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 GSBRNA2T00109513001
Common NameGSBRNA2T00109513001
Organism
Brassica napus
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica
Family bZIP
Protein Properties Length: 730aa    MW: 79699.3 Da    PI: 8.4341
Description bZIP family protein
Gene Model
Gene Model ID Type Source Coding Sequence
GSBRNA2T00109513001genomeGenoscopeView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1bZIP_121.64.8e-071581463
                         XCHHHCHHHHHHHHHHHHHHHHH.......HHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH CS
               bZIP_1  4 lkrerrkqkNReAArrsRqRKka.......eieeLeekvkeLeaeNkaLkkeleelkkevaklksev 63
                          k+ +rk +NRe+ArrsR++K++       ei  Le+++ke ++  k  + +l++l+ e a l+se+
  GSBRNA2T00109513001 15 EKKRKRKLSNRESARRSRLKKQKmmedtihEISTLERRIKEYSERCKVARRRLDSLESENAGLRSEK 81
                         5899******************933333334557999999999999989999999999988888875 PP
Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
Gene3DG3DSA:1.20.5.1705.3E-8879No hitNo description
SMARTSM003389.7E-101276IPR004827Basic-leucine zipper domain
PfamPF077162.1E-51455IPR004827Basic-leucine zipper domain
PROSITE profilePS502179.531477IPR004827Basic-leucine zipper domain
SuperFamilySSF579591.97E-61670No hitNo description
CDDcd147022.90E-151768No hitNo description
PROSITE patternPS0003601934IPR004827Basic-leucine zipper domain
SuperFamilySSF517352.21E-13129257IPR016040NAD(P)-binding domain
Gene3DG3DSA:3.40.50.7203.1E-17130254IPR016040NAD(P)-binding domain
PRINTSPR017989.7E-5217234IPR005810Succinyl-CoA ligase, alpha subunit
SuperFamilySSF482563.14E-70251725IPR002020Citrate synthase
Gene3DG3DSA:3.40.50.2614.6E-52255434IPR016102Succinyl-CoA synthetase-like
PROSITE patternPS012170289314IPR017866Succinyl-CoA synthetase, beta subunit, conserved site
PROSITE patternPS012160295324IPR005810Succinyl-CoA ligase, alpha subunit
PfamPF005497.2E-11295418IPR005811ATP-citrate lyase/succinyl-CoA ligase
PRINTSPR017989.7E-5320338IPR005810Succinyl-CoA ligase, alpha subunit
PRINTSPR017989.7E-5351364IPR005810Succinyl-CoA ligase, alpha subunit
PROSITE patternPS003990380396IPR017440ATP-citrate lyase/succinyl-CoA ligase, active site
PRINTSPR017989.7E-5387404IPR005810Succinyl-CoA ligase, alpha subunit
CDDcd061002.60E-89490727No hitNo description
PfamPF002852.6E-17519717IPR002020Citrate synthase
Gene3DG3DSA:1.10.580.107.4E-6520579IPR016142Citrate synthase-like, large alpha subdomain
Gene3DG3DSA:1.10.230.108.8E-13580667IPR016143Citrate synthase-like, small alpha subdomain
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0005829Cellular Componentcytosol
GO:0005886Cellular Componentplasma membrane
GO:0009346Cellular Componentcitrate lyase complex
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
GO:0003878Molecular FunctionATP citrate synthase activity
GO:0043565Molecular Functionsequence-specific DNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 730 aa     Download sequence    Send to blast
MANAEKTSSG SDIDEKKRKR KLSNRESARR SRLKKQKMME DTIHEISTLE RRIKEYSERC  60
KVARRRLDSL ESENAGLRSE KTWLLSYVRD LENMMATTSL TLTQSGGDEQ EANADGDYLS  120
KMATGQLFSR TTQALFYNYK QLPVQRMLDF DFLCGRETPS VAGIINPGSE GFQKLFFGQE  180
EIAIPVHAAI EAACAAHPTA DVFINFASFR SAAASSMAAL KQPTIKVVAI IAEGVPESDT  240
KQLIAYARAN NKVVIGPATV GGIQAGAFKI GDTAGTIDNI IQCKLYRPGS VGFVSKSGGM  300
SNEMYNTVAR VTDGIYEGIA IGGDVFPGST LSDHILRFNN IPQIKMMVVL GELGGRDEYS  360
LVEALKQGKV NKPVVAWVSG TCARLFKSEV QFGHAGAKSG GEMESAQAKN QALMDAGAIV  420
PTSFEALESA IKETFEKLVE EGKVSPIKEV TPPQIPEDLS SAIKSGKVRA PTHIISTISD  480
DRGEEPCYAG VPMSSIIEQG LGVGDVISLL WFKRSLPRYC TKFIEICIML CADHGPCVSG  540
AHNTIVTARA GKDLVSSLVS GLLTIGPRFG GAIDDAARYF KDACDRNLTP YEFVEGMKKK  600
