PLCB1

PLCB1
Identifiers
Aliases	PLCB1, EIEE12, PI-PLC, PLC-154, PLC-I, PLC154, PLCB1A, PLCB1B, PLC-beta-1, phospholipase C beta 1
External IDs	OMIM: 607120 MGI: 97613 HomoloGene: 22876 GeneCards: PLCB1
Gene location (Human)
Chr.	Chromosome 20 (human)[1]
End	8,968,360 bp[1]
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)[2]
End	135,475,258 bp[2]
RNA expression pattern
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	• calcium ion binding; • protein homodimerization activity; • GO:0005097, GO:0005099, GO:0005100 GTPase activator activity; • signal transducer activity; • GO:0001948 protein binding; • phosphoric diester hydrolase activity; • enzyme binding; • phosphatidylinositol-4,5-bisphosphate binding; • hydrolase activity; • lamin binding; • phosphatidylinositol phospholipase C activity; • phospholipase C activity; • calmodulin binding;
Cellular component	• cytoplasm; • cytosol; • nuclear speck; • not the membrane; • membrane; • myelin; • nuclear chromatin; • extracellular exosome; • cell nucleus; • postsynapse; • glutamatergic synapse; • GABA-ergic synapse; • macromolecular complex;
Biological process	• G-protein coupled acetylcholine receptor signaling pathway; • glutamate receptor signaling pathway; • insulin-like growth factor receptor signaling pathway; • interleukin-15-mediated signaling pathway; • GO:0007243 intracellular signal transduction; • positive regulation of developmental growth; • phosphatidylinositol metabolic process; • negative regulation of monocyte extravasation; • positive regulation of interleukin-12 production; • regulation of G-protein coupled receptor protein signaling pathway; • lipid metabolism; • inositol phosphate metabolic process; • positive regulation of JNK cascade; • memory; • regulation of cell cycle; • positive regulation of transcription, DNA-templated; • lipid catabolic process; • positive regulation of G1/S transition of mitotic cell cycle; • interleukin-1-mediated signaling pathway; • positive regulation of acrosome reaction; • brain development; • G2/M transition of mitotic cell cycle; • interleukin-12-mediated signaling pathway; • positive regulation of myoblast differentiation; • positive regulation of CD24 biosynthetic process; • cerebral cortex development; • activation of meiosis involved in egg activation; • regulation of fertilization; • positive regulation of embryonic development; • negative regulation of transcription, DNA-templated; • fat cell differentiation; • signal transduction; • Wnt signaling pathway, calcium modulating pathway; • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity; • G-protein coupled receptor signaling pathway; • postsynaptic modulation of chemical synaptic transmission; • regulation of retrograde trans-synaptic signaling by endocanabinoid; • inositol trisphosphate biosynthetic process; • phosphatidylinositol-mediated signaling; • release of sequestered calcium ion into cytosol;
	Sources:Amigo / QuickGO
Orthologs
	23236
	18795
	ENSG00000182621
	ENSMUSG00000051177
	Q9NQ66
	Q9Z1B3
	NM_015192; NM_182734
	NM_001145830; NM_019677
	NP_056007; NP_877398
	NP_001139302; NP_062651
	Wikidata
View/Edit Human	View/Edit Mouse

1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1 is an enzyme that in humans is encoded by the PLCB1 gene.[5][6][7]

Function

The protein encoded by this gene catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of many extracellular signals. This gene is activated by two G-protein alpha subunits, alpha-q and alpha-11. Two transcript variants encoding different isoforms have been found for this gene.[7]

Interactions

PLCB1 has been shown to interact with TRPM7.[8]

Pathology

Homozygous PLCB1 deletion is associated with malignant migrating partial seizures in infancy.[9]

