CD203c; ectonucleotide pyrophosphatase/phosphodiesterase family member 3; E-NPP 3; phosphodiesterase I beta; PD-Ibeta; phosphodiesterase I/nucleotide pyrophosphatase 3; includes: alkaline phosphodiesterase I; nucleotide pyrophosphatase (ENPP3, PDNP3, NPPase)

Function: - cleaves a variety of phosphodiester & phosphosulfate bonds including deoxynucleotides, nucleotide sugars, & NAD - hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides - at low concentrations of ATP, a phosphorylated active site intermediate is formed which inhibits further ATP hydrolysis - the active SMB domain may be permitted disulfide bond heterogeneity - 2 alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both Cofactor: - binds 2 divalent metal cations per subunit (probable) Structure: - N-glycosylation is necessary for correct trafficking to the apical surface, but is not the apical targeting signal - belongs to the nucleotide - pyrophosphatase/phosphodiesterase family - contains 2 SMB (somatomedin-B) domains Compartment: - membrane; single-pass type 2 membrane protein (putative) - secreted - located at the apical surface in intestinal & kidney epithelial cells - located at the cell surface of basophils, & at the apical plasma membrane of bile duct cells - secreted into plasma, & into lumen lined by epithelial cells Expression: - expressed in bile ducts, prostate, uterus & colon - expressed on basophils, mast cells & their progenitors - up-regulated by stimulation by allergen or by cross-linking with IgE - IgE-mediated activation is enhanced by tetradecanoyl phorbol acetate, a stimulator of the PKC pathway, & inhibited by the P13 kinase inhibitors, LY294002 & wortmannin Pathology: - up-regulated in invasive bile duct cancers

General

cluster-of-differentiation antigen; cluster designation antigen; CD antigen glycoprotein membrane protein phosphodiesterase I/nucleotide pyrophosphatase or ectonucleotide pyrophosphatase/phosphodiesterase

Properties

SIZE: entity length = 875 aa MW = 100 kD COMPARTMENT: cellular membrane MOTIF: transmembrane domain {12-30} SMB 1 {50-93} MOTIF: cysteine residue {C54} MODIFICATION: cysteine residue {C71} cysteine residue {C54} MODIFICATION: cysteine residue {C58} cysteine residue {C58} MODIFICATION: cysteine residue {C54} cysteine residue {C58} MODIFICATION: cysteine residue {C89} cysteine residue {C69} MODIFICATION: cysteine residue {C82} cysteine residue {C69} MODIFICATION: cysteine residue {C71} cysteine residue {C71} MODIFICATION: cysteine residue {C54} cysteine residue {C71} MODIFICATION: cysteine residue {C69} cysteine residue {C75} MODIFICATION: cysteine residue {C81} Cell attachment site {78-80} cysteine residue {C81} MODIFICATION: cysteine residue {C75} cysteine residue {C82} MODIFICATION: cysteine residue {C69} cysteine residue {C82} MODIFICATION: cysteine residue {C89} cysteine residue {C89} MODIFICATION: cysteine residue {C58} cysteine residue {C89} MODIFICATION: cysteine residue {C82} SMB 2 {94-138} MOTIF: cysteine residue {C98} MODIFICATION: cysteine residue {C115} cysteine residue {C98} MODIFICATION: cysteine residue {C103} cysteine residue {C103} MODIFICATION: cysteine residue {C98} cysteine residue {C103} MODIFICATION: cysteine residue {C133} cysteine residue {C113} MODIFICATION: cysteine residue {C126} cysteine residue {C113} MODIFICATION: cysteine residue {C115} cysteine residue {C115} MODIFICATION: cysteine residue {C98} cysteine residue {C115} MODIFICATION: cysteine residue {C113} cysteine residue {C119} MODIFICATION: cysteine residue {C125} cysteine residue {C125} MODIFICATION: cysteine residue {C119} cysteine residue {C126} MODIFICATION: cysteine residue {C113} cysteine residue {C126} MODIFICATION: cysteine residue {C133} cysteine residue {C133} MODIFICATION: cysteine residue {C103} cysteine residue {C133} MODIFICATION: cysteine residue {C126} Phosphodiesterase {140-510} MOTIF: threonine residue {T205} N-glycosylation site {N236} N-glycosylation site {N279} N-glycosylation site {N290} N-glycosylation site {N426} N-glycosylation site {N533} N-glycosylation site {N582} N-glycosylation site {N594} Nuclease {605-875} MOTIF: N-glycosylation site {N687} N-glycosylation site {N699} N-glycosylation site {N789}

Database Correlations

OMIM 602182 UniProt O14638 PFAM correlations Entrez Gene 5169 Kegg hsa:5169 ENZYME correlations

References

UniProt :accession O14638