EOT1_SOLLC
ID EOT1_SOLLC Reviewed; 351 AA.
AC K4B6C9;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Protein EXPRESSION OF TERPENOIDS 1 {ECO:0000303|PubMed:24142382};
DE Short=SlEOT1 {ECO:0000303|PubMed:24142382};
GN Name=EOT1 {ECO:0000303|PubMed:24142382};
GN OrderedLocusNames=Solyc02g062400 {ECO:0000305};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24142382; DOI=10.1007/s11103-013-0142-0;
RA Spyropoulou E.A., Haring M.A., Schuurink R.C.;
RT "Expression of Terpenoids 1, a glandular trichome-specific transcription
RT factor from tomato that activates the terpene synthase 5 promoter.";
RL Plant Mol. Biol. 84:345-357(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [3]
RP FUNCTION.
RX PubMed=24884371; DOI=10.1186/1471-2164-15-402;
RA Spyropoulou E.A., Haring M.A., Schuurink R.C.;
RT "RNA sequencing on Solanum lycopersicum trichomes identifies transcription
RT factors that activate terpene synthase promoters.";
RL BMC Genomics 15:402-402(2014).
CC -!- FUNCTION: Transcription activator involved in the transcriptional
CC regulation of terpene biosynthesis in glandular trichomes
CC (PubMed:24884371, PubMed:24142382). Binds to the promoter of the
CC linalool synthase TPS5 and promotes TPS5 gene transactivation
CC (PubMed:24884371, PubMed:24142382). Acts synergistically with MYC1 in
CC the transactivation of TPS5 (PubMed:24884371).
CC {ECO:0000269|PubMed:24142382, ECO:0000269|PubMed:24884371}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with LRP1.
CC {ECO:0000250|UniProtKB:Q9SD40}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24142382}.
CC -!- SIMILARITY: Belongs to the SHI protein family. {ECO:0000305}.
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DR EMBL; KC331910; AGW27396.1; -; mRNA.
DR EMBL; CM001065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001274697.1; NM_001287768.1.
DR AlphaFoldDB; K4B6C9; -.
DR STRING; 4081.Solyc02g062400.2.1; -.
DR PaxDb; K4B6C9; -.
DR PRIDE; K4B6C9; -.
DR EnsemblPlants; Solyc02g062400.3.1; Solyc02g062400.3.1; Solyc02g062400.3.
DR GeneID; 101251254; -.
DR Gramene; Solyc02g062400.3.1; Solyc02g062400.3.1; Solyc02g062400.3.
DR KEGG; sly:101251254; -.
DR eggNOG; ENOG502QQ15; Eukaryota.
DR HOGENOM; CLU_041493_1_0_1; -.
DR InParanoid; K4B6C9; -.
DR OMA; VFQCIQM; -.
DR OrthoDB; 1014431at2759; -.
DR PhylomeDB; K4B6C9; -.
DR Proteomes; UP000004994; Chromosome 2.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR007818; SHI.
DR InterPro; IPR006511; SHI_C.
DR InterPro; IPR006510; Znf_LRP1.
DR PANTHER; PTHR31604; PTHR31604; 1.
DR TIGRFAMs; TIGR01624; LRP1_Cterm; 1.
DR TIGRFAMs; TIGR01623; put_zinc_LRP1; 1.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..351
FT /note="Protein EXPRESSION OF TERPENOIDS 1"
FT /id="PRO_0000447555"
FT DNA_BIND 129..156
FT /note="Zn(2)-C6 fungal-type; degenerate"
FT /evidence="ECO:0000305"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 258..261
FT /note="Required for homo- and heterodimerization"
FT /evidence="ECO:0000250|UniProtKB:Q9SD40"
FT COMPBIAS 175..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 38501 MW; 1633DD2C338EBE5F CRC64;
MANFFSLGGN QEQQHQEISS SQALVPTESN NWFLYRNEHH HHHHNQEIPN TYKGFELWQS
GNTPQHQHQH HQQQQQFRHP IYPLQDLYST DVGLGVGPSR SGFDISAGDH EASRSGFVMM
RSGGGGISCQ DCGNQAKKDC QHMRCRTCCK SRGFQCQTHV KSTWVPAAKR RERQQQLAAL
QQQQQGHNNN NNNHKNKRQR EDPSASSLVS TRLPSNTNGL EVGKFPSKVR TSAVFQCIQM
SSIEDDEDQL AYQAAVSIGG HVFKGILYDQ GHESQYNNMV AAGGDTSSGG SAGGVQHHHH
NSAAVATATT TSGGDATAAG PSNFLDPSLF PAPLSTFMVA GTQFFPPSRS P
