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Information on EC 3.1.4.3 - phospholipase C and Organism(s) Mus musculus and UniProt Accession Q8BGN3
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3.1.4.3 phospholipase CIUBMB Comments
The bacterial enzyme, which is a zinc protein, also acts on sphingomyelin and phosphatidylinositol; that from seminal plasma does not act on phosphatidylinositol.
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Word Map
- 3.1.4.3
- inositol
- agonist
- phosphatidylinositol
- pkc
- phospholipid
- diacylglycerol
- phosphoinositide
- cyclase
- pertussis
- camp
-
phorbol
- g-proteins
- platelet
-
arachidonic
- 1,4,5-trisphosphate
- 4,5-bisphosphate
-
receptor-mediated
- vibrio
- thapsigargin
- trisphosphate
- adenylate
-
protein-coupled
-
blocker
-
adenylyl
- phospholipases
-
muscarinic
-
phosphatidic
- cereus
- carbachol
- perfringens
- pip2
-
fura-2
- neomycin
-
ca2+-free
-
phosphatidylinositol-specific
-
metabotropic
-
13-acetate
-
thromboxane
- nifedipine
- parahaemolyticus
- staurosporine
- bradykinin
- enterotoxin
-
desensitization
-
ryanodine
-
prelabeled
-
toxin-sensitive
-
store-operated
- chelerythrine
-
agonist-induced
- analysis
- drug development
- medicine
- food industry
- pharmacology
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
phospholipase c, plc, hemolysin, pc-plc, lecithinase, phosphatidylcholine-specific phospholipase c, plcbeta, plcg2, beta toxin, plcg1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-toxin
-
-
-
-
Beta toxin
-
-
-
-
Beta-hemolysin
-
-
-
-
Beta-toxin
-
-
-
-
Cbp
-
-
-
-
Clostridium oedematiens beta- and gamma-toxins
-
-
-
-
Clostridium welchii alpha-toxin
-
-
-
-
Gamma-toxin
-
-
-
-
Heat labile-hemolysin
-
-
-
-
heat-labile hemolysin
-
-
-
-
Hemolysin
-
-
-
-
Lecithinase
-
-
-
-
lecithinase C
-
-
-
-
lipophosphodiesterase C
-
-
-
-
lipophosphodiesterase I
-
-
-
-
MTP40 antigen
-
-
-
-
PC-PLC
phosphatidase C
-
-
-
-
Phosphatidylcholine cholinephosphohydrolase
-
-
-
-
PLC
-
-
-
-
SMase
-
-
-
-
sphingomyelinase
-
-
-
-
PC-PLC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
phosphatidylcholine cholinephosphohydrolase
The bacterial enzyme, which is a zinc protein, also acts on sphingomyelin and phosphatidylinositol; that from seminal plasma does not act on phosphatidylinositol.
CAS REGISTRY NUMBER
COMMENTARY
9001-86-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
p-nitrophenyl phenylphosphate + H2O
?
pNPPP, classical NPP substrate
-
-
?
p-nitrophenyl phosphorylcholine + H2O
?
recombinant NPP6 efficiently hydrolyzes the classical substrate for phospholipase C
-
-
?
p-nitrophenyl phosphorylcholine + H2O
? + p-nitrophenol
pNPPC, classical NPP substrate
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
additional information
?
-
release nucleoside 5'-monophosphate from a variety of nucleotides and nucleotide derivatives
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
additional information
?
-
release nucleoside 5'-monophosphate from a variety of nucleotides and nucleotide derivatives
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tricyclodecan-9-yl-xanthogenate
-
i.e. D609, a specific inhibitor, significantly suppresses the (S)-3-methyl-2-phenyl-N-(1-phenylpropyl)-4-quinolinecarboxamide-induced current in type I nNOS neurons
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
no expression of NPP6 detectable in Modulla oblongata and uterus
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
(S)-3-methyl-2-phenyl-N-(1-phenylpropyl)-4-quinolinecarboxamide activates TRP-like ion channels through an phosphatidylcholine-specific phospholipase C-dependent signaling pathway, mechanism, overview
physiological function
physiological function
-
PLC activation initiates the calcium signaling system. Phospholipase C activity is necessary for methylmercury-induced interleukin-6 release. Sustained interleukin-6 exposure can be detrimental to cerebellar granule neurons, one of the major cellular targets of methylmercury cytotoxicity
physiological function
-
the enzyme is involved in the regulation of Ca2+-permeable nonselective cation channels. (S)-3-methyl-2-phenyl-N-(1-phenylpropyl)-4-quinolinecarboxamide-induced current is mediated by the enzyme in neuronal nitric oxide synthase-expressing, GFP-responsive GABAergic neurons of the visual neocortex. (S)-3-methyl-2-phenyl-N-(1-phenylpropyl)-4-quinolinecarboxamide-induced current is mediated by G proteins and suppressed by D609, an inhibitor of phosphatidylcholine-specific phospholipase C, but not by inhibitors of phosphatidylinositol-specific phospholipase C, EC 3.1.4.11, adenylate cyclase or Src tyrosine kinases
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
mNPP6-ex
truncated form of hNPP6, cDNA for the extracellular domain of mNPP6 with Myc tag at the carboxyl terminus
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mono Q ion exchange chromatography column and eluted with a linear gradient of NaCl (0-2 M) using the deltaKTA system
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dupont, G.; McGuinnes, O.M.; Johnson, M.H.; Berridge, M.J.; Borgese, F.
Phospholipase C in mouse oocytes: Characterization of beta and gamma isoforms and their possible involvement in sperm-induced Ca2+ spiking
Biochem. J.
316
583-591
1996
Mus musculus
-
Sakagami, H.; Aoki, J.; Natori, Y.; Nishikawa, K.; Kakehi, Y.; Arai, H.
Biochemical and molecular characterization of a novel choline-specific glycerophosphodiester phosphodiesterase belonging to the nucleotide pyrophosphatase/phosphodiesterase family
J. Biol. Chem.
280
23084-23093
2005
Homo sapiens (Q6UWR7), Homo sapiens, Mus musculus (Q8BGN3)
Chang, J.Y.
Methylmercury-induced IL-6 release requires phospholipase C activities
Neurosci. Lett.
496
152-156
2011
Mus musculus, Mus musculus C57BL/6
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