOFORM 1).
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-406 (ISOFORM 3).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [6]
RP FUNCTION.
RX PubMed=15044016; DOI=10.1016/s0014-5793(04)00222-4;
RA Ayadi M., Delaporte V., Li Y.F., Zhou D.X.;
RT "Analysis of GT-3a identifies a distinct subgroup of trihelix DNA-binding
RT transcription factors in Arabidopsis.";
RL FEBS Lett. 562:147-154(2004).
RN [7]
RP FUNCTION, PHOSPHORYLATION AT THR-133 AND SER-198, AND MUTAGENESIS OF
RP THR-86; THR-133; SER-175; THR-179; SER-198 AND THR-278.
RX PubMed=10437822; DOI=10.1023/a:1006131330930;
RA Marechal E., Hiratsuka K., Delgado J., Nairn A., Qin J., Chait B.T.,
RA Chua N.H.;
RT "Modulation of GT-1 DNA-binding activity by calcium-dependent
RT phosphorylation.";
RL Plant Mol. Biol. 40:373-386(1999).
RN [8]
RP STRUCTURE BY NMR OF 81-166, AND MUTAGENESIS OF THR-133.
RX PubMed=20717979; DOI=10.1002/prot.22827;
RA Nagata T., Niyada E., Fujimoto N., Nagasaki Y., Noto K., Miyanoiri Y.,
RA Murata J., Hiratsuka K., Katahira M.;
RT "Solution structures of the trihelix DNA-binding domains of the wild-type
RT and a phosphomimetic mutant of Arabidopsis GT-1: Mechanism for an increase
RT in DNA-binding affinity through phosphorylation.";
RL Proteins 78:3033-3047(2010).
CC -!- FUNCTION: Probable transcription factor that binds specifically to the
CC core DNA sequence 5'-GGTTAA-3'. May act as a molecular switch in
CC response to light signals. {ECO:0000269|PubMed:10437822,
CC ECO:0000269|PubMed:15044016, ECO:0000269|PubMed:7866025}.
CC -!- SUBUNIT: Binds DNA as homodimer. {ECO:0000269|PubMed:7866025}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7866025}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9FX53-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FX53-2; Sequence=VSP_040173;
CC Name=3;
CC IsoId=Q9FX53-3; Sequence=VSP_040174, VSP_040175;
CC -!- PTM: Phosphorylated on Thr-133 and Ser-198. Phosphorylation is calcium-
CC dependent and increases DNA-binding activity 10 to 20-fold.
CC {ECO:0000269|PubMed:10437822}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX813511; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; L36806; AAA66473.1; -; mRNA.
DR EMBL; AC011810; AAG09542.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29018.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29019.2; -; Genomic_DNA.
DR EMBL; CP002684; AEE29020.1; -; Genomic_DNA.
DR EMBL; AK228305; BAF00248.1; -; mRNA.
DR EMBL; BX813511; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001117279.1; NM_001123807.2. [Q9FX53-3]
DR RefSeq; NP_001318993.1; NM_001332067.1. [Q9FX53-3]
DR RefSeq; NP_172802.2; NM_101215.4. [Q9FX53-1]
DR PDB; 2EBI; NMR; -; A=81-166.
DR PDB; 2JMW; NMR; -; A=81-166.
DR PDBsum; 2EBI; -.
DR PDBsum; 2JMW; -.
DR AlphaFoldDB; Q9FX53; -.
DR SMR; Q9FX53; -.
DR BioGRID; 23145; 47.
DR IntAct; Q9FX53; 44.
DR STRING; 3702.AT1G13450.1; -.
DR iPTMnet; Q9FX53; -.
DR PaxDb; Q9FX53; -.
DR PRIDE; Q9FX53; -.
DR ProteomicsDB; 234212; -. [Q9FX53-1]
DR EnsemblPlants; AT1G13450.1; AT1G13450.1; AT1G13450. [Q9FX53-1]
DR EnsemblPlants; AT1G13450.2; AT1G13450.2; AT1G13450. [Q9FX53-3]
DR EnsemblPlants; AT1G13450.3; AT1G13450.3; AT1G13450. [Q9FX53-3]
DR GeneID; 837905; -.
DR Gramene; AT1G13450.1; AT1G13450.1; AT1G13450. [Q9FX53-1]
DR Gramene; AT1G13450.2; AT1G13450.2; AT1G13450. [Q9FX53-3]
DR Gramene; AT1G13450.3; AT1G13450.3; AT1G13450. [Q9FX53-3]
DR KEGG; ath:AT1G13450; -.
