PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
Previous version: v3.0 v4.0
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID C.cajan_09277
Common NameKK1_009538
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Cajanus
Family HSF
Protein Properties Length: 337aa    MW: 38286.9 Da    PI: 5.3012
Description HSF family protein
Gene Model
Gene Model ID Type Source Coding Sequence
C.cajan_09277genomeIIPGView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1HSF_DNA-bind113.71.2e-35431342102
                    HHHHHHHHHCTGGGTTTSEESSSSSEEEES-HHHHHHHTHHHHSTT--HHHHHHHHHHTTEEE---SSBTTTTXTTSEEEEESXXXXXXXXXXXXX CS
   HSF_DNA-bind   2 FlkklyeiledeelkeliswsengnsfvvldeeefakkvLpkyFkhsnfaSFvRQLnmYgFkkvkdeekkskskekiweFkhksFkkgkkelleki 97 
                    Fl+k+++++ed+++++++sws+  nsfvv+d+++f++++Lp+yFkh+nf+SFvRQLn+YgF+kv+ ++         weF+++ F +g+++ll++i
  C.cajan_09277  43 FLTKTFDVVEDPSTDDVVSWSRARNSFVVWDSHRFSTTILPRYFKHNNFSSFVRQLNTYGFRKVDPDK---------WEFANEGFLAGQRHLLKTI 129
                    9****************************************************************999.........******************* PP

                    XXXXX CS
   HSF_DNA-bind  98 krkks 102
                    kr+++
  C.cajan_09277 130 KRRRH 134
                    **975 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SMARTSM004152.1E-6039132IPR000232Heat shock factor (HSF)-type, DNA-binding
Gene3DG3DSA:1.10.10.108.8E-3839132IPR011991Winged helix-turn-helix DNA-binding domain
SuperFamilySSF467852.58E-3339132IPR011991Winged helix-turn-helix DNA-binding domain
PRINTSPR000562.0E-194366IPR000232Heat shock factor (HSF)-type, DNA-binding
PfamPF004471.4E-3143132IPR000232Heat shock factor (HSF)-type, DNA-binding
PRINTSPR000562.0E-198193IPR000232Heat shock factor (HSF)-type, DNA-binding
PROSITE patternPS00434082106IPR000232Heat shock factor (HSF)-type, DNA-binding
PRINTSPR000562.0E-1994106IPR000232Heat shock factor (HSF)-type, DNA-binding
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0009644Biological Processresponse to high light intensity
GO:0010200Biological Processresponse to chitin
GO:0010286Biological Processheat acclimation
GO:0034605Biological Processcellular response to heat
GO:0034620Biological Processcellular response to unfolded protein
GO:0042542Biological Processresponse to hydrogen peroxide
GO:0045893Biological Processpositive regulation of transcription, DNA-templated
GO:0071456Biological Processcellular response to hypoxia
GO:0005634Cellular Componentnucleus
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
GO:0043565Molecular Functionsequence-specific DNA binding
GO:0044212Molecular Functiontranscription regulatory region DNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 337 aa     Download sequence    Send to blast
MKGVTVKEEE TMAYAPSASS SSTPSNLSPQ PMEGLHEVGP PPFLTKTFDV VEDPSTDDVV  60
SWSRARNSFV VWDSHRFSTT ILPRYFKHNN FSSFVRQLNT YGFRKVDPDK WEFANEGFLA  120
GQRHLLKTIK RRRHVTQTQS REGGGGACVE LGEFGLEGEI DRLRRDRTVL MAEIVRLRQL  180
QHNSREQLLG METRLQATEK KHQQMMTFLA KALNNQAFIQ QFLHRNAQSI ELQGARRKRR  240
LTNSPSVENL QEDPVIIEEG SATIESQMES FFSAACDDES STEIKDSMLS TVPTAVVMDD  300
FSQIDVPVED LVTKTDDEWN EDLQNLVDHM GYLGSKP
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
5d5u_B4e-261613215129Heat shock factor protein 1
5d5v_B4e-261613215129Heat shock factor protein 1
5d5v_D4e-261613215129Heat shock factor protein 1
Search in ModeBase
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
1125131LKTIKRR
2161166RLRRDR
Functional Description ? help Back to Top
Source Description
UniProtTranscriptional activator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE). Involved in heat stress responses. Seems to be involved in other environmental stress responses. Activates ascorbate peroxidase 2 (APX2) in addition to several heat shock protein (HSPs). {ECO:0000269|PubMed:16649111, ECO:0000269|PubMed:17059409, ECO:0000269|PubMed:17085506}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapC.cajan_09277
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: By heat stress, high light and hydrogen peroxide (H(2)O(2)). {ECO:0000269|PubMed:16649111, ECO:0000269|PubMed:17059409, ECO:0000269|PubMed:17085506}.
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankJN8963060.0JN896306.1 Glycine max heat shock transcription factor HSFA2 mRNA, complete cds.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_020213559.10.0heat shock factor protein HSF30
RefseqXP_020213560.10.0heat shock factor protein HSF30
SwissprotO809821e-123HSFA2_ARATH; Heat stress transcription factor A-2
TrEMBLA0A151TTF00.0A0A151TTF0_CAJCA; Heat stress transcription factor A-2
STRINGGLYMA04G05500.50.0(Glycine max)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
FabidsOGEF82253143
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT2G26150.11e-123heat shock transcription factor A2
Publications ? help Back to Top
  1. Liu HC,Charng YY
    Common and distinct functions of Arabidopsis class A1 and A2 heat shock factors in diverse abiotic stress responses and development.
