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NEU1

Domain

A C-terminal internalization signal (YGTL) appears to allow the targeting of plasma membrane proteins to endosomes.

Function

Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage.

Involvement in disease

Sialidosis

SIALIDOSIS

Lysosomal storage disease occurring as two types with various manifestations. Type 1 sialidosis (cherry red spot-myoclonus syndrome or normosomatic type) is late-onset and it is characterized by the formation of cherry red macular spots in childhood, progressive debilitating myoclonus, insiduous visual loss and rarely ataxia. The diagnosis can be confirmed by the screening of the urine for sialyloligosaccharides. Type 2 sialidosis (also known as dysmorphic type) occurs as several variants of increasing severity with earlier age of onset. It is characterized by the presence of abnormal somatic features including coarse facies and dysostosis multiplex, vertebral deformities, intellectual disability, cherry-red spot/myoclonus, sialuria, cytoplasmic vacuolation of peripheral lymphocytes, bone marrow cells and conjunctival epithelial cells.

None

The disease is caused by variants affecting the gene represented in this entry.

Post-translational modifications

N-glycosylated.

Phosphorylation of tyrosine within the internalization signal results in inhibition of sialidase internalization and blockage on the plasma membrane.

Sequence Similarities

Belongs to the glycosyl hydrolase 33 family.

Tissue Specificity

Highly expressed in pancreas, followed by skeletal muscle, kidney, placenta, heart, lung and liver. Weakly expressed in brain.

Cellular localization

Alternative names

NANH, NEU1, Sialidase-1, Acetylneuraminyl hydrolase, G9 sialidase, Lysosomal sialidase, N-acetyl-alpha-neuraminidase 1

swissprot:Q99519 omim:608272 entrezGene:4758