PLCB3

Protein-coding gene in the species Homo sapiens

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; OMA:PLCB3 - orthologs

Gene location (Human)

Chr.	Chromosome 11 (human)^[1]

Band	11q13.1	Start	64,251,530 bp^[1]
Band	11q13.1	End	64,269,150 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 19 (mouse)^[2]

Band	19 A\|19 5.1 cM	Start	6,929,693 bp^[2]
Band	19 A\|19 5.1 cM	End	6,953,838 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

mucosa of transverse colon

tendon of biceps brachii

duodenum

buccal mucosa cell

right adrenal gland

ectocervix

left adrenal cortex

stromal cell of endometrium

right adrenal cortex

right coronary artery

Top expressed in

crypt of lieberkuhn of small intestine

duodenum

jejunum

lumbar spinal ganglion

ileum

left colon

cumulus cell

migratory enteric neural crest cell

granulocyte

More reference expression data

BioGPS


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

Species

Human

Mouse

Entrez


5331


18797

Ensembl


ENSG00000149782


ENSMUSG00000024960

UniProt


Q01970


P51432

RefSeq (mRNA)


NM_000932 NM_001184883 NM_001316314


NM_001290349 NM_008874

RefSeq (protein)


NP_000923 NP_001171812 NP_001303243


NP_001277278 NP_032900

Location (UCSC)

Chr 11: 64.25 – 64.27 Mb

Chr 19: 6.93 – 6.95 Mb

PubMed search

^[3]

^[4]

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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000149782 – Ensembl, May 2017
^ ^a ^b ^c 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.

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4:
Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease
and ribonuclease)

3.1.11-16:
Exonuclease

Exodeoxyribonuclease	RecBCD
Exoribonuclease	Oligonucleotidase

3.1.21-31:
Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme;see {{Restriction enzyme}} UvrABC endonuclease
Endoribonuclease	RNase III Drosha: Microprocessor complex Dicer: RNA-induced silencing complex RNase H 1 2A 2B 2C RNase P RNase A RNase Z RNase E 1 2 3 4/5 RNase T1
either deoxy- or ribo-	Nuclease S1 Mung bean nuclease Serratia marcescens nuclease Micrococcal nuclease

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme 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)