PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID SapurV1A.1072s0100.1.p
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Malpighiales; Salicaceae; Saliceae; Salix
Family bZIP
Protein Properties Length: 736aa    MW: 79178.4 Da    PI: 6.1878
Description bZIP family protein
Gene Model
Gene Model ID Type Source Coding Sequence
SapurV1A.1072s0100.1.pgenomeJGIView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1bZIP_134.54.4e-11244305162
                             XXXXCHHHCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH CS
                  bZIP_1   1 ekelkrerrkqkNReAArrsRqRKkaeieeLeekvkeLeaeNkaLkkeleelkkevaklkse 62 
                             e+e k+  r+ +NRe+A  sRqRKk ++eeLe+kv ++ +   +L  +++    e a+l+++
  SapurV1A.1072s0100.1.p 244 EEEEKKRARLVRNRESAHLSRQRKKHYVEELEDKVRAMHSTIADLNGRVSYFMAENATLRQQ 305
                             67889999********************************9999999999999999988887 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SMARTSM003383.3E-14244308IPR004827Basic-leucine zipper domain
PfamPF001701.3E-10244306IPR004827Basic-leucine zipper domain
PROSITE profilePS502179.921246306IPR004827Basic-leucine zipper domain
Gene3DG3DSA:1.20.5.1703.8E-15248307No hitNo description
SuperFamilySSF579591.9E-11248306No hitNo description
CDDcd147043.22E-21249300No hitNo description
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0042538Biological Processhyperosmotic salinity response
GO:0045893Biological Processpositive regulation of transcription, DNA-templated
GO:0005634Cellular Componentnucleus
GO:0005783Cellular Componentendoplasmic reticulum
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
GO:0043565Molecular Functionsequence-specific DNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 736 aa     Download sequence    Send to blast
MEEELNSQLP IPPLDHLFFN QNSDQNDNFD VPDLSSDFED MSDFDITFDD LTNLYFPSEN  60
EQFLIPDNNA VNPDQGRSDN PGFETGSLEG CLGGLGSNPV NLESPESGGS GICGDQGGLE  120
VDTYLNPSPS EAGSCDSGGS DSRSSDLGPA SSHGSGNSGS GVLNAGSPES GTNDNPCTHV  180
VDQKVVKNET ESAKNVKNDK IAFTKRKKEM GDGENGDVMR NFKYRKAEGE DVSVNVSGSV  240
ISGEEEEKKR ARLVRNRESA HLSRQRKKHY VEELEDKVRA MHSTIADLNG RVSYFMAENA  300
TLRQQLNGNS ACPPPMYAPM APYPWMSCAP YVVKPQGSQV PLVPIPRLKP QQAVPVAKTK  360
KVESKKGEGK TKKVASVSLF GLVFFILLFG GLVPMVDVKF GGIRESGFGF GSDRFLDQHK  420
GRILIVDGHS NGSHENVSVG FSDDKILCVR GRKGCPEHDS ANKRAGEHLP GSDEFGQFGN  480
ASEQLVASLY VPRNDKLVKI DGNLIIHSIL ASERAMASHE SPEVNITKQT ALAIPDVGNN  540
IGRHSHVYRT HAERQKALSS GSDDTSKDNL KSSAAKGKLQ QWFREGLAGP MLSSGMCTEV  600
FQFDVSPTPG AIVPASSVAN VTAEHRKNNS TCLKKGGRNR RILRGLPIPL SGSDLNITGE  660
HGGNNTHKSF QGNKSVSPMV VSVLVDPREA GDSDVDGVIT PKSLSRIFVV VLVDSIKYVT  720
YSCVLPTIGP HLVTT*
Functional Description ? help Back to Top
Source Description
UniProtTranscriptional activator involved in salt and osmotic stress responses. Functions as a stress sensor and transducer in a signaling pathway that resembles an ER stress response. Following salt stress, BZIP17 is cleaved by SBT6.1 (S1P) and S2P at the C-terminus and the N-terminal bZIP component is translocated to the nucleus, where it activates the expression of salt stress response genes (PubMed:17662035). Functions as a stress sensor and transducer in ER stress signaling pathway. ER stress induces proteolysis of BZIP17 by SBT6.1 (S1P) and S2P, and the N-terminal bZIP component is translocated to the nucleus, where it activates the expression and production of ER chaperones, as well as protein involved in brassinosteroid (BR) signaling, which is required for stress acclimation and growth (PubMed:20876872). {ECO:0000269|PubMed:17662035, ECO:0000269|PubMed:20876872}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapSapurV1A.1072s0100.1.p
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankAC2134140.0AC213414.1 Populus trichocarpa clone POP015-I11, complete sequence.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_024443297.10.0bZIP transcription factor 17
SwissprotO222080.0BZP17_ARATH; bZIP transcription factor 17
TrEMBLA0A2K1X9Z90.0A0A2K1X9Z9_POPTR; Uncharacterized protein
STRINGPOPTR_0016s03220.10.0(Populus trichocarpa)
Orthologous Group ? help Back to Top
LineageOrthologous Group IDTaxa NumberGene Number
FabidsOGEF74873448
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT2G40950.11e-166bZIP family protein
Publications ? help Back to Top
  1. Zhou SF, et al.
    Membrane-associated transcription factor peptidase, site-2 protease, antagonizes ABA signaling in Arabidopsis.
    New Phytol., 2015. 208(1): p. 188-97
    [PMID:25919792]
  2. Sagor GH, et al.
    The polyamine spermine induces the unfolded protein response via the MAPK cascade in Arabidopsis.
    Front Plant Sci, 2015. 6: p. 687
    [PMID:26442007]
  3. Ezer D, et al.
    The G-Box Transcriptional Regulatory Code in Arabidopsis.
    Plant Physiol., 2017. 175(2): p. 628-640
    [PMID:28864470]
  4. Kim JS,Yamaguchi-Shinozaki K,Shinozaki K
    ER-Anchored Transcription Factors bZIP17 and bZIP28 Regulate Root Elongation.
    Plant Physiol., 2018. 176(3): p. 2221-2230
    [PMID:29367234]
  5. Cifuentes-Esquivel N, et al.
    bZIP17 regulates the expression of genes related to seed storage and germination, reducing seed susceptibility to osmotic stress.
    J. Cell. Biochem., 2018. 119(8): p. 6857-6868
    [PMID:29693271]
  6. Guan P, et al.
    SENSITIVE TO SALT1, An Endoplasmic Reticulum-Localized Chaperone, Positively Regulates Salt Resistance.
    Plant Physiol., 2018. 178(3): p. 1390-1405
    [PMID:30287478]