PLCB4

Protein-coding gene in the species Homo sapiens
PLCB4
Identifiers
AliasesPLCB4, ARCND2, PI-PLC, phospholipase C beta 4
External IDsOMIM: 600810; MGI: 107464; HomoloGene: 8471; GeneCards: PLCB4; OMA:PLCB4 - orthologs
Gene location (Human)
Chromosome 20 (human)
Chr.Chromosome 20 (human)[1]
Chromosome 20 (human)
Genomic location for PLCB4
Genomic location for PLCB4
Band20p12.3-p12.2Start9,068,763 bp[1]
End9,481,242 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for PLCB4
Genomic location for PLCB4
Band2 F3|2 66.64 cMStart135,500,931 bp[2]
End135,856,513 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • parotid gland

  • lateral nuclear group of thalamus

  • sural nerve

  • bronchial epithelial cell

  • cerebellar cortex

  • cerebellar hemisphere

  • mucosa of sigmoid colon

  • mucosa of paranasal sinus

  • right hemisphere of cerebellum

  • cerebellar vermis
Top expressed in
  • vestibular membrane of cochlear duct

  • medial geniculate nucleus

  • medial dorsal nucleus

  • parotid gland

  • iris

  • submandibular gland

  • cerebellar vermis

  • lobe of cerebellum

  • lateral geniculate nucleus

  • superior colliculus
More reference expression data
BioGPS


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
  • smooth endoplasmic reticulum
  • parallel fiber to Purkinje cell synapse
  • glutamatergic synapse
  • postsynapse
  • intracellular anatomical structure
Biological process
  • lipid metabolism
  • lipid catabolic process
  • signal transduction
  • intracellular signal transduction
  • inositol phosphate metabolic process
  • G protein-coupled receptor signaling pathway
  • modulation of chemical synaptic transmission
  • inositol trisphosphate biosynthetic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5332

18798

Ensembl

ENSG00000101333

ENSMUSG00000039943

UniProt

Q15147

n/a

RefSeq (mRNA)

NM_000933
NM_001172646
NM_182797

NM_013829
NM_001355153
NM_001355154
NM_001355155
NM_001355156

RefSeq (protein)
NP_000924
NP_001166117
NP_877949
NP_001364063
NP_001364064

NP_001364065
NP_001364071
NP_001364072

n/a

Location (UCSC)Chr 20: 9.07 – 9.48 MbChr 2: 135.5 – 135.86 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. ^ a b c GRCh38: Ensembl release 89: ENSG00000101333 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000039943 – 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.
  5. ^ 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. doi:10.1006/geno.1995.1214. PMID 8530101.
  6. ^ a b "Entrez Gene: PLCB4 phospholipase C, beta 4".

Further reading

  • 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. doi:10.1172/JCI114950. PMC 329852. PMID 1979339.
  • 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. doi:10.1002/eji.1830250944. PMID 7589147. S2CID 20562627.
  • 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. doi:10.1007/s003359900151. PMID 8672127. S2CID 32396932.
  • 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.
  • 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. 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.
  • 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. doi:10.1038/88107. PMID 11329013. S2CID 25064683.
  • Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. Bibcode:2001Natur.414..865D. doi:10.1038/414865a. PMID 11780052.
  • 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • 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. doi:10.1006/viro.2002.1676. PMID 12482669.
  • 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. doi:10.1038/ng1285. PMID 14702039.
  • 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. doi:10.1038/nm1418. PMID 16767099. S2CID 8250592.
  • 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. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
  • v
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3.1.1: Carboxylic
ester hydrolases3.1.2: Thioesterase3.1.3: Phosphatase3.1.4:
Phosphodiesterase3.1.6: SulfataseNuclease (includes
deoxyribonuclease
and ribonuclease)
3.1.11-16:
Exonuclease
Exodeoxyribonuclease
Exoribonuclease
3.1.21-31:
Endonuclease
Endodeoxyribonuclease
Endoribonuclease
either deoxy- or ribo-    
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