PLCB4

Identifiers

PLCB4, ARCND2, PI-PLC, phospholipase C beta 4

External IDs

MGI: 107464 HomoloGene: 8471 GeneCards: PLCB4

Gene location (Human)

Chr.	Chromosome 20 (human)^[1]

Band	No data available	Start	9,068,763 bp^[1]
Band	No data available	End	9,481,242 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 2 (mouse)^[2]

Band	No data available	Start	135,659,011 bp^[2]
Band	No data available	End	136,014,593 bp^[2]

RNA expression pattern

More reference expression data

Gene ontology
Molecular function	• phospholipase C activity • phosphoric diester hydrolase activity • calcium ion binding • protein binding • hydrolase activity • signal transducer activity • phosphatidylinositol phospholipase C activity
Cellular component	• cytosol • dendrite • nucleus • postsynaptic density of dendrite • smooth endoplasmic reticulum • intracellular
Biological process	• lipid metabolic process • lipid catabolic process • signal transduction • intracellular signal transduction • inositol phosphate metabolic process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


5332


18798

Ensembl


ENSG00000101333


ENSMUSG00000039943

UniProt


Q15147


n/a

RefSeq (mRNA)


NM_000933 NM_001172646 NM_182797


NM_013829

RefSeq (protein)


NP_000924 NP_001166117 NP_877949


n/a

Location (UCSC)

Chr 20: 9.07 – 9.48 Mb

Chr 20: 135.66 – 136.01 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4 is an enzyme that in humans is encoded by the PLCB4 gene.^[5]^[6]

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 in the retina. Two transcript variants encoding different isoforms have been found for this gene.^[6]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000101333 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000039943 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Alvarez RA, Ghalayini AJ, Xu P, Hardcastle A, Bhattacharya S, Rao PN, Pettenati MJ, Anderson RE, Baehr W (Feb 1996). "cDNA sequence and gene locus of the human retinal phosphoinositide-specific phospholipase-C beta 4 (PLCB4)". Genomics. 29 (1): 53–61. PMID 8530101. doi:10.1006/geno.1995.1214.
1 2 "Entrez Gene: PLCB4 phospholipase C, beta 4".

Cefai D, Debre P, Kaczorek M, et al. (1991). "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. PMC 329852 . PMID 1979339. doi:10.1172/JCI114950.
Zauli G, Previati M, Caramelli E, et al. (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. PMID 7589147. doi:10.1002/eji.1830250944.
Lyu MS, Park DJ, Rhee SG, Kozak CA (1996). "Genetic mapping of the human and mouse phospholipase C genes.". Mamm. Genome. 7 (7): 501–4. PMID 8672127. doi:10.1007/s003359900151.
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. PMID 9278385. doi:10.1074/jbc.272.36.22385.
Mayne M, Bratanich AC, Chen P, et al. (1998). "HIV-1 tat molecular diversity and induction of TNF-alpha: implications for HIV-induced neurological disease.". Neuroimmunomodulation. 5 (3–4): 184–92. PMID 9730685. doi:10.1159/000026336.
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. PMID 10501179. doi:10.1046/j.1471-4159.1999.0731363.x.
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. PMID 10843712. doi:10.4049/jimmunol.164.12.6538.
Harrington JJ, Sherf B, Rundlett S, et al. (2001). "Creation of genome-wide protein expression libraries using random activation of gene expression". Nat. Biotechnol. 19 (5): 440–5. PMID 11329013. doi:10.1038/88107.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. PMID 11780052. doi:10.1038/414865a.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
Bennasser Y, Badou A, Tkaczuk J, Bahraoui E (2003). "Signaling pathways triggered by HIV-1 Tat in human monocytes to induce TNF-alpha". Virology. 303 (1): 174–80. PMID 12482669. doi:10.1006/viro.2002.1676.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. PMID 14702039. doi:10.1038/ng1285.
Hahn CG, Wang HY, Cho DS, et al. (2006). "Altered neuregulin 1-erbB4 signaling contributes to NMDA receptor hypofunction in schizophrenia". Nat. Med. 12 (7): 824–8. PMID 16767099. doi:10.1038/nm1418.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. PMID 17081983. doi:10.1016/j.cell.2006.09.026.

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 UvrABC endonuclease
Endoribonuclease	RNase III RNase H 1 2A 2B 2C RNase P RNase A 1 2 3 4/5 RNase T1 RNA-induced silencing complex
either deoxy- or ribo-	Aspergillus nuclease S1 Micrococcal nuclease

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
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)

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PLCB4

Function

References

Further reading