ENPP3 — Ectonucleotide pyrophosphatase/phosphodiesterase 3
ENPP3 belongs to a gene co-expression module in 2 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
ENPP3's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Enterocytes | Chylomicron apolipoprotein assembly Lipid metabolism | APOA1, APOA4, APOC3, ARG2, CYP3A4, FLVCR1, RMDN3, THSD4 | View in SCUBA |
| Hematopoietic progenitor cells | Mast Cell Basophil Granulocyte development | HPGD, IL1RL1, ITGB8, KRT1, NDFIP2, SLC18A2, TPSB2, TPSD1 +1 more |
About the gene
| Synonyms | B10, CD203c, gp130RB13-6, PD-IBETA, PDNP3 |
|---|---|
| Chromosome | 6: 131628442-131747418 |
| Predicted location | Intracellular, Secreted |
| Essential gene | No |
| Protein class | CD markers, Enzymes, Metabolic proteins, Predicted intracellular proteins, Predicted secreted proteins |
| Molecular function | Hydrolase |
Function
Hydrolase that metabolizes extracellular nucleotides, including ATP, GTP, UTP and CTP. Limits mast cells and basophils response during inflammation and during the chronic phases of allergic responses by eliminating extracellular ATP, a signaling molecule activating these cells in an autocrine manner. Metabolizes extracellular ATP in the lumen of the small intestine, and thereby prevents ATP-induced apoptosis of intestinal plasmacytoid dendritic cells (By similarity). Has a broad specificity and can also hydrolyze UDP-GlcNAc into UMP and GlcNAc-1-phosphate and potentially several other intracellular nucleotide sugars, including UDP-GalNAc, CMP-NeuAc, GDP-Fuc, and UDP-GlcA. Thereby, could modulate glycan biosynthesis and protein glycosylation (By similarity). Can hydrolyze extracellular dinucleoside polyphosphates, including the vasoactive adenosine polyphosphates as well. In addition, displays an alkaline phosphodiesterase activity in vitro.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.