1QAS,1DJG,1DJX


Conserved Protein Domain Family
PI-PLCc_delta1

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cd08629: PI-PLCc_delta1 
Click on image for an interactive view with Cn3D
Catalytic domain of metazoan phosphoinositide-specific phospholipase C-delta1
This subfamily corresponds to the catalytic domain present in metazoan phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11)-delta1 isozymes. PI-PLC is a signaling enzyme that hydrolyzes the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which then phosphorylates other molecules, leading to altered cellular activity. Calcium is required for the catalysis. PLC-delta represents a class of mammalian PI-PLC that has an N-terminal pleckstrin homology (PH) domain, an array of EF hands, a PLC catalytic core domain, and a C-terminal C2 domain. This subfamily corresponds to the catalytic domain which is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1,3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Unlike PI-PLC-delta 4, PI-PLC-delta1 and 3 possess a putative nuclear export sequence (NES) located in the EF-hand domain, which may be responsible transporting PI-PLC-delta1and 3 from the cell nucleus. Experiments show PI-PLC-delta1 is essential for normal hair formation.
Statistics
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PSSM-Id: 176566
Aligned: 5 rows
Threshold Bit Score: 455.263
Created: 9-Mar-2010
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 2 residues -Click on image for an interactive view with Cn3D
Feature 1:catalytic site [active site]
Evidence:
  • Comment:Both prokaryotic and eukaryotic PI-PLCs utilize a similar catalytic mechanism, a general base and acid catalysis involving two well conserved histidines. It consists of two steps, a phosphotransfer and a phosphodiesterase reaction.
  • Structure:1DJX; Rat Phosphoinositide-specific phospholipase C-Delta1 catalytic residues are well conserved in all eukaryotic PI-PLCs.
  • Citation:PMID 9048554

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                     #                                            #                  
1QAS_A    161 YQDMDQPLSHYLVSSSHNTYLLEDQLTGPSStEAYIRALCKGCRCLELDCWDGPNqEPIIYHGYTFTSKILFCDVLRAIR 240 Norway rat
1DJG_A    163 YQDMDQPLSHYLVSSSHNTYLLEDQLTGPSStEAYIRALCKGCRCLELDCWDGPNqEPIIYHGYTFTSKILFCDVLRAIR 242 Norway rat
1DJX_B    163 YQDMDQPLSHYLVSSSHNTYLLEDQLTGPSStEAYIRALCKGCRCLELDCWDGPNqEPIIYHGYTFTSKILFCDVLRAIR 242 Norway rat
XP_418522 316 YQDMTQPLSHYFVSSSHNTYLMDDQLTGPSStEAYIRALTKGCRCVELDCWDGPNsEPIIYHGYTLTSKILFSDVIKAIK 395 chicken
NP_956362 291 YHDMNQPLSHYFISSSHNTYLMEDQLKGPSStEAYIKALLKGCRCVELDCWDGSDgEPVIYHGYTLTSKILFKDVIKAIK 370 zebrafish
Feature 1                                                                                     
1QAS_A    241 DYAFKASPYPVILSLENHCSLEQQRVMARHLRAILGPILLDQPLDgvt-tsLPSPEQLKGKILLKGKKLggllpaggeng 319 Norway rat
1DJG_A    243 DYAFKASPYPVILSLENHCSLEQQRVMARHLRAILGPILLDQPLDgvt-tsLPSPEQLKGKILLKGKKLggllpaggeng 321 Norway rat
1DJX_B    243 DYAFKASPYPVILSLENHCSLEQQRVMARHLRAILGPILLDQPLDgvt-tsLPSPEQLKGKILLKGKKLggllpaggeng 321 Norway rat
XP_418522 396 NYAFKTSPYPVIISLENHCSLEQQKVMAQHMTTILQDMLLVAPIDgsk-sqFPSPEQLKGKILVKGKKLsrqedptgtng 474 chicken
NP_956362 371 EYAFKTSEYPVILSLENHCGVEQQKIMAQHLTSILGSALVTKPLGdqmptcLPAPEELKGRFIVKGKRLdklenafsdes 450 zebrafish
Feature 1                                                                                     
1QAS_A    320 seatdvsdeve---aaemedeavrsqvqhkpkedklKLVPELSDMIiYCKSVHFGGFSspgtsgqaFYEMASFSESRALR 396 Norway rat
1DJG_A    322 seatdvsdeve---aaemedeavrsqvqhkpkedklKLVPELSDMIiYCKSVHFGGFSspgtsgqaFYEMASFSESRALR 398 Norway rat
1DJX_B    322 seatdvsdeve---aaemedeavrsqvqhkpkedklKLVPELSDMIiYCKSVHFGGFSspgtsgqaFYEMASFSESRALR 398 Norway rat
XP_418522 475 nnnleaedvsdedeaaemedesvktevqqkgksdtlKLAKELSDTVvYCKSVHFNGFEdpsh-praFYEMSSFTESKALK 553 chicken
NP_956362 451 kmadeesvs--------eeeddegdeennekksgslKLAKELSDIViYCKSVPFHGLEdsre-khsFYEMASFKEGKALK 521 zebrafish
Feature 1                                                                       
1QAS_A    397 LLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDN 462 Norway rat
1DJG_A    399 LLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDN 464 Norway rat
1DJX_B    399 LLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDN 464 Norway rat
XP_418522 554 LAQESGNSFILHNIRHLSRIYPAGWRTDSSNYNPVDLWNVGCQIVALNFQTGGTEMDVYQGRFQDN 619 chicken
NP_956362 522 LAEESATEYIRHNTDKLSRIYPGGMRTDSSNYNPVPMWNAGCQIVALNFQTPCLEMDLNQGLFYQN 587 zebrafish

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