References

GRCh38: Ensembl release 89: ENSG00000182621 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000051177 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Peruzzi D, Calabrese G, Faenza I, Manzoli L, Matteucci A, Gianfrancesco F, Billi AM, Stuppia L, Palka G, Cocco L (Jun 2000). "Identification and chromosomal localisation by fluorescence in situ hybridisation of human gene of phosphoinositide-specific phospholipase C beta(1)". Biochim. Biophys. Acta. 1484 (2–3): 175–82. doi:10.1016/s1388-1981(00)00012-3. PMID 10760467.
Caricasole A, Sala C, Roncarati R, Formenti E, Terstappen GC (Jan 2001). "Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1)". Biochim. Biophys. Acta. 1517 (1): 63–72. doi:10.1016/S0167-4781(00)00260-8. PMID 11118617.
"Entrez Gene: PLCB1 phospholipase C, beta 1 (phosphoinositide-specific)".
Runnels LW, Yue L, Clapham DE (May 2002). "The TRPM7 channel is inactivated by PIP(2) hydrolysis". Nat. Cell Biol. 4 (5): 329–36. doi:10.1038/ncb781. PMID 11941371. S2CID 21592843.
Poduri A, Chopra SS, Neilan EG, Elhosary PC, Kurian MA, Meyer E, Barry BJ, Khwaja OS, Salih MA, Stödberg T, Scheffer IE, Maher ER, Sahin M, Wu BL, Berry GT, Walsh CA, Picker J, Kothare SV (2012). "Homozygous PLCB1 deletion associated with malignant migrating partial seizures in infancy". Epilepsia. 53 (8): e146–50. doi:10.1111/j.1528-1167.2012.03538.x. PMC 3851296. PMID 22690784.

Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T (2002). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. doi:10.1093/dnares/9.3.99. PMID 12168954.
Martelli AM, Fiume R, Faenza I, Tabellini G, Evangelista C, Bortul R, Follo MY, Falà F, Cocco L (2005). "Nuclear phosphoinositide specific phospholipase C (PI-PLC)-beta 1: a central intermediary in nuclear lipid-dependent signal transduction". Histol. Histopathol. 20 (4): 1251–60. PMID 16136505.
Cocco L, Follo MY, Faenza I, Bavelloni A, Billi AM, Martelli AM, Manzoli L (2007). "Nuclear inositide signaling: an appraisal of phospholipase C beta 1 behavior in myelodysplastic and leukemia cells". Adv. Enzyme Regul. 47: 2–9. doi:10.1016/j.advenzreg.2006.12.003. PMID 17335878.
Cefai D, Debre P, Kaczorek M, Idziorek T, Autran B, Bismuth G (1990). "Human immunodeficiency virus-1 glycoproteins gp120 and gp160 specifically inhibit the CD3/T cell-antigen receptor phosphoinositide transduction pathway". J. Clin. Invest. 86 (6): 2117–24. doi:10.1172/JCI114950. PMC 329852. PMID 1979339.
Zauli G, Previati M, Caramelli E, Bassini A, Falcieri E, Gibellini D, Bertolaso L, Bosco D, Robuffo I, Capitani S (1995). "Exogenous human immunodeficiency virus type-1 Tat protein selectively stimulates a phosphatidylinositol-specific phospholipase C nuclear pathway in the Jurkat T cell line". Eur. J. Immunol. 25 (9): 2695–700. doi:10.1002/eji.1830250944. PMID 7589147.
Hwang SC, Park KH, Ha MJ, Noh IS, Park TB, Lee YH (1996). "Distribution of phospholipase C isozymes in normal human lung tissue and their immunohistochemical localization". J. Korean Med. Sci. 11 (4): 305–13. doi:10.3346/jkms.1996.11.4.305. PMC 3054083. PMID 8878798.
Chen P, Mayne M, Power C, Nath A (1997). "The Tat protein of HIV-1 induces tumor necrosis factor-alpha production. Implications for HIV-1-associated neurological diseases". J. Biol. Chem. 272 (36): 22385–8. doi:10.1074/jbc.272.36.22385. PMID 9278385.
Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (1998). "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 5 (1): 31–9. doi:10.1093/dnares/5.1.31. PMID 9628581.
Snow BE, Hall RA, Krumins AM, Brothers GM, Bouchard D, Brothers CA, Chung S, Mangion J, Gilman AG, Lefkowitz RJ, Siderovski DP (1998). "GTPase activating specificity of RGS12 and binding specificity of an alternatively spliced PDZ (PSD-95/Dlg/ZO-1) domain". J. Biol. Chem. 273 (28): 17749–55. doi:10.1074/jbc.273.28.17749. PMID 9651375.
Mayne M, Bratanich AC, Chen P, Rana F, Nath A, Power C (1998). "HIV-1 tat molecular diversity and induction of TNF-alpha: implications for HIV-induced neurological disease". Neuroimmunomodulation. 5 (3–4): 184–92. doi:10.1159/000026336. PMID 9730685. S2CID 19529677.
Haughey NJ, Holden CP, Nath A, Geiger JD (1999). "Involvement of inositol 1,4,5-trisphosphate-regulated stores of intracellular calcium in calcium dysregulation and neuron cell death caused by HIV-1 protein tat". J. Neurochem. 73 (4): 1363–74. doi:10.1046/j.1471-4159.1999.0731363.x. PMID 10501179. S2CID 25410140.
Mayne M, Holden CP, Nath A, Geiger JD (2000). "Release of calcium from inositol 1,4,5-trisphosphate receptor-regulated stores by HIV-1 Tat regulates TNF-alpha production in human macrophages". J. Immunol. 164 (12): 6538–42. doi:10.4049/jimmunol.164.12.6538. PMID 10843712.
Tang Y, Tang J, Chen Z, Trost C, Flockerzi V, Li M, Ramesh V, Zhu MX (2000). "Association of mammalian trp4 and phospholipase C isozymes with a PDZ domain-containing protein, NHERF". J. Biol. Chem. 275 (48): 37559–64. doi:10.1074/jbc.M006635200. PMID 10980202.
Dowal L, Elliott J, Popov S, Wilkie TM, Scarlata S (2001). "Determination of the contact energies between a regulator of G protein signaling and G protein subunits and phospholipase C beta 1". Biochemistry. 40 (2): 414–21. doi:10.1021/bi001923+. PMID 11148035.
Xu A, Wang Y, Xu LY, Gilmour RS (2001). "Protein kinase C alpha -mediated negative feedback regulation is responsible for the termination of insulin-like growth factor I-induced activation of nuclear phospholipase C beta1 in Swiss 3T3 cells". J. Biol. Chem. 276 (18): 14980–6. doi:10.1074/jbc.M009144200. PMID 11278470.
Xu A, Suh PG, Marmy-Conus N, Pearson RB, Seok OY, Cocco L, Gilmour RS (2001). "Phosphorylation of nuclear phospholipase C beta1 by extracellular signal-regulated kinase mediates the mitogenic action of insulin-like growth factor I". Mol. Cell. Biol. 21 (9): 2981–90. doi:10.1128/MCB.21.9.2981-2990.2001. PMC 86927. PMID 11287604.
Vitale M, Matteucci A, Manzoli L, Rodella L, Mariani AR, Zauli G, Falconi M, Billi AM, Martelli AM, Gilmour RS, Cocco L (2001). "Interleukin 2 activates nuclear phospholipase Cbeta by mitogen-activated protein kinase-dependent phosphorylation in human natural killer cells". FASEB J. 15 (10): 1789–91. doi:10.1096/fj.01-0008fje. PMID 11481231. S2CID 13373496.
Singer AU, Waldo GL, Harden TK, Sondek J (2002). "A unique fold of phospholipase C-beta mediates dimerization and interaction with G alpha q". Nat. Struct. Biol. 9 (1): 32–6. doi:10.1038/nsb731. PMID 11753430. S2CID 13301839.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000182621 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000051177 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10760467-5] Peruzzi D, Calabrese G, Faenza I, Manzoli L, Matteucci A, Gianfrancesco F, Billi AM, Stuppia L, Palka G, Cocco L (Jun 2000). "Identification and chromosomal localisation by fluorescence in situ hybridisation of human gene of phosphoinositide-specific phospholipase C beta(1)". Biochim. Biophys. Acta. 1484 (2–3): 175–82. doi:10.1016/s1388-1981(00)00012-3. PMID 10760467.

