Activating Compound | Comment | Organism | Structure |
---|---|---|---|
B cell antigen receptor | induces activation of PLC-gamma2, pathway | Mammalia | |
G protein alpha12 | activates PLC-epsilon | Homo sapiens | |
G protein betagamma | activates PLC-beta isoenzymes with the exception of PLC-beta4 | Mammalia | |
G protein qalpha | activates PLC-beta isoenzymes, G protein-coupled receptor-mediated activation | Mammalia | |
additional information | modes of activation/activation pathways of the PLC isoenzymes beta, gamma, delta and epsilon | Mammalia | |
Ras | activator of PLC-epsilon | Homo sapiens | |
receptor protein tyrosine kinase | activates PLC-gamma, growth factor receptor-mediated activation | Mammalia | |
T cell antigen receptor | induces activation of PLC-gamma1, pathway | Mammalia |
Crystallization (Comment) | Organism |
---|---|
PLC-delta1 complexed with inositol 1,4,5-trisphosphate | Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell membrane | the PH domain of PLC-delta1 may tether the enzyme to the cell membrane by specific binding to phosphatidylinositol 4,5-bisphosphate | Rattus norvegicus | - |
- |
membrane | PLC-beta | Mammalia | 16020 | - |
nucleus | PLC-beta1 is the major isoform of the nucleus | Mammalia | 5634 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | requirement, mode of Ca2+ binding at the catalytic domain of PLC-delta1 | Rattus norvegicus | |
Ca2+ | requirement, PLC isoenzymes beta, gamma, delta and epsilon, delta-type isoenzymes are most sensitive | Mammalia |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
85000 | - |
x * 85000, about, PLC-delta isoenzymes, x * 120000-155000, PLC-beta and -gamma isoenzymes, x * 230000-260000, PLC-epsilon | Mammalia |
230000 | - |
x * 230000, x * 260000, two alternatively spliced PLC-epsilon forms | Homo sapiens |
260000 | - |
x * 230000, x * 260000, two alternatively spliced PLC-epsilon forms | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O | Mammalia | regulation of PLC isoenzymes, cellular signaling | 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol | intracellular messengers | ? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
PLC-epsilon | - |
Mammalia | - |
PLC-beta, -gamma, -delta and -epsilon | - |
Rattus norvegicus | - |
PLC-delta1 | - |
Rattus norvegicus PLC-delta1 | - |
PLC-delta1 | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | PLC-gamma1 and 2, tyrosine phosphorylation activates enzyme | Mammalia |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol | mechanism | Mammalia |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
heart | PLC-epsilon, most abundantly in | Homo sapiens | - |
additional information | the two alternatively spliced forms of PLC-epsilon are present in a wide variety of human tissues | Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O | domain organization of the PLC isoenzymes beta, gamma, delta and epsilon, distinct regulatory domains | Mammalia | 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol | - |
? | |
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O | domain structure of PLC-epsilon, contains RasGEF and RA domains | Homo sapiens | 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol | - |
? | |
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O | PLC-delta1, structure of the catalytic domain, His-311 and His-356 act as general acid-base catalysts | Rattus norvegicus | 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol | 4- and 5-phosphoryl groups of inositol 1,4,5-trisphosphate interact with the side chains of Lys-32 and Lys-57 and with those of Lys-30, Arg-40 and Lys-57 of PLC-delta1, respectively | ? | |
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O | regulation of PLC isoenzymes, cellular signaling | Mammalia | 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol | intracellular messengers | ? | |
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O | PLC-delta1, structure of the catalytic domain, His-311 and His-356 act as general acid-base catalysts | Rattus norvegicus PLC-delta1 | 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol | 4- and 5-phosphoryl groups of inositol 1,4,5-trisphosphate interact with the side chains of Lys-32 and Lys-57 and with those of Lys-30, Arg-40 and Lys-57 of PLC-delta1, respectively | ? | |
phosphatidylinositol + H2O | PLC-delta1, structure of the catalytic domain | Rattus norvegicus | ? | - |
? | |
phosphatidylinositol + H2O | PLC-delta1, structure of the catalytic domain | Rattus norvegicus PLC-delta1 | ? | - |
? | |
phosphatidylinositol 4-phosphate + H2O | PLC-delta1, structure of the catalytic domain | Rattus norvegicus | ? | - |
? | |
phosphatidylinositol 4-phosphate + H2O | PLC-delta1, structure of the catalytic domain | Rattus norvegicus PLC-delta1 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 230000, x * 260000, two alternatively spliced PLC-epsilon forms | Homo sapiens |
? | x * 85000, about, PLC-delta isoenzymes, x * 120000-155000, PLC-beta and -gamma isoenzymes, x * 230000-260000, PLC-epsilon | Mammalia |
Synonyms | Comment | Organism |
---|---|---|
More | four PLC subfamilies: beta, gamma, delta and epsilon | Mammalia |