PlantTFDB - Plant Transcription Factor Database @ CBI, PKU

PlantRegMap/PlantTFDB v5.0

Plant Transcription Factor Database

Transcription Factor Information

Basic Information | Signature Domain | Sequence |

Basic Information? help Back to Top

TF ID

Rsa1.0_10066.1_g00002.1

Organism

Raphanus sativus

Taxonomic ID

3726

Taxonomic Lineage

cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Raphanus

Family

HSF

Protein Properties

Length: 347aa MW: 39144.9 Da PI: 4.9893

Description

HSF family protein

Gene Model

Gene Model ID	Type	Source	Coding Sequence
Rsa1.0_10066.1_g00002.1	genome	RGD	View CDS

Signature Domain? help Back to Top

No.	Domain	Score	E-value	Start	End	HMM Start	HMM End
1	HSF_DNA-bind	115.3	3.9e-36	45	136	2	102
HHHHHHHHHCTGGGTTTSEESSSSSEEEES-HHHHHHHTHHHHSTT--HHHHHHHHHHTTEEE---SSBTTTTXTTSEEEEESXXX CS HSF_DNA-bind 2 FlkklyeiledeelkeliswsengnsfvvldeeefakkvLpkyFkhsnfaSFvRQLnmYgFkkvkdeekkskskekiweFkhksFk 87 Fl+k+ye++ed+++++++sws+ nsf+v+d+++f++++Lp+yFkhsnf+SF+RQLn+YgF+k++ ++ weF+++ F Rsa1.0_10066.1_g00002.1 45 FLTKTYEMVEDPATDTVVSWSNGRNSFIVWDSHKFSTTLLPRYFKHSNFSSFIRQLNTYGFRKIDPDR---------WEFANEGFL 121 9**************************************************************999.........***** PP XXXXXXXXXXXXXXX CS HSF_DNA-bind 88 kgkkellekikrkks 102 +g+k+ll++ikr+++ Rsa1.0_10066.1_g00002.1 122 AGQKHLLKSIKRRRN 136 **********986 PP

Protein Features ? help Back to Top

Database	Entry ID	E-value	Start	End	InterPro ID	Description
Gene3D	G3DSA:1.10.10.10	1.9E-38	41	134	IPR011991	Winged helix-turn-helix DNA-binding domain
SMART	SM00415	2.3E-59	41	134	IPR000232	Heat shock factor (HSF)-type, DNA-binding
SuperFamily	SSF46785	2.99E-35	41	134	IPR011991	Winged helix-turn-helix DNA-binding domain
Pfam	PF00447	1.0E-31	45	134	IPR000232	Heat shock factor (HSF)-type, DNA-binding
PRINTS	PR00056	2.9E-19	45	68	IPR000232	Heat shock factor (HSF)-type, DNA-binding
PRINTS	PR00056	2.9E-19	83	95	IPR000232	Heat shock factor (HSF)-type, DNA-binding
PROSITE pattern	PS00434	0	84	108	IPR000232	Heat shock factor (HSF)-type, DNA-binding
PRINTS	PR00056	2.9E-19	96	108	IPR000232	Heat shock factor (HSF)-type, DNA-binding

Gene Ontology ? help Back to Top
GO Term	GO Category	GO Description
GO:0009644	Biological Process	response to high light intensity
GO:0010200	Biological Process	response to chitin
GO:0010286	Biological Process	heat acclimation
GO:0034605	Biological Process	cellular response to heat
GO:0034620	Biological Process	cellular response to unfolded protein
GO:0042542	Biological Process	response to hydrogen peroxide
GO:0045893	Biological Process	positive regulation of transcription, DNA-templated
GO:0071456	Biological Process	cellular response to hypoxia
GO:0005634	Cellular Component	nucleus
GO:0003700	Molecular Function	transcription factor activity, sequence-specific DNA binding
GO:0043565	Molecular Function	sequence-specific DNA binding
GO:0044212	Molecular Function	transcription regulatory region DNA binding

