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Information on EC 3.6.1.6 - nucleoside diphosphate phosphatase and Organism(s) Mus musculus and UniProt Accession Q8VCF1
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3.6.1.6 nucleoside diphosphate phosphataseIUBMB Comments
The enzyme, which appears to be limited to metazoa, acts on multiple nucleoside diphosphates as well as on D-ribose 5-diphosphate. Specificity depends on species and isoform.
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Word Map
- 3.6.1.6
- thiamine
- apparatus
-
cytochemical
-
cisternae
- microglial
-
cytochemistry
-
saccule
- 5'-nucleotidase
- glucose-6-phosphatase
- ectonucleotidases
-
purinergic
-
osmium
- nadpase
-
monophosphatase
-
ramify
-
tetroxide
-
ectonucleoside
-
histoenzymatic
-
ultracytochemical
-
cmpase
-
postfix
-
dictyosome
- g-6-pase
- analysis
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
tppase, nucleoside diphosphatase, ndpase, inosine diphosphatase, idpase, ntpdase5, ntpdase6, nucleoside triphosphate diphosphohydrolase-1, e-ntpdase1, sa1684, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine diphosphatase
-
-
-
-
adenosinepyrophosphatase
-
-
-
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ADPase
-
-
-
-
CDPase
-
-
-
-
ER-UDPase
-
-
-
-
GDPase
-
-
-
-
guanosine 5'-diphosphatase
-
-
-
-
guanosine diphosphatase
-
-
-
-
IDPase
-
-
-
-
inosine 5'-diphosphatase
-
-
-
-
inosine diphosphatase
-
-
-
-
Lysosomal apyrase-like protein of 70 kDa
-
-
-
-
NDPase
-
-
-
-
NTPDase4
-
-
-
-
NTPDase5
-
-
-
-
NTPDase6
nucleoside 5'-diphosphatase
-
-
-
-
Nucleoside diphosphatase
-
-
-
-
nucleoside diphosphate phosphatase
-
-
-
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nucleoside diphosphate phosphohydrolase
-
-
-
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Proto-oncogene cph
-
-
-
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thiaminpyrophosphatase
-
-
-
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TPPase
-
-
-
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type B nucleoside diphosphatase
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-
-
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type L nucleoside diphosphatase
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-
-
-
additional information
-
the enzyme belongs to the ectonucleoside triphosphate diphosphohydrolase, E-NTPDase, family
NTPDase6
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
nucleoside-diphosphate phosphohydrolase
The enzyme, which appears to be limited to metazoa, acts on multiple nucleoside diphosphates as well as on D-ribose 5-diphosphate. Specificity depends on species and isoform.
CAS REGISTRY NUMBER
COMMENTARY
9027-69-4
-
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
additional information
?
-
-
NTPDase1 hydrolyzes ATP and ADP at a similar rate
-
-
?
additional information
?
-
-
the enzyme specifically binds to P2Y1 and P2Y2 receptors
-
-
?
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
additional information
?
