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 RrC2946_p1
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Raphanus
Family C3H
Protein Properties Length: 845aa    MW: 96003 Da    PI: 6.702
Description C3H family protein
Gene Model
Gene Model ID Type Source Coding Sequence
RrC2946_p1genomeMSUView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1zf-CCCH19.61.6e-06627649326
                 S---SGGGGTS--TTTTT-SS-SS CS
     zf-CCCH   3 telCrffartGtCkyGdrCkFaHg 26 
                 +++C+ fa+ G C++G++C+ +Hg
  RrC2946_p1 627 YPICS-FAAAGDCPRGSQCPHMHG 649
                 78999.**************9998 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
SuperFamilySSF474731.5E-816105IPR011992EF-hand domain pair
Gene3DG3DSA:1.10.238.101.2E-92598IPR011992EF-hand domain pair
Gene3DG3DSA:3.20.20.1902.4E-92100250IPR017946PLC-like phosphodiesterase, TIM beta/alpha-barrel domain
CDDcd085991.35E-114102421No hitNo description
PROSITE profilePS5000743.047103248IPR000909Phosphatidylinositol-specific phospholipase C, X domain
SMARTSM001481.9E-71103248IPR000909Phosphatidylinositol-specific phospholipase C, X domain
SuperFamilySSF516951.2E-112103435IPR017946PLC-like phosphodiesterase, TIM beta/alpha-barrel domain
PfamPF003886.0E-51105248IPR000909Phosphatidylinositol-specific phospholipase C, X domain
PRINTSPR003902.3E-42108126IPR001192Phosphoinositide phospholipase C family
PRINTSPR003902.3E-42134154IPR001192Phosphoinositide phospholipase C family
PRINTSPR003902.3E-42232249IPR001192Phosphoinositide phospholipase C family
Gene3DG3DSA:3.20.20.1902.4E-92312442IPR017946PLC-like phosphodiesterase, TIM beta/alpha-barrel domain
SMARTSM001491.4E-66317434IPR001711Phospholipase C, phosphatidylinositol-specific, Y domain
PfamPF003871.1E-28345433IPR001711Phospholipase C, phosphatidylinositol-specific, Y domain
PROSITE profilePS5000837.118347433IPR001711Phospholipase C, phosphatidylinositol-specific, Y domain
PRINTSPR003902.3E-42372393IPR001192Phosphoinositide phospholipase C family
PRINTSPR003902.3E-42393411IPR001192Phosphoinositide phospholipase C family
PROSITE profilePS5000412.676451547IPR000008C2 domain
CDDcd002752.18E-35452582No hitNo description
SuperFamilySSF495625.95E-26454581IPR000008C2 domain
SMARTSM002391.5E-12454562IPR000008C2 domain
Gene3DG3DSA:2.60.40.1502.2E-20454581IPR000008C2 domain
PfamPF001686.9E-9475555IPR000008C2 domain
PRINTSPR003902.3E-42548558IPR001192Phosphoinositide phospholipase C family
SMARTSM003560.024624650IPR000571Zinc finger, CCCH-type
PROSITE profilePS5010312.399624651IPR000571Zinc finger, CCCH-type
Gene3DG3DSA:3.30.40.106.0E-10674752IPR013083Zinc finger, RING/FYVE/PHD-type
SuperFamilySSF578502.09E-12682757No hitNo description
CDDcd001622.08E-6692752No hitNo description
PfamPF000972.8E-7693750IPR018957Zinc finger, C3HC4 RING-type
SMARTSM001848.7E-8693750IPR001841Zinc finger, RING-type
PROSITE profilePS5008912.386693751IPR001841Zinc finger, RING-type
PROSITE patternPS005180717726IPR017907Zinc finger, RING-type, conserved site
PROSITE profilePS5010313.253780809IPR000571Zinc finger, CCCH-type
SMARTSM003560.75780808IPR000571Zinc finger, CCCH-type
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006629Biological Processlipid metabolic process
GO:0035556Biological Processintracellular signal transduction
GO:0004435Molecular Functionphosphatidylinositol phospholipase C activity
GO:0005515Molecular Functionprotein binding
GO:0008270Molecular Functionzinc ion binding
Sequence ? help Back to Top
Protein Sequence    Length: 845 aa     Download sequence    Send to blast
MSKQTYRVCF CFNRRFRYTA SEAPRDVKTL FEKYSENGVM TVDHLHRFLI DIQKQDKATK  60
