PLCD4

Identifiers

PLCD4, phospholipase C delta 4

External IDs

OMIM: 605939 MGI: 107469 HomoloGene: 88782 GeneCards: PLCD4

Gene location (Human)

Chr.	Chromosome 2 (human)^[1]

Band	2q35	Start	218,607,855 bp^[1]
Band	2q35	End	218,637,184 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 1 (mouse)^[2]

Band	1 C4\|1 38.54 cM	Start	74,582,047 bp^[2]
Band	1 C4\|1 38.54 cM	End	74,606,953 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

vastus lateralis muscle

gastrocnemius muscle

skeletal muscle tissue

biceps brachii

deltoid muscle

tibialis anterior muscle

gastric mucosa

sural nerve

pituitary gland

anterior pituitary

Top expressed in

triceps brachii muscle

knee joint

vastus lateralis muscle

seminiferous tubule

spermatid

sternocleidomastoid muscle

spermatocyte

tibialis anterior muscle

skeletal muscle tissue

temporal muscle

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	phosphoric diester hydrolase activity phospholipase C activity calcium ion binding hydrolase activity signal transducer activity metal ion binding phosphatidylinositol phospholipase C activity
Cellular component	plasma membrane nuclear membrane intracellular anatomical structure endoplasmic reticulum nucleus membrane cytoplasm endoplasmic reticulum membrane cytosol
Biological process	lipid catabolic process acrosome reaction intracellular signal transduction phosphatidylinositol metabolic process signal transduction lipid metabolism inositol phosphate metabolic process inositol trisphosphate biosynthetic process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


84812


18802

Ensembl


ENSG00000115556


ENSMUSG00000026173

UniProt


Q9BRC7


Q8K3R3

RefSeq (mRNA)


NM_032726


NM_001081456 NM_148937

RefSeq (protein)


NP_116115


NP_001074925 NP_683739

Location (UCSC)

Chr 2: 218.61 – 218.64 Mb

Chr 1: 74.58 – 74.61 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4 is an enzyme that in humans is encoded by the PLCD4 gene.^[5]^[6]^[7]

References

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.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
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.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
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.
Ananthanarayanan B, Das S, Rhee SG, et al. (2002). "Membrane targeting of C2 domains of phospholipase C-delta isoforms". J. Biol. Chem. 277 (5): 3568–75. doi:10.1074/jbc.M109705200. PMID 11706040.
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.
Lee SB, Várnai P, Balla A, et al. (2004). "The pleckstrin homology domain of phosphoinositide-specific phospholipase Cdelta4 is not a critical determinant of the membrane localization of the enzyme". J. Biol. Chem. 279 (23): 24362–71. doi:10.1074/jbc.M312772200. PMID 15037625.
Leung DW, Tompkins C, Brewer J, et al. (2004). "Phospholipase C δ-4 overexpression upregulates ErbB1/2 expression, Erk signaling pathway, and proliferation in MCF-7 cells". Mol. Cancer. 3: 15. doi:10.1186/1476-4598-3-15. PMC 420486. PMID 15140260.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Chae SW, Kim JM, Yun YP, et al. (2007). "Identification and analysis of the promoter region of the human PLC-delta4 gene". Mol. Biol. Rep. 34 (2): 69–77. doi:10.1007/s11033-006-9014-x. PMID 17394098. S2CID 24577383.

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)

References

Further reading