[pmid11118617-6] Caricasole A, Sala C, Roncarati R, Formenti E, Terstappen GC (Jan 2001). "Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1)". Biochim. Biophys. Acta. 1517 (1): 63–72. doi:10.1016/S0167-4781(00)00260-8. PMID 11118617.

[entrez-7] "Entrez Gene: PLCB1 phospholipase C, beta 1 (phosphoinositide-specific)".

[pmid11941371-8] Runnels LW, Yue L, Clapham DE (May 2002). "The TRPM7 channel is inactivated by PIP(2) hydrolysis". Nat. Cell Biol. 4 (5): 329–36. doi:10.1038/ncb781. PMID 11941371. S2CID 21592843.

[9] Poduri A, Chopra SS, Neilan EG, Elhosary PC, Kurian MA, Meyer E, Barry BJ, Khwaja OS, Salih MA, Stödberg T, Scheffer IE, Maher ER, Sahin M, Wu BL, Berry GT, Walsh CA, Picker J, Kothare SV (2012). "Homozygous PLCB1 deletion associated with malignant migrating partial seizures in infancy". Epilepsia. 53 (8): e146–50. doi:10.1111/j.1528-1167.2012.03538.x. PMC 3851296. PMID 22690784.

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

PLCB1

Function

Interactions

Pathology

References

Further reading