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 TRIUR3_18522-P1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; Liliopsida; Petrosaviidae; commelinids; Poales; Poaceae; BOP clade; Pooideae; Triticodae; Triticeae; Triticinae; Triticum
Family ERF
Protein Properties Length: 402aa    MW: 44775 Da    PI: 8.1609
Description ERF family protein
Gene Model
Gene Model ID Type Source Coding Sequence
TRIUR3_18522-P1genomeBGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1AP226.71.3e-08302344250
              AP2   2 gykGVrwdkkrgrWvAeIrdpsengkr.krfslgkfgtaeeAakaaiaar 50 
                      gy+GVr ++ +g + AeIr       +  r slg+f t  eA +a++aa 
  TRIUR3_18522-P1 302 GYRGVRVCP-SGMFYAEIRS------SgVRLSLGTFETVHEADRAYDAAV 344
                      7********.7*********......44********************96 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
Gene3DG3DSA:3.40.30.101.9E-3045135IPR012336Thioredoxin-like fold
PROSITE profilePS5040415.35354133IPR004045Glutathione S-transferase, N-terminal
PfamPF134171.1E-1763132IPR004045Glutathione S-transferase, N-terminal
SuperFamilySSF528332.21E-1863134IPR012336Thioredoxin-like fold
CDDcd005701.54E-1464121No hitNo description
PROSITE profilePS504059.638111257IPR010987Glutathione S-transferase, C-terminal-like
SuperFamilySSF476163.14E-23128255IPR010987Glutathione S-transferase, C-terminal-like
CDDcd032012.13E-78134254No hitNo description
Gene3DG3DSA:1.20.1050.103.4E-34137256IPR010987Glutathione S-transferase, C-terminal-like
PfamPF134101.1E-7162228No hitNo description
SMARTSM003802.0E-7302363IPR001471AP2/ERF domain
SuperFamilySSF541711.05E-12302358IPR016177DNA-binding domain
PROSITE profilePS5103214.394302357IPR001471AP2/ERF domain
CDDcd000181.53E-15303359No hitNo description
Gene3DG3DSA:3.30.730.103.7E-14303358IPR001471AP2/ERF domain
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0010731Biological Processprotein glutathionylation
GO:0005634Cellular Componentnucleus
GO:0005829Cellular Componentcytosol
GO:0005886Cellular Componentplasma membrane
GO:0003677Molecular FunctionDNA binding
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
GO:0005515Molecular Functionprotein binding
GO:0016740Molecular Functiontransferase activity
GO:0043295Molecular Functionglutathione binding
GO:0045174Molecular Functionglutathione dehydrogenase (ascorbate) activity
Sequence ? help Back to Top
Protein Sequence    Length: 402 aa     Download sequence    Send to blast
MGSWPQRELR AVPAATRASR EHASPQIDRA RPLRFPAAGA VNRTPRRRLC VKAAVGHPDT  60
LGDCPFSQRV LLTLEEKKVP YQMKLIDVSN KPDWFLKINP EGKVPVYNGG DGKWIADSDV  120
ITQVIEEKYP TPSLVTPAEY ASVGSKIFST FVTFLKSKDA SDGSEKALVD ELQALEEHLK  180
AHGPYINGAN ISAVDLSLAP KLYHLQVALE HFKGWKVPET LTSVHAYTEA LFSRESFVKT  240
KATKENLIAG WAPKVNPEWR SASEEVRCAP RCRHRALLVD AFSSVADSSA VDMPLRARSS  300
FGYRGVRVCP SGMFYAEIRS SGVRLSLGTF ETVHEADRAY DAAVWRLFRT SLHMNFDDAR  360
TCQQAQDLVP PLRLVTDKDG HEHCRRQCCL LITEADELAM AE
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
5d9t_A1e-1374825621229Dehydroascorbate reductase
5d9v_A1e-1374825621229Dehydroascorbate reductase
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtInvolved in ascorbate homeostasis. Maintains redox pools of ascorbate by recycling dihydroascorbate (DHA) to ascorbate (Probable). Involved in scavenging reactive oxygen species (ROS) under oxidative stresses. Possesses dehydroascorbate reductase (DHAR) activity in vitro (PubMed:19011360). May function via a ping-pong reaction mechanism with an electron transfer at the active site (PubMed:26775680). Possesses chaperone-like activity in vitro (PubMed:26775680). {ECO:0000269|PubMed:19011360, ECO:0000269|PubMed:26775680, ECO:0000305|PubMed:23519921}.