Sequence ? help Back to Top
Protein Sequence Length: 347 aa Download sequence Send to blast
MEQLKVEFEE ETVTYGGSGA ASSSVGSSSS PRPMEGLNET GPPPFLTKTY EMVEDPATDT 60 VVSWSNGRNS FIVWDSHKFS TTLLPRYFKH SNFSSFIRQL NTYGFRKIDP DRWEFANEGF 120 LAGQKHLLKS IKRRRNMGLQ TVNQQGSGSG MSCVEVGQYG FEGEVERLKR DHSVLVAEVV 180 RLRQQQHNSK SQVAEMEQRL LVTEKRQQQM MTFLAKALNN PNFVQQFALM SKEKRGLLGS 240 DVGRKRRLTS SPSLGTTEER VLHDQEFDRM KDDMETLLAA AIDNESSNLA ASKDEQCLEA 300 MNVMMEDGHL EPEIYVKVED LVASPLDWGS EDLHDIVDQM GFLGSEP

Sequence ? help Back to Top

Protein Sequence Length: 347 aa Download sequence Send to blast

MEQLKVEFEE ETVTYGGSGA ASSSVGSSSS PRPMEGLNET GPPPFLTKTY EMVEDPATDT  60
VVSWSNGRNS FIVWDSHKFS TTLLPRYFKH SNFSSFIRQL NTYGFRKIDP DRWEFANEGF  120
LAGQKHLLKS IKRRRNMGLQ TVNQQGSGSG MSCVEVGQYG FEGEVERLKR DHSVLVAEVV  180
RLRQQQHNSK SQVAEMEQRL LVTEKRQQQM MTFLAKALNN PNFVQQFALM SKEKRGLLGS  240
DVGRKRRLTS SPSLGTTEER VLHDQEFDRM KDDMETLLAA AIDNESSNLA ASKDEQCLEA  300
MNVMMEDGHL EPEIYVKVED LVASPLDWGS EDLHDIVDQM GFLGSEP

3D Structure ? help Back to Top

PDB ID	Evalue	Query Start	Query End	Hit Start	Hit End	Description
5d5u_B	3e-25	19	134	1	129	Heat shock factor protein 1
5d5v_B	3e-25	19	134	1	129	Heat shock factor protein 1
5d5v_D	3e-25	19	134	1	129	Heat shock factor protein 1
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Nucleic Localization Signal ? help Back to Top

No.	Start	End	Sequence
1	127	133	LKSIKRR

Functional Description ? help Back to Top
Source	Description
UniProt	Transcriptional 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
Source	Link
PlantRegMap	Rsa1.0_10066.1_g00002.1

Regulation -- Description ? help Back to Top
Source	Description
UniProt	INDUCTION: 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
PlantRegMap	Retrieve	-

Annotation -- Nucleotide ? help Back to Top
Source	Hit ID	E-value	Description
GenBank	HQ435240	0.0	HQ435240.1 Brassica napus cultivar Deyou No.5 heat shock transcription factor A2 (HsfA2) mRNA, complete cds.

Annotation -- Protein ? help Back to Top
Source	Hit ID	E-value	Description
Refseq	XP_018463277.1	0.0	PREDICTED: heat stress transcription factor A-2
Swissprot	O80982	0.0	HSFA2_ARATH; Heat stress transcription factor A-2
TrEMBL	A0A3P6AYX6	0.0	A0A3P6AYX6_BRAOL; Uncharacterized protein (Fragment)
STRING	Bo3g042080.1	0.0	(Brassica oleracea)

Orthologous Group ? help Back to Top
Lineage	Orthologous Group ID	Taxa Number	Gene Number
Malvids	OGEM11672	27	32

Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID	E-value	Description
AT2G26150.1	0.0	heat shock transcription factor A2

Publications ? help Back to Top
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] 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] 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] Ding Y, et al. Four distinct types of dehydration stress memory genes in Arabidopsis thaliana. BMC Plant Biol., 2013. 13: p. 229 [PMID:24377444] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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] 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]