PLCB3

PLCB3
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3OHM, 4GNK, 4QJ3, 4QJ4, 4QJ5
Identifiers
Aliases	PLCB3, phospholipase C beta 3, SMDCD
External IDs	OMIM: 600230 MGI: 104778 HomoloGene: 47960 GeneCards: PLCB3
Gene location (Human)
Chr.	Chromosome 11 (human)[1]
End	64,269,150 bp[1]
Gene location (Mouse)
Chr.	Chromosome 19 (mouse)[2]
End	6,953,838 bp[2]
RNA expression pattern
	Top expressed in
	duodenum; ; right adrenal gland; ; stromal cell of endometrium; ; right coronary artery; ; left uterine tube; ; left coronary artery; ; canal of the cervix; ; ascending aorta; ; vagina; ; popliteal artery;
	Top expressed in
	crypt of lieberkuhn of small intestine; ; duodenum; ; jejunum; ; ileum; ; lip; ; left colon; ; cumulus cell; ; Paneth cell; ; esophagus; ; stomach;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	calcium ion binding; signal transducer activity; phosphoric diester hydrolase activity; hydrolase activity; phosphatidylinositol phospholipase C activity; cadherin binding; protein binding; calmodulin binding; phospholipase C activity;
Cellular component	cytosol; membrane; nucleoplasm; protein-containing complex; postsynaptic cytosol;
Biological process	intracellular signal transduction; lipid metabolism; inositol phosphate metabolic process; lipid catabolic process; regulation of systemic arterial blood pressure; signal transduction; Wnt signaling pathway, calcium modulating pathway; G protein-coupled receptor signaling pathway; inositol trisphosphate biosynthetic process; phosphatidylinositol-mediated signaling; release of sequestered calcium ion into cytosol;
	Sources:Amigo / QuickGO
Orthologs
	5331
	18797
	ENSG00000149782
	ENSMUSG00000024960
	Q01970
	P51432
	NM_000932; NM_001184883; NM_001316314
	NM_001290349; NM_008874
	NP_000923; NP_001171812; NP_001303243
	NP_001277278; NP_032900
	Wikidata
View/Edit Human	View/Edit Mouse

1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3 is an enzyme that in humans is encoded by the PLCB3 gene.[5][6]

The gene codes for the enzyme phospholipase C β3. The enzyme 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, as well as G-beta gamma subunits.

Interactions

PLCB3 has been shown to interact with Sodium-hydrogen exchange regulatory cofactor 2.[7]

References

GRCh38: Ensembl release 89: ENSG00000149782 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000024960 - 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.
Weber G, Friedman E, Grimmond S, Hayward NK, Phelan C, Skogseid B, Gobl A, Zedenius J, Sandelin K, Teh BT (March 1995). "The phospholipase C beta 3 gene located in the MEN1 region shows loss of expression in endocrine tumours". Hum. Mol. Genet. 3 (10): 1775–81. doi:10.1093/hmg/3.10.1775. PMID 7849701.
"Entrez Gene: PLCB3 phospholipase C, beta 3 (phosphatidylinositol-specific)".
Hwang JI, Heo K, Shin KJ, Kim E, Yun C, Ryu SH, Shin HS, Suh PG (June 2000). "Regulation of phospholipase C-beta 3 activity by Na+/H+ exchanger regulatory factor 2". J. Biol. Chem. 275 (22): 16632–7. doi:10.1074/jbc.M001410200. PMID 10748023.