EDTQSIINSA SSLLHRNGLQ LDAFFKYLFG DTNPPLALHE VHQDMDAPIS HYFIFTGHNS  120
YLTGNQLSSD CSEVPIIDAL KKGVRVIELD IWPNSNKNDI DVLHGRTLTS PVELIKCLRA  180
IKEHAFDVSD YPVVVTLEDH LTPELQSKVA EMVTEIFGEI LFTPPVGESL KEFPSPNSLK  240
KRIIISTKPP KEYKEGKDEE VVPKGKALGD EEVWGREVPS FIERNKSGDK DELDDDEEDD  300
EDDDDVEKSK KNAPPQYKHL IAIHAGKPKG GITACLKVDP DKVRRLSLSE EQLEKAAEKY  360
ATQIVRFTQQ NLLRIYPKGT RVTSSNYNPL VGWSYGAQMV AFNMQGYGRS LWLMQGMFRA  420
NGGCGYIKKP DILLKGGSDS DIFDPKATLP VKTTLRVTIY MGEGWYFDFR HTHFDQYSPP  480
DFYTRVGIAG VPADTVMKKT KTLEDNWVPS WDEVFEFPLT VPELALLRLE VHEYDMSEKD  540
DFGGQTCLPV WELQEGIRSF PLHSRKGEKY KSVKLLVRCR YEHVRSTSQP HVPPPPPPPL  600
PSDSHPQQKG DNNNNDNDVC YIHPREYPIC SFAAAGDCPR GSQCPHMHGD VCSTCGKKCL  660
HPFRPEEREE HTKECEKKQK RIEALKKSQE IECSVCLDRV LSKATPGERK FGLLTECHHP  720
FCIQCIRNWR SSAPVSGMDV NSTLRACPIC RKLSYFVVPS VVWYSTPDEK KEIIDIYKAK  780
LRSINCKHFN FGNGNCPFGG SCFYKHAYSD GQLDEVVVRN LGSQEGETVI ADSIRLSEFL  840
GRVHI
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
1djg_A6e-643957895619PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
1djg_B6e-643957895619PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
1djh_A6e-643957895619PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
1djh_B6e-643957895619PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
1dji_A6e-643957895619PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
1dji_B6e-643957895619PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
1djw_A6e-643957895619PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
1djw_B6e-643957895619PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
1djx_A6e-643957895619PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
1djx_B6e-643957895619PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
1djy_A6e-643957895619PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
1djy_B6e-643957895619PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
1djz_A6e-643957895619PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
1djz_B6e-643957895619PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
1qas_A5e-643957893617PHOSPHOLIPASE C DELTA-1
1qas_B5e-643957893617PHOSPHOLIPASE C DELTA-1
1qat_A5e-643957893617PHOSPHOLIPASE C DELTA-1
1qat_B5e-643957893617PHOSPHOLIPASE C DELTA-1
2isd_A6e-643957895619PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
2isd_B6e-643957895619PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtThe production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. At physiological calcium concentration, the preferred substrate is phosphatidylinositol 4,5-bisphosphate versus phosphatidylinositol. {ECO:0000269|PubMed:11377433, ECO:0000269|Ref.10}.
Regulation -- Description ? help Back to Top
Source Description
UniProtINDUCTION: Not induced by environmental stresses such as dehydration, salinity and low temperature.
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Nucleotide ? help Back to Top
Source Hit ID E-value Description
GenBankAF1081230.0AF108123.1 Brassica napus phosphoinositide-specific phospholipase C (PLC) mRNA, complete cds.
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_018440503.10.0PREDICTED: phosphoinositide phospholipase C 2-like
SwissprotQ390330.0PLCD2_ARATH; Phosphoinositide phospholipase C 2
TrEMBLA0A0D3AF200.0A0A0D3AF20_BRAOL; Phosphoinositide phospholipase C
STRINGBo1g145030.10.0(Brassica oleracea)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT3G08505.21e-123C3H family protein
Publications ? help Back to Top
  1. Otterhag L,Sommarin M,Pical C
    N-terminal EF-hand-like domain is required for phosphoinositide-specific phospholipase C activity in Arabidopsis thaliana.