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: Induced by heat shock (PubMed:10648822). Down-regulated during senescence (PubMed:25546583). {ECO:0000269|PubMed:10648822, ECO:0000269|PubMed:25546583}.
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankAY0747840.0AY074784.1 Triticum aestivum dehydroascorbate reductase (DHAR) mRNA, complete cds.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_020196644.11e-150glutathione S-transferase DHAR2-like
SwissprotQ65XA01e-136DHAR1_ORYSJ; Probable glutathione S-transferase DHAR1, cytosolic
TrEMBLM7ZKX90.0M7ZKX9_TRIUA; Glutathione S-transferase DHAR2
STRINGTRIUR3_18522-P10.0(Triticum urartu)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT2G47520.11e-09ERF family protein
Publications ? help Back to Top
  1. Urano J, et al.
    Molecular cloning and characterization of a rice dehydroascorbate reductase.
    FEBS Lett., 2000. 466(1): p. 107-11
    [PMID:10648822]
  2. Chen Z,Young TE,Ling J,Chang SC,Gallie DR
    Increasing vitamin C content of plants through enhanced ascorbate recycling.
    Proc. Natl. Acad. Sci. U.S.A., 2003. 100(6): p. 3525-30
    [PMID:12624189]
  3. Kikuchi S, et al.
    Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice.
    Science, 2003. 301(5631): p. 376-9
    [PMID:12869764]
  4. Cheng CH, et al.
    A fine physical map of the rice chromosome 5.
    Mol. Genet. Genomics, 2005. 274(4): p. 337-45
    [PMID:16261349]
  5. Shin SY, et al.
    Scavenging reactive oxygen species by rice dehydroascorbate reductase alleviates oxidative stresses in Escherichia coli.
    Mol. Cells, 2008. 26(6): p. 616-20
    [PMID:19011360]
  6. Jain M,Ghanashyam C,Bhattacharjee A
    Comprehensive expression analysis suggests overlapping and specific roles of rice glutathione S-transferase genes during development and stress responses.
    BMC Genomics, 2010. 11: p. 73
    [PMID:20109239]
  7. Kim YS, et al.
    Homologous expression of cytosolic dehydroascorbate reductase increases grain yield and biomass under paddy field conditions in transgenic rice (Oryza sativa L. japonica).
    Planta, 2013. 237(6): p. 1613-25
    [PMID:23519921]
  8. Li J, et al.
    Isolation and functional characterization of a novel rice constitutive promoter.
    Plant Cell Rep., 2014. 33(10): p. 1651-60
    [PMID:24980160]
  9. Li Z, et al.
    Transcriptional profile of genes involved in ascorbate glutathione cycle in senescing leaves for an early senescence leaf (esl) rice mutant.
    J. Plant Physiol., 2015. 176: p. 1-15
    [PMID:25546583]
  10. Kumar A, et al.
    Comparative proteomics reveals differential induction of both biotic and abiotic stress response associated proteins in rice during Xanthomonas oryzae pv. oryzae infection.
    Funct. Integr. Genomics, 2015. 15(4): p. 425-37
    [PMID:25648443]
  11. Do H, et al.
    Structural understanding of the recycling of oxidized ascorbate by dehydroascorbate reductase (OsDHAR) from Oryza sativa L. japonica.
    Sci Rep, 2016. 6: p. 19498
    [PMID:26775680]