GIRVPGIGHR IKSRDNRDKR VELLQKFARS NFPSVKYMEY AVTVESYTLS KANNLVLNVD  660
GAIGSLFLDL LAGSGMFTKQ EIDEIVQIGY LNGLFVLARS IGLIGHTFDQ KRLKQPLYRH  720
PWEDVLYTK*
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
6hxi_B0.01277278608Succinyl-CoA ligase (ADP-forming) subunit alpha
6hxi_D0.01277278608Succinyl-CoA ligase (ADP-forming) subunit alpha
Search in ModeBase
Nucleic Localization Signal ? help Back to Top
NLS
No. Start End Sequence
11421EKKRKRKL
21520KKRKRK
Expression -- UniGene ? help Back to Top
UniGene ID E-value Expressed in
Bna.8090.0flower| leaf| microspore| root| seed| stem
Expression -- Description ? help Back to Top
Source Description
UniprotDEVELOPMENTAL STAGE: Expressed in flower buds at stage 6 of development in tapetal cells and at stage 10 in the epidermal cells of growing petals and ovaries. In young siliques, expressed transiently in the inner integument of the ovules just prior to testal deposition. Expressed in the developing embryo with a maximal level at the heart and torpedo stages. The expression then disappears in the mature embryo. During seed germination, expressed in the vascular bundles, apical meristem, epidermis of the seedling cotyledon, stem, and root. Highly expressed in the root tip of seedlings 4 days after imbibition. {ECO:0000269|PubMed:12376641}.
UniprotTISSUE SPECIFICITY: Expressed in trichomes, epidermal leaf cells, anther tapetal cells, stigma and in young vascular bundles of expanding leaves, cotyledons, roots, pedicel of flowers and siliques. {ECO:0000269|PubMed:12376641}.
Functional Description ? help Back to Top
Source Description
UniProtATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA, used for the elongation of fatty acids and biosynthesis of isoprenoids, flavonoids and malonated derivatives. May supply substrate to the cytosolic acetyl-CoA carboxylase, which generates the malonyl-CoA used for the synthesis of a multitude of compounds, including very long chain fatty acids and flavonoids. Required for normal growth and development and elongation of C18 fatty acids to C20 to C24 fatty acids in seeds. n contrast to all known animal ACL enzymes having a homomeric structure, plant ACLs are composed of alpha and beta chains. {ECO:0000269|PubMed:12376641}.
Cis-element ? help Back to Top
SourceLink
PlantRegMapGSBRNA2T00109513001
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankAY0350670.0AY035067.1 Arabidopsis thaliana putative ATP citrate lyase (At5g49460) mRNA, complete cds.
GenBankAY0565940.0AY056594.1 Arabidopsis thaliana ATP-citrate lyase subunit B mRNA, complete cds.
GenBankAY0629560.0AY062956.1 Arabidopsis thaliana putative ATP citrate lyase (At5g49460) mRNA, complete cds.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_022558915.10.0ATP-citrate synthase beta chain protein 2
RefseqXP_022558916.10.0ATP-citrate synthase beta chain protein 2
SwissprotQ9FGX10.0ACLB2_ARATH; ATP-citrate synthase beta chain protein 2
TrEMBLA0A3P5YF440.0A0A3P5YF44_BRACM; Uncharacterized protein
STRINGBra036142.1-P0.0(Brassica rapa)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT5G49450.13e-59basic leucine-zipper 1
Publications ? help Back to Top
  1. Fatland BL, et al.
    Molecular characterization of a heteromeric ATP-citrate lyase that generates cytosolic acetyl-coenzyme A in Arabidopsis.
    Plant Physiol., 2002. 130(2): p. 740-56
    [PMID:12376641]
  2. Fatland BL,Nikolau BJ,Wurtele ES
    Reverse genetic characterization of cytosolic acetyl-CoA generation by ATP-citrate lyase in Arabidopsis.
    Plant Cell, 2005. 17(1): p. 182-203
    [PMID:15608338]
  3. Chalhoub B, et al.
    Plant genetics. Early allopolyploid evolution in the post-Neolithic Brassica napus oilseed genome.
    Science, 2014. 345(6199): p. 950-3
    [PMID:25146293]