ENPP3

The protein encoded by this gene belongs to a series of ectoenzymes that are involved in hydrolysis of extracellular nucleotides. These ectoenzymes possess ATPase and ATP pyrophosphatase activities and are type II transmembrane proteins. Expression of the related rat mRNA has been found in a subset of immature glial cells and in the alimentary tract. The corresponding rat protein has been detected in the pancreas, small intestine, colon, and liver. The human mRNA is expressed in glioma cells, prostate, and uterus. Expression of the human protein has been detected in uterus, basophils, and mast cells. [provided by RefSeq]

Full Name

ectonucleotide pyrophosphatase/phosphodiesterase 3

Research Area

Hydrolase that metabolizes extracellular nucleotides, including ATP, GTP, UTP and CTP (PubMed:29717535).

Limits mast cell and basophil responses during inflammation and during the chronic phases of allergic responses by eliminating the extracellular ATP that functions as signaling molecule and activates basophils and mast cells and induces the release of inflammatory cytokines. Metabolizes extracellular ATP in the lumen of the small intestine, and thereby prevents ATP-induced apoptosis of intestinal plasmacytoid dendritic cells (By similarity).

Has also alkaline phosphodiesterase activity (PubMed:11342463).

Biological Process

ATP metabolic process Source: UniProtKB
Basophil activation involved in immune response Source: UniProtKB
Negative regulation of inflammatory response Source: UniProtKB
Negative regulation of mast cell activation involved in immune response Source: UniProtKB
Negative regulation of mast cell proliferation Source: UniProtKB
Nucleoside triphosphate catabolic process Source: BHF-UCL
Phosphate-containing compound metabolic process Source: BHF-UCL
Pyrimidine nucleotide metabolic process Source: UniProtKB

Cellular Location

Cell membrane; Apical cell membrane; Secreted. Detected at the cell surface of basophils (PubMed:11342463). Detected at the apical plasma membrane of bile duct cells (PubMed:15072822). Located to the apical surface in intestinal and kidney epithelial cells. Secreted in serum, and in lumen of epithelial cells.

Topology

Cytoplasmic: 1-11
Helical: 12-30
Extracellular: 31-875

PTM

N-glycosylated. N-glycosylation is necessary for normal transport to the cell membrane, but is not the apical targeting signal.