-
-
the enzyme specifically binds to P2Y1 and P2Y2 receptors
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
oviductal and uterine, endothelium, NTPDase1 is located especially in the lamina propria mucosae and uterine blood vessel endothelium
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while all cell layers of the esophagus express NTPDase3, NTPDase3 localization in the forestomach is limited to the basal cell layer
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NTPDase3 in cells from the stratified esophageal and forestomach epithelia, and in some enteroendocrine cells of the gastric antrum. NTPDase3 and -2 are coexpressed within the myenteric and submucosal plexuses, as well as in the nerve terminals of the smooth muscle layer and mucosa
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parenchyma, NTPDase1 and NTPDase2, the latter in association with connective tissue. NTPDase3 is located in the apical pole of the epithelial cells lining the lumen of the secretory portion of the prostate gland
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NTPDase3 in epithelial cells in serous acini of salivary glands and mucous acini and duct cells of sublingual salivary glands
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of tunica muscularis and blood vessels of the muscular layer of oviductal serosa, NTPDase1
additional information
additional information
-
specific localization of NTPDase3 in the digestive system, by semiquantitative RT-PCR, immunohistochemistry, and in situ activity assay, detailed overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
enzyme knock-out mice recapitulate the desbuquois dysplasia type 1 phenotype
physiological function
the enzyme is critical for glycosaminoglycan biosynthesis in cartilage and endochondral ossification
malfunction
physiological function
additional information
-
uracil nucleotides induce a strong contractile response in Entpd1-/- denuded aortic rings, ATP and ADP do not display constrictor effect at concentrations below 0.03 mM
malfunction
-
macrophages isolated from NTPDase1-null mice are devoid of all ADPase and most ATPase activities when compared with wild type macrophages. NTPDase1-null macrophages exposed to millimolar concentrations of ATP are more susceptible to cell death, release more interleukin-1beta and interleukin-18 after TLR2 or TLR4 priming, and incorporate the fluorescent dye Yo-Pro-1 more efficiently (suggestive of increased pore formation) than wild type cells
malfunction
-
nucleotide hydrolysis is impaired in the wall of Entpd1-/- vessels compared with Entpd1+/+ aortas, which display significant ADPase and ATPase activity
malfunction
-
the mean glial Ca2+ response to ATP was significantly larger in the presence of an NTPDase inhibitor
physiological function
-
NTPDase1 is the dominant ectonucleotidase responsible for the hydrolysis of ATP and ADP at the surface of mouse primary macrophages. NTPDase1 regulates P2X7-dependent responses in peritoneal macrophages
physiological function
-
functional roles of NTPDase3 in association with NTPDase2 and ecto-5'-nucleotidase, in epithelial functions such as secretion and in enteric neurotransmission
physiological function
-
NTPDase1 controls endothelial P2Y receptor-dependent relaxation, regulating both agonist level and P2 receptor reactivity. NTPDase1 differentially influences UTP and ATP responses in vivo
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). CANT1_MOUSE
403
0
45653
Swiss-Prot
other Location (Reliability: 4)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
NTPDase activities are increased in Entpd1-deficient mice
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Martin-Satue, M.; Lavoie, E.G.; Pelletier, J.; Fausther, M.; Csizmadia, E.; Guckelberger, O.; Robson, S.C.; Sevigny, J.
Localization of plasma membrane bound NTPDases in the murine reproductive tract
Histochem. Cell Biol.
131
615-628
2009
Mus musculus, Mus musculus C57BL/6, Rattus norvegicus
Levesque, S.A.; Kukulski, F.; Enjyoji, K.; Robson, S.C.; Sevigny, J.
NTPDase1 governs P2X7-dependent functions in murine macrophages
Eur. J. Immunol.
40
1473-1485
2010
Mus musculus
Lavoie, E.G.; Gulbransen, B.D.; Martin-Satue, M.; Aliagas, E.; Sharkey, K.A.; Sevigny, J.
Ectonucleotidases in the digestive system: focus on NTPDase3 localization
Am. J. Physiol. Gastrointest. Liver Physiol.
300
G608-G620
2011
Mus musculus, Mus musculus C57BL/6
Kauffenstein, G.; Fuerstenau, C.R.; DOrleans-Juste, P.; Sevigny, J.
The ecto-nucleotidase NTPDase1 differentially regulates P2Y1 and P2Y2 receptor-dependent vasorelaxation
Br. J. Pharmacol.
159
576-585
2010
Mus musculus, Mus musculus 129 SVJ x C57 BL/6
Paganini, C.; Monti, L.; Costantini, R.; Besio, R.; Lecci, S.; Biggiogera, M.; Tian, K.; Schwartz, J.M.; Huber, C.; Cormier-Daire, V.; Gibson, B.G.; Pirog, K.A.; Forlino, A.; Rossi, A.
Calcium activated nucleotidase 1 (CANT1) is critical for glycosaminoglycan biosynthesis in cartilage and endochondral ossification
Matrix Biol.
81
70-90
2018
Mus musculus (Q8VCF1)
EXTERNAL LINKS (specific for EC-Number 3.6.1.6)
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