    Plant Physiol., 2013. 163(1): p. 276-90
    [PMID:23832625]
  2. Jung HS, et al.
    Subset of heat-shock transcription factors required for the early response of Arabidopsis to excess light.
    Proc. Natl. Acad. Sci. U.S.A., 2013. 110(35): p. 14474-9
    [PMID:23918368]
  3. Chauhan H,Khurana N,Agarwal P,Khurana JP,Khurana P
    A seed preferential heat shock transcription factor from wheat provides abiotic stress tolerance and yield enhancement in transgenic Arabidopsis under heat stress environment.
    PLoS ONE, 2013. 8(11): p. e79577
    [PMID:24265778]
  4. Ding Y, et al.
    Four distinct types of dehydration stress memory genes in Arabidopsis thaliana.
    BMC Plant Biol., 2013. 13: p. 229
    [PMID:24377444]
  5. Weng M, et al.
    Histone chaperone ASF1 is involved in gene transcription activation in response to heat stress in Arabidopsis thaliana.
    Plant Cell Environ., 2014. 37(9): p. 2128-38
    [PMID:24548003]
  6. Jang YH, et al.
    A homolog of splicing factor SF1 is essential for development and is involved in the alternative splicing of pre-mRNA in Arabidopsis thaliana.
    Plant J., 2014. 78(4): p. 591-603
    [PMID:24580679]
  7. Stief A, et al.
    Arabidopsis miR156 Regulates Tolerance to Recurring Environmental Stress through SPL Transcription Factors.
    Plant Cell, 2014. 26(4): p. 1792-1807
    [PMID:24769482]
  8. Dobrá J, et al.
    The impact of heat stress targeting on the hormonal and transcriptomic response in Arabidopsis.
    Plant Sci., 2015. 231: p. 52-61
    [PMID:25575991]
  9. Yamauchi Y,Kunishima M,Mizutani M,Sugimoto Y
    Reactive short-chain leaf volatiles act as powerful inducers of abiotic stress-related gene expression.
    Sci Rep, 2015. 5: p. 8030
    [PMID:25619826]
  10. Shi H, et al.
    Melatonin induces class A1 heat-shock factors (HSFA1s) and their possible involvement of thermotolerance in Arabidopsis.
    J. Pineal Res., 2015. 58(3): p. 335-42
    [PMID:25711624]
  11. Mueller SP,Krause DM,Mueller MJ,Fekete A
    Accumulation of extra-chloroplastic triacylglycerols in Arabidopsis seedlings during heat acclimation.
    J. Exp. Bot., 2015. 66(15): p. 4517-26
    [PMID:25977236]
  12. Nie S,Yue H,Xing D
    A Potential Role for Mitochondrial Produced Reactive Oxygen Species in Salicylic Acid-Mediated Plant Acquired Thermotolerance.
    Plant Physiol., 2016.
    [PMID:26099269]
  13. Nguyen AH, et al.
    Loss of Arabidopsis 5'-3' Exoribonuclease AtXRN4 Function Enhances Heat Stress Tolerance of Plants Subjected to Severe Heat Stress.
    Plant Cell Physiol., 2015. 56(9): p. 1762-72
    [PMID:26136597]
  14. Hu Z, et al.
    Histone acetyltransferase GCN5 is essential for heat stress-responsive gene activation and thermotolerance in Arabidopsis.
    Plant J., 2015. 84(6): p. 1178-91
    [PMID:26576681]
  15. Lämke J,Brzezinka K,Bäurle I
    HSFA2 orchestrates transcriptional dynamics after heat stress in Arabidopsis thaliana.
    Transcription, 2016. 7(4): p. 111-4
    [PMID:27383578]
  16. Wang X,Huang W,Liu J,Yang Z,Huang B
    Molecular regulation and physiological functions of a novel FaHsfA2c cloned from tall fescue conferring plant tolerance to heat stress.
    Plant Biotechnol. J., 2017. 15(2): p. 237-248
    [PMID:27500592]
  17. Chen ST,He NY,Chen JH,Guo FQ
    Identification of core subunits of photosystem II as action sites of HSP21, which is activated by the GUN5-mediated retrograde pathway in Arabidopsis.
    Plant J., 2017. 89(6): p. 1106-1118
    [PMID:27943531]
  18. Kataoka R,Takahashi M,Suzuki N
    Coordination between bZIP28 and HSFA2 in the regulation of heat response signals in Arabidopsis.
    Plant Signal Behav, 2017. 12(11): p. e1376159
    [PMID:28873003]
  19. Wang X,Zhuang L,Shi Y,Huang B
    Up-Regulation of HSFA2c and HSPs by ABA Contributing to Improved Heat Tolerance in Tall Fescue and Arabidopsis.
    Int J Mol Sci, 2018.
    [PMID:28914758]
  20. Llamas E,Pulido P,Rodriguez-Concepcion M
    Interference with plastome gene expression and Clp protease activity in Arabidopsis triggers a chloroplast unfolded protein response to restore protein homeostasis.
    PLoS Genet., 2017. 13(9): p. e1007022
    [PMID:28937985]
  21. Li X, et al.
    Plastid Translation Elongation Factor Tu Is Prone to Heat-Induced Aggregation Despite Its Critical Role in Plant Heat Tolerance.
    Plant Physiol., 2018. 176(4): p. 3027-3045
    [PMID:29444814]