2FJU


Conserved Protein Domain Family
EFh_PI-PLCbeta2

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cd16209: EFh_PI-PLCbeta2 
Click on image for an interactive view with Cn3D
EF-hand motif found in phosphoinositide phospholipase C beta 2 (PI-PLC-beta2)
PI-PLC-beta2, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2, or phospholipase C-beta-2 (PLC-beta2), is expressed at highest levels in cells of hematopoietic origin. It is activated by the heterotrimeric G protein alpha q subunits (G alpha(q)) through their C2 domain and long C-terminal extension. It is also activated by the beta-gamma subunits of heterotrimeric G proteins. PI-PLC-beta2 has two cellular binding partners, alpha- and gamma-synuclein. The binding of either alpha- and gamma-synuclein inhibits PI-PLC-beta2 activity through preventing the binding of its activator G alpha(q). However, the binding of gamma-synuclein to PI-PLC-beta2 does not affect its binding to G beta(gamma) subunits or small G proteins, but enhances these signals. Meanwhile, gamma-synuclein may protect PI-PLC-beta2 from protease degradation and contribute to its over-expression in breast cancer. In leukocytes, the G beta(gamma)-mediated activation of PI-PLC-beta2 can be promoted by a scaffolding protein WDR26, which is also required for the translocation of PI-PLC-beta2 from the cytosol to the membrane in polarized leukocytes. PI-PLC-beta2 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. Besides, it has a unique C-terminal coiled-coil (CT) domain necessary for homodimerization. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.
Statistics
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PSSM-Id: 320039
View PSSM: cd16209
Aligned: 5 rows
Threshold Bit Score: 280.226
Threshold Setting Gi: 82254205
Created: 18-Nov-2014
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 30 residues -Click on image for an interactive view with Cn3D
Feature 1:EF-hand motif [structural motif]
Evidence:
  • None

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1         ##############################                                                  
2FJU_B        149 DKILVKLKMQLNSEGKIPVKNFFQMFPADRkrvEAALSACHLPKGKNDAINPEDFPEPVYKSFlmslcprpEIDEIFTSY 228
gi 465956123  147 EKILVKLKMQLSAEGKIPVRNIFQMFPADRkrvEAALHACHLPKGKNDAINPEDFPEKVYKTFlmnlcprpEIDEIFTSL 226
gi 512862569  149 EKIHVKLQLQLNSEGKIPVRNFFQMFPADRkrvEQALNSCHLSKGKNDAINPEDFPESVFRTFlmqlcprpEIDEIFTSY 228
gi 82254205   149 EKIYVRISLHTNKDGKIPVKNIYKMFPADKkrvESALASAHLPKGKYDTMKPDVFTEAAFKVFmnnlcprpEILEIFTSY 228
gi 632977199  149 DKIYTKIKMLVNEERRIPVKSFYQMFPADRkrvEAALSACHLPKLKTDMINLEDFNEVVFQQFlaqlcprpEISQIFDLL 228
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
Feature 1                                                                                
2FJU_B        229 hakAKPYMTKEHLTKFINQKQRDSRLNSLLFPparpdQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPE 299
gi 465956123  227 hskAKPYMTKEHLAKFINKKQRDSRLNDMLFPpakpeQVQGLIEKYEPSGINIQRGQLSPEGMVWFLCGPE 297
gi 512862569  229 hskAKPYMTKVHLTKFINQKQRDSRLNDLIFPpakieQVQGLIEKYEPSVINVQRGQLSPEGMVWFLCGSE 299
gi 82254205   229 s--TKPTMTKENFTKFLNEKQRDSRLNEELFPrlrqdQIKALIDKYEPCSSNTHRSLISPEGLLNFLMGPE 297
gi 632977199  229 kakAKPFLTRDQLCHFVNKIQRDSRLNEELCPplqpaQIQSLIEKYEPSNITARKGHLSPEGLILYLSGPE 299

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