DR Araport; AT1G13450; -.
DR TAIR; locus:2009897; AT1G13450.
DR eggNOG; KOG4282; Eukaryota.
DR HOGENOM; CLU_052933_1_0_1; -.
DR InParanoid; Q9FX53; -.
DR OMA; KVDSFMH; -.
DR OrthoDB; 866865at2759; -.
DR PhylomeDB; Q9FX53; -.
DR EvolutionaryTrace; Q9FX53; -.
DR PRO; PR:Q9FX53; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FX53; baseline and differential.
DR Genevisible; Q9FX53; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR InterPro; IPR044822; Myb_DNA-bind_4.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF13837; Myb_DNA-bind_4; 1.
DR SMART; SM00717; SANT; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..406
FT /note="Trihelix transcription factor GT-1"
FT /id="PRO_0000401378"
FT DOMAIN 79..143
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 133
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:10437822"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10437822"
FT VAR_SEQ 219..263
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040173"
FT VAR_SEQ 265..278
FT /note="DDSHGQPFGGRVIT -> KSSEKAYINLSLKV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_040174"
FT VAR_SEQ 279..406
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_040175"
FT MUTAGEN 86
FT /note="T->A: No significant change in DNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:10437822"
FT MUTAGEN 86
FT /note="T->D: No significant change in DNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:10437822"
FT MUTAGEN 89
FT /note="Q->P: Decreases strongly DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:7866025"
FT MUTAGEN 118
FT /note="Q->P: Abolishes DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:7866025"
FT MUTAGEN 133
FT /note="T->A: Decreases DNA-binding activity 2-fold."
FT /evidence="ECO:0000269|PubMed:10437822,
FT ECO:0000269|PubMed:20717979"
FT MUTAGEN 133
FT /note="T->D: Increases DNA-binding activity 3-fold."
FT /evidence="ECO:0000269|PubMed:10437822,
FT ECO:0000269|PubMed:20717979"
FT MUTAGEN 143
FT /note="L->P: Abolishes DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:7866025"
FT MUTAGEN 175
FT /note="S->A: No significant change in DNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:10437822"
FT MUTAGEN 175
FT /note="S->D: No significant change in DNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:10437822"
FT MUTAGEN 179
FT /note="T->A: No significant change in DNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:10437822"
FT MUTAGEN 179
FT /note="T->D: No significant change in DNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:10437822"
FT MUTAGEN 198
FT /note="S->A: No significant change in DNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:10437822"
FT MUTAGEN 198
FT /note="S->D: Decreases DNA-binding activity 8-fold."
FT /evidence="ECO:0000269|PubMed:10437822"
FT MUTAGEN 278
FT /note="T->A: No significant change in DNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:10437822"
FT MUTAGEN 278
FT /note="T->D: No significant change in DNA-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:10437822"
FT CONFLICT 376
FT /note="R -> L (in Ref. 1; AAA66473)"
FT /evidence="ECO:0000305"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2JMW"
FT HELIX 89..108
FT /evidence="ECO:0007829|PDB:2EBI"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:2EBI"
FT HELIX 132..146
FT /evidence="ECO:0007829|PDB:2EBI"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2JMW"
SQ SEQUENCE 406 AA; 46676 MW; 0075E3A61B1CDE16 CRC64;
MFISDKSRPT DFYKDDHHNS STTSTTRDMM IDVLTTTNES VDLQSHHHHN HHNHHLHQSQ
PQQQILLGES SGEDHEVKAP KKRAETWVQD ETRSLIMFRR GMDGLFNTSK SNKHLWEQIS
SKMREKGFDR SPTMCTDKWR NLLKEFKKAK HHDRGNGSAK MSYYKEIEDI LRERSKKVTP
PQYNKSPNTP PTSAKVDSFM QFTDKGFDDT SISFGSVEAN GRPALNLERR LDHDGHPLAI
TTAVDAVAAN GVTPWNWRET PGNGDDSHGQ PFGGRVITVK FGDYTRRIGV DGSAEAIKEV
IRSAFGLRTR RAFWLEDEDQ IIRCLDRDMP LGNYLLRLDD GLAIRVCHYD ESNQLPVHSE
EKIFYTEEDY REFLARQGWS SLQVDGFRNI ENMDDLQPGA VYRGVR
