PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
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(e.g., LFY)
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID XP_010558681.1
Organism
Tarenaya hassleriana
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Cleomaceae; Tarenaya
Family GRAS
Protein Properties Length: 533aa    MW: 58570 Da    PI: 4.8978
Description GRAS family protein
Gene Model
Gene Model ID Type Source Coding Sequence
XP_010558681.1genomeNCBIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1GRAS382.26.3e-1171735281374
            GRAS   1 lvelLlecAeavssgdlelaqalLarlselaspdgdpmqRlaayfteALaarlarsvselykalppsetseknsseelaalklfsevsPilkfsh 95 
                     lv++L++cA  v+ g+ ela+al++r+  la++++ +m ++a+yfteALa+r++r        + p +     s + +  +++    +P+lkf+h
  XP_010558681.1 173 LVHTLVACAX-VQLGNIELADALVKRVGLLAASQAGAMGKVATYFTEALARRIYR--------IFPGD-----SHDDVLKMHFHEPSCPYLKFAH 253
                     689******8.9*******************************************........22333.....3345555677889********* PP

            GRAS  96 ltaNqaIleavegeervHiiDfdisqGlQWpaLlqaLasRpegppslRiTgvgspesgskeeleetgerLakfAeelgvpfefnvlvakrledle 190
                     ltaNqaIlea++++++vH+iD+++ qG+QWpaL+qaLa R++gpps+   +vg+p s+  + ++++g++La++A+++gv+fef+ lv+++l+dle
  XP_010558681.1 254 LTANQAILEALSEAREVHVIDLGLRQGMQWPALMQALALRDGGPPSFHPPAVGPPPSETFDGVHQVGRKLARYADNIGVEFEFKGLVVDSLSDLE 348
                     *********************************************************************************************** PP

            GRAS 191 leeLrvkp.gEalaVnlvlqlhrlldesvsleserdevLklvkslsPkvvvvveqeadhnsesFlerflealeyysalfdsleaklpreseerik 284
                     +++++++p  E l+Vn+v+ lh ll++++s+e+    vL ++k+l+P++++vveqea+hn+  Fl+rf eal+yys+lfdsle+++    +++++
  XP_010558681.1 349 PDMFETRPeSEILVVNSVFGLHPLLARPGSIEK----VLAAMKKLRPDIMTVVEQEANHNGVVFLDRFNEALHYYSSLFDSLESSV---LSQDRV 436
                     ********9************************....*********************************************9997...677788 PP

