NEU3
Function
Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan moiety in the catabolism of glycolipids, glycoproteins and oligosacharides. Displays high catalytic efficiency for gangliosides including alpha-(2->3)-sialylated GD1a and GM3 and alpha-(2->8)-sialylated GD3 (PubMed:10405317, PubMed:10861246, PubMed:11298736, PubMed:12011038, PubMed:15847605, PubMed:20511247, PubMed:28646141). Plays a role in the regulation of transmembrane signaling through the modulation of ganglioside content of the lipid bilayer and by direct interaction with signaling receptors, such as EGFR (PubMed:17334392, PubMed:25922362). Desialylates EGFR and activates downstream signaling in proliferating cells (PubMed:25922362). Contributes to clathrin-mediated endocytosis by regulating sorting of endocytosed receptors to early and recycling endosomes (PubMed:26251452).
Post-translational modifications
Palmitoylated; may regulate intracellular trafficking and anchorage to plasma membrane and endomembranes.
Sequence Similarities
Belongs to the glycosyl hydrolase 33 family.
Tissue Specificity
Highly expressed in skeletal muscle, testis, adrenal gland and thymus, followed by pancreas, liver, heart and thymus. Weakly expressed in kidney, placenta, brain and lung.
Cellular localization
- Cell membrane
- Peripheral membrane protein
- Membrane
- Caveola
- Early endosome membrane
- Peripheral membrane protein
- Recycling endosome membrane
- Peripheral membrane protein
- Lysosome membrane
- Peripheral membrane protein
- Associates with the external leaflet of the plasma membrane (By similarity). S-acylated NEU3 likely spans the lipid bilayer with a portion of C-terminus exposed to the cytosol and the catalytic region facing the extracellular space (PubMed:28646141).
Alternative names
Sialidase-3, Ganglioside sialidasedis, Membrane sialidase, N-acetyl-alpha-neuraminidase 3, NEU3