    FEBS Lett., 2001. 497(2-3): p. 165-70
    [PMID:11377433]
  2. Mueller-Roeber B,Pical C
    Inositol phospholipid metabolism in Arabidopsis. Characterized and putative isoforms of inositol phospholipid kinase and phosphoinositide-specific phospholipase C.
    Plant Physiol., 2002. 130(1): p. 22-46
    [PMID:12226484]
  3. Nühse TS,Boller T,Peck SC
    A plasma membrane syntaxin is phosphorylated in response to the bacterial elicitor flagellin.
    J. Biol. Chem., 2003. 278(46): p. 45248-54
    [PMID:12949074]
  4. Lin WH,Ye R,Ma H,Xu ZH,Xue HW
    DNA chip-based expression profile analysis indicates involvement of the phosphatidylinositol signaling pathway in multiple plant responses to hormone and abiotic treatments.
    Cell Res., 2004. 14(1): p. 34-45
    [PMID:15040888]
  5. Nelson CJ,Hegeman AD,Harms AC,Sussman MR
    A quantitative analysis of Arabidopsis plasma membrane using trypsin-catalyzed (18)O labeling.
    Mol. Cell Proteomics, 2006. 5(8): p. 1382-95
    [PMID:16635983]
  6. Cao Z, et al.
    Preparation of polyclonal antibody specific for AtPLC4, an Arabidopsis phosphatidylinositol-specific phospholipase C in rabbits.
    Protein Expr. Purif., 2007. 52(2): p. 306-12
    [PMID:17142056]
  7. Niittylä T,Fuglsang AT,Palmgren MG,Frommer WB,Schulze WX
    Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis.
    Mol. Cell Proteomics, 2007. 6(10): p. 1711-26
    [PMID:17586839]
  8. Marmagne A, et al.
    A high content in lipid-modified peripheral proteins and integral receptor kinases features in the arabidopsis plasma membrane proteome.
    Mol. Cell Proteomics, 2007. 6(11): p. 1980-96
    [PMID:17644812]
  9. Nühse TS,Bottrill AR,Jones AM,Peck SC
    Quantitative phosphoproteomic analysis of plasma membrane proteins reveals regulatory mechanisms of plant innate immune responses.
    Plant J., 2007. 51(5): p. 931-40
    [PMID:17651370]
  10. Ueoka-Nakanishi H, et al.
    Thioredoxin h regulates calcium dependent protein kinases in plasma membranes.
    FEBS J., 2013. 280(14): p. 3220-31
    [PMID:23615222]
  11. Li L, et al.
    Arabidopsis PLC2 is involved in auxin-modulated reproductive development.
    Plant J., 2015. 84(3): p. 504-15
    [PMID:26340337]
  12. Kanehara K, et al.
    Arabidopsis AtPLC2 Is a Primary Phosphoinositide-Specific Phospholipase C in Phosphoinositide Metabolism and the Endoplasmic Reticulum Stress Response.
    PLoS Genet., 2015. 11(9): p. e1005511
    [PMID:26401841]
  13. Di Fino LM, et al.
    Arabidopsis phosphatidylinositol-phospholipase C2 (PLC2) is required for female gametogenesis and embryo development.
    Planta, 2017. 245(4): p. 717-728
    [PMID:27999988]
  14. D'Ambrosio JM, et al.
    Phospholipase C2 Affects MAMP-Triggered Immunity by Modulating ROS Production.
    Plant Physiol., 2017. 175(2): p. 970-981
    [PMID:28827453]
  15. Hirayama T,Mitsukawa N,Shibata D,Shinozaki K
    AtPLC2, a gene encoding phosphoinositide-specific phospholipase C, is constitutively expressed in vegetative and floral tissues in Arabidopsis thaliana.
    Plant Mol. Biol., 1997. 34(1): p. 175-80
    [PMID:9177324]