            GRAS 285 vErellgreivnvvacegaerrerhetlekWrerleeaGFkpvplsekaakqaklllrkvk..sdgyrveeesgslvlgWkdrpLvsvSaWr 374
                     +++++lgr+ivnvv + g +r+erhetl +Wr r+++aGF pv+l++++ kqa++ll+ ++  ++gyrve+++g+++ gW++r+L+s+SaW+
  XP_010558681.1 437 MSEVYLGRQIVNVVGAGGGDRIERHETLTQWRTRMRSAGFVPVHLGSNVFKQASMLLAIFGggGNGYRVEDNHGCIMVGWHTRSLISTSAWK 528
                     99999*******************************************************988899*************************8 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SMARTSM011294.6E-2240111No hitNo description
PfamPF120411.4E-2140100IPR021914Transcriptional factor DELLA, N-terminal
PROSITE profilePS5098554.39147506IPR005202Transcription factor GRAS
PfamPF035142.2E-114173528IPR005202Transcription factor GRAS
Sequence ? help Back to Top
Protein Sequence    Length: 533 aa     Download sequence    Send to blast
MKRGHVESWD PSSGEGHSMV DKGKNPVSVS PDEGGADNMD ELFAVMGYKV RPLDMTGVAQ  60
KLQQLEMDLT HDDVTSGSLN DTVHYNPSEL SRWVEDMLES DDPTDLDPTR LGICGDGSEQ  120
DLWAIPGMSA YPADGPEDEN QSKRMRLEPW YDPLTGFDRP VVVAQSPEAG VRLVHTLVAC  180
AXVQLGNIEL ADALVKRVGL LAASQAGAMG KVATYFTEAL ARRIYRIFPG DSHDDVLKMH  240
FHEPSCPYLK FAHLTANQAI LEALSEAREV HVIDLGLRQG MQWPALMQAL ALRDGGPPSF  300
HPPAVGPPPS ETFDGVHQVG RKLARYADNI GVEFEFKGLV VDSLSDLEPD MFETRPESEI  360
LVVNSVFGLH PLLARPGSIE KVLAAMKKLR PDIMTVVEQE ANHNGVVFLD RFNEALHYYS  420
SLFDSLESSV LSQDRVMSEV YLGRQIVNVV GAGGGDRIER HETLTQWRTR MRSAGFVPVH  480
LGSNVFKQAS MLLAIFGGGG NGYRVEDNHG CIMVGWHTRS LISTSAWKLG ESL
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
5b3h_A3e-5516852713377Protein SCARECROW
5b3h_D3e-5516852713377Protein SCARECROW
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtProbable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway. No effect of the BOI proteins on its stability. Probably acts by participating in large multiprotein complexes that repress transcription of GA-inducible genes. Upon GA application, it is degraded by the proteasome, allowing the GA signaling pathway. Acts as a major GA-response repressor of seed germination, including seed thermoinhibition. Promotes the biosynthesis of abscisic acid (ABA), especially in seed coats to maintain seed dormancy. Delays flowering and adult leaf production. Also regulates the floral development, petal, stamen and anther development, by repressing the continued growth of floral organs. Its activity is probably regulated by other phytohormones such as auxin and ethylene. Involved in the regulation of seed dormancy and germination, including glucose-induced delay of seed germination. Promotes salt tolerance. Acts as a repressor of positive regulators of trichome initiation. Required during the flagellin-derived peptide flg22-mediated growth inhibition. Contributes to the susceptibility to the biotrophic pathogen P.syringae pv. tomato and to the resistance to the necrotrophic pathogens B.cinerea A.brassicicola, probably by repressing the SA-defense pathway and preventing cell death. Prevents stress-induced reactive oxygen species (ROS) accumulation (e.g. salt stress) by acting on the ROS scavenging system, and delays ROS-induced cell death, thus promoting stress tolerance. {ECO:0000269|PubMed:11877383, ECO:0000269|PubMed:12610625, ECO:0000269|PubMed:14615596, ECO:0000269|PubMed:14973286, ECO:0000269|PubMed:15128937, ECO:0000269|PubMed:16034591, ECO:0000269|PubMed:16400150, ECO:0000269|PubMed:16916886, ECO:0000269|PubMed:17141619, ECO:0000269|PubMed:17384169, ECO:0000269|PubMed:17704233, ECO:0000269|PubMed:18162586, ECO:0000269|PubMed:18450450, ECO:0000269|PubMed:18450451, ECO:0000269|PubMed:18941053, ECO:0000269|PubMed:20093430, ECO:0000269|PubMed:20956298}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapXP_010558681.1
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: Up-regulated transiently following seed imbibition to decline rapidly as germination proceeds; this induction is delayed at supraoptimal temperature conditions (e.g. 34 degrees Celsius). Accumulates in seed coats of dormant seeds where germination does not occur after imbibition. Increased levels upon abscisic acid (ABA) treatment. Down-regulated by norflurazon (NF), an ABA biosynthesis inhibitor. Induced by stress such as glucose, salt or mannitol treatment. {ECO:0000269|PubMed:11877383, ECO:0000269|PubMed:16916886, ECO:0000269|PubMed:17384169, ECO:0000269|PubMed:18162586, ECO:0000269|PubMed:18450450, ECO:0000269|PubMed:18941053, ECO:0000269|PubMed:20956298}.
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_010558681.10.0PREDICTED: LOW QUALITY PROTEIN: DELLA protein RGL2
SwissprotQ8GXW10.0RGL2_ARATH; DELLA protein RGL2
TrEMBLD7L0H60.0D7L0H6_ARALL; Uncharacterized protein
STRINGXP_010558681.10.0(Tarenaya hassleriana)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
MalvidsOGEM83728121
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT3G03450.10.0RGA-like 2
Publications ? help Back to Top
  1. Duarte JM, et al.
    Expression pattern shifts following duplication indicative of subfunctionalization and neofunctionalization in regulatory genes of Arabidopsis.
    Mol. Biol. Evol., 2006. 23(2): p. 469-78
    [PMID:16280546]
  2. Gallego-Giraldo C, et al.
    Role of the gibberellin receptors GID1 during fruit-set in Arabidopsis.
    Plant J., 2014. 79(6): p. 1020-1032
    [PMID:24961590]
  3. Fukazawa J, et al.
    DELLAs function as coactivators of GAI-ASSOCIATED FACTOR1 in regulation of gibberellin homeostasis and signaling in Arabidopsis.
    Plant Cell, 2014. 26(7): p. 2920-38
    [PMID:25035403]
  4. Hauvermale AL,Tuttle KM,Takebayashi Y,Seo M,Steber CM
    Loss of Arabidopsis thaliana Seed Dormancy is Associated with Increased Accumulation of the GID1 GA Hormone Receptors.
    Plant Cell Physiol., 2015. 56(9): p. 1773-85
    [PMID:26136598]
  5. Ibarra SE, et al.
    Molecular mechanisms underlying the entrance in secondary dormancy of Arabidopsis seeds.
    Plant Cell Environ., 2016. 39(1): p. 213-21
    [PMID:26177669]
  6. Zhong C, et al.
    Gibberellic Acid-Stimulated Arabidopsis6 Serves as an Integrator of Gibberellin, Abscisic Acid, and Glucose Signaling during Seed Germination in Arabidopsis.
    Plant Physiol., 2015. 169(3): p. 2288-303
    [PMID:26400990]
  7. Dave A,Vaistij FE,Gilday AD,Penfield SD,Graham IA
    Regulation of Arabidopsis thaliana seed dormancy and germination by 12-oxo-phytodienoic acid.
    J. Exp. Bot., 2016. 67(8): p. 2277-84
    [PMID:26873978]
  8. Kazachkova Y, et al.
    Salt Induces Features of a Dormancy-Like State in Seeds of Eutrema (Thellungiella) salsugineum, a Halophytic Relative of Arabidopsis.
    Front Plant Sci, 2016. 7: p. 1071
    [PMID:27536302]
  9. Liu X, et al.
    The NF-YC-RGL2 module integrates GA and ABA signalling to regulate seed germination in Arabidopsis.
    Nat Commun, 2016. 7: p. 12768
    [PMID:27624486]
  10. Ravindran P,Verma V,Stamm P,Kumar PP
    A Novel RGL2-DOF6 Complex Contributes to Primary Seed Dormancy in Arabidopsis thaliana by Regulating a GATA Transcription Factor.
    Mol Plant, 2017. 10(10): p. 1307-1320
    [PMID:28917589]