Carozzi AJ, Kriz RW, Webster C, Parker PJ (1992). "Identification, purification and characterization of a novel phosphatidylinositol-specific phospholipase C, a third member of the beta subfamily". Eur. J. Biochem. 210 (2): 521–9. doi:10.1111/j.1432-1033.1992.tb17450.x. PMID 1333955.
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. S2CID 20562627.
Lagercrantz J, Carson E, Phelan C, Grimmond S, Rosén A, Daré E, Nordenskjöld M, Hayward NK, Larsson C, Weber G (1995). "Genomic organization and complete cDNA sequence of the human phosphoinositide-specific phospholipase C beta 3 gene (PLCB3)". Genomics. 26 (3): 467–72. doi:10.1016/0888-7543(95)80164-H. PMID 7607669.
Mazuruk K, Schoen TJ, Chader GJ, Rodriguez IR (1995). "Structural organization and expression of the human phosphatidylinositol-specific phospholipase C beta-3 gene". Biochem. Biophys. Res. Commun. 212 (1): 190–5. doi:10.1006/bbrc.1995.1955. PMID 7612006.
Sinke RJ, Geurts van Kessel AG (1995). "Localization of the human phosphatidylinositol-specific phospholipase c beta 3 gene (PLCB3) within chromosome band 11q13". Genomics. 25 (2): 568–9. doi:10.1016/0888-7543(95)80060-Y. PMID 7789993.
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.
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.
Wang S, Zhou Y, Lukinius A, Oberg K, Skogseid B, Gobl A (1998). "Molecular cloning and characterization of a cDNA encoding mouse phospholipase C-beta3". Biochim. Biophys. Acta. 1393 (1): 173–8. doi:10.1016/s0005-2760(98)00074-5. PMID 9714794.
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.
Hwang JI, Heo K, Shin KJ, Kim E, Yun C, Ryu SH, Shin HS, Suh PG (2000). "Regulation of phospholipase C-beta 3 activity by Na+/H+ exchanger regulatory factor 2". J. Biol. Chem. 275 (22): 16632–7. doi:10.1074/jbc.M001410200. PMID 10748023.
Wang JC, Waltner-Law M, Yamada K, Osawa H, Stifani S, Granner DK (2000). "Transducin-like enhancer of split proteins, the human homologs of Drosophila groucho, interact with hepatic nuclear factor 3beta". J. Biol. Chem. 275 (24): 18418–23. doi:10.1074/jbc.M910211199. PMID 10748198.
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.
Caricasole A, Sala C, Roncarati R, Formenti E, Terstappen GC (2000). "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.
Stålberg P, Lopez-Egido JR, Wang S, Gobl A, Oberg K, Skogseid B (2001). "Differentially expressed cDNAs in PLCbeta3-induced tumor suppression in a human endocrine pancreatic tumor cell line: activation of the human mismatch repair protein 3 gene". Biochem. Biophys. Res. Commun. 281 (1): 227–31. doi:10.1006/bbrc.2001.4329. PMID 11178984.
Xia C, Bao Z, Yue C, Sanborn BM, Liu M (2001). "Phosphorylation and regulation of G-protein-activated phospholipase C-beta 3 by cGMP-dependent protein kinases". J. Biol. Chem. 276 (23): 19770–7. doi:10.1074/jbc.M006266200. PMID 11278298.
Yue C, Sanborn BM (2001). "KN-93 inhibition of G protein signaling is independent of the ability of Ca2+/calmodulin-dependent protein kinase II to phosphorylate phospholipase Cbeta3 on 537-Ser". Mol. Cell. Endocrinol. 175 (1–2): 149–56. doi:10.1016/S0303-7207(01)00383-5. PMID 11325525. S2CID 338776.
Bennasser Y, Badou A, Tkaczuk J, Bahraoui E (2002). "Signaling pathways triggered by HIV-1 Tat in human monocytes to induce TNF-alpha". Virology. 303 (1): 174–80. doi:10.1006/viro.2002.1676. PMID 12482669.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000149782 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000024960 - 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.

[pmid7849701-5] Weber G, Friedman E, Grimmond S, Hayward NK, Phelan C, Skogseid B, Gobl A, Zedenius J, Sandelin K, Teh BT (March 1995). "The phospholipase C beta 3 gene located in the MEN1 region shows loss of expression in endocrine tumours". Hum. Mol. Genet. 3 (10): 1775–81. doi:10.1093/hmg/3.10.1775. PMID 7849701.

[entrez-6] "Entrez Gene: PLCB3 phospholipase C, beta 3 (phosphatidylinositol-specific)".

[pmid10748023-7] Hwang JI, Heo K, Shin KJ, Kim E, Yun C, Ryu SH, Shin HS, Suh PG (June 2000). "Regulation of phospholipase C-beta 3 activity by Na+/H+ exchanger regulatory factor 2". J. Biol. Chem. 275 (22): 16632–7. doi:10.1074/jbc.M001410200. PMID 10748023.

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited 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)

PLCB3

Interactions

References

Further reading