PLCD3

Protein-coding gene in the species Homo sapiens

PLCD3

Identifiers

Aliases

PLCD3, PLC-delta-3, phospholipase C delta 3

External IDs

OMIM: 608795; MGI: 107451; HomoloGene: 14858; GeneCards: PLCD3; OMA:PLCD3 - orthologs

Gene location (Human)

Chr.	Chromosome 17 (human)^[1]

Band	17q21.31	Start	45,108,959 bp^[1]
Band	17q21.31	End	45,133,354 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 11 (mouse)^[2]

Band	11 E1\|11 66.71 cM	Start	102,961,130 bp^[2]
Band	11 E1\|11 66.71 cM	End	102,992,484 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

mucosa of transverse colon

muscle of thigh

apex of heart

gastric mucosa

Descending thoracic aorta

right coronary artery

buccal mucosa cell

left adrenal cortex

ascending aorta

gastrocnemius muscle

Top expressed in

neural layer of retina

gastrula

decidua

vestibular membrane of cochlear duct

otolith organ

utricle

morula

epithelium of lens

sciatic nerve

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	hydrolase activity signal transducer activity metal ion binding phosphoric diester hydrolase activity phosphatidylinositol phospholipase C activity protein binding
Cellular component	cytosol plasma membrane cleavage furrow membrane cytoplasm intracellular anatomical structure
Biological process	angiogenesis lipid catabolic process intracellular signal transduction labyrinthine layer blood vessel development inositol phosphate metabolic process regulation of cell population proliferation lipid metabolism signal transduction inositol trisphosphate biosynthetic process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


113026


72469

Ensembl


ENSG00000161714


ENSMUSG00000020937

UniProt


Q8N3E9


Q8K2J0

RefSeq (mRNA)


NM_133373


NM_152813 NM_001361706

RefSeq (protein)


NP_588614


NP_690026 NP_001348635

Location (UCSC)

Chr 17: 45.11 – 45.13 Mb

Chr 11: 102.96 – 102.99 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3 is an enzyme that in humans is encoded by the PLCD3 gene.^[5]^[6]^[7]

Function

This gene encodes a member of the phospholipase C family, which catalyze the hydrolysis of phosphatidylinositol 4,5-bisphosphate to generate the second messengers diacylglycerol and inositol 1,4,5-trisphosphate (IP₃). Diacylglycerol and IP₃ mediate a variety of cellular responses to extracellular stimuli by inducing protein kinase C and increasing cytosolic Ca²⁺ concentrations. This enzyme localizes to the plasma membrane and requires calcium for activation. Its activity is inhibited by spermine, sphingosine, and several phospholipids.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000161714 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020937 – 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.
^ Kim H, Suh PG, Ryu SH, Park SH (Apr 2000). "Assignment of the human PLC delta3 gene (PLCD3) to human chromosome band 17q21 by fluorescence in situ hybridization". Cytogenetics and Cell Genetics. 87 (3–4): 209–10. doi:10.1159/000015469. PMID 10702670. S2CID 87171791.
^ Ghosh S, Pawelczyk T, Lowenstein JM (Mar 1997). "Phospholipase C isoforms delta 1 and delta 3 from human fibroblasts. High-yield expression in Escherichia coli, simple purification, and properties". Protein Expression and Purification. 9 (2): 262–78. doi:10.1006/prep.1996.0682. PMID 9056492.
^ ^a ^b "Entrez Gene: PLCD3 phospholipase C, delta 3".

Cefai D, Debre P, Kaczorek M, Idziorek T, Autran B, Bismuth G (Dec 1990). "Human immunodeficiency virus-1 glycoproteins gp120 and gp160 specifically inhibit the CD3/T cell-antigen receptor phosphoinositide transduction pathway". The Journal of Clinical Investigation. 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 (Sep 1995). "Exogenous human immunodeficiency virus type-1 Tat protein selectively stimulates a phosphatidylinositol-specific phospholipase C nuclear pathway in the Jurkat T cell line". European Journal of Immunology. 25 (9): 2695–700. doi:10.1002/eji.1830250944. PMID 7589147. S2CID 20562627.
Chen P, Mayne M, Power C, Nath A (Sep 1997). "The Tat protein of HIV-1 induces tumor necrosis factor-alpha production. Implications for HIV-1-associated neurological diseases". The Journal of Biological Chemistry. 272 (36): 22385–8. doi:10.1074/jbc.272.36.22385. PMID 9278385.
Pawełczyk T, Matecki A (1998). "Expression, purification and kinetic properties of human recombinant phospholipase C delta 3". Acta Biochimica Polonica. 44 (2): 221–9. doi:10.18388/abp.1997_4417. PMID 9360711.
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.
Pawelczyk T, Matecki A (Oct 1998). "Localization of phospholipase C delta3 in the cell and regulation of its activity by phospholipids and calcium". European Journal of Biochemistry. 257 (1): 169–77. doi:10.1046/j.1432-1327.1998.2570169.x. PMID 9799116.
Pawelczyk T, Matecki A (Jun 1999). "Phospholipase C-delta3 binds with high specificity to phosphatidylinositol 4,5-bisphosphate and phosphatidic acid in bilayer membranes". European Journal of Biochemistry. 262 (2): 291–8. doi:10.1046/j.1432-1327.1999.00388.x. PMID 10336610.
Haughey NJ, Holden CP, Nath A, Geiger JD (Oct 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". Journal of Neurochemistry. 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 (Jun 2000). "Release of calcium from inositol 1,4,5-trisphosphate receptor-regulated stores by HIV-1 Tat regulates TNF-alpha production in human macrophages". Journal of Immunology. 164 (12): 6538–42. doi:10.4049/jimmunol.164.12.6538. PMID 10843712.
Lin FG, Cheng HF, Lee IF, Kao HJ, Loh SH, Lee WH (Aug 2001). "Downregulation of phospholipase C delta3 by cAMP and calcium". Biochemical and Biophysical Research Communications. 286 (2): 274–80. doi:10.1006/bbrc.2001.5371. PMID 11500033.
Ananthanarayanan B, Das S, Rhee SG, Murray D, Cho W (Feb 2002). "Membrane targeting of C2 domains of phospholipase C-delta isoforms". The Journal of Biological Chemistry. 277 (5): 3568–75. doi:10.1074/jbc.M109705200. PMID 11706040.
Nagase T, Kikuno R, Ohara O (Dec 2001). "Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins". DNA Research. 8 (6): 319–27. doi:10.1093/dnares/8.6.319. PMID 11853319.
Bennasser Y, Badou A, Tkaczuk J, Bahraoui E (Nov 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.
Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (Jul 2004). "Functional proteomics mapping of a human signaling pathway". Genome Research. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.

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)