Sialidase 2, Cytosolic (SIAL2)

MEU2; N-Acetyl-Alpha-Neuraminidase 2; Cytosolic sialidase

SPN	S501
HGNC	7759
MGI	1344417
RGD	3164
UniProt	Q9Y3R4
Wiki	NEU2

SIAL2 belongs to a family of glycohydrolytic enzymes which remove sialic acid residues from glycoproteins and glycolipids. Expression studies in COS7 cells confirmed that this gene encodes a functional sialidase. Its cytosolic localization was demonstrated by cell fractionation experiments. The 2 putative exons of NEU2 encode a deduced 380-amino acid protein with a calculated molecular mass of 42.23 kD. The NEU2 protein has significant homology with the mammalian, viral, and bacterial sialidases. It shares over 72% similarity with the hamster and rat cytosolic sialidases and over 42% similarity with human NEU1. NEU2 contains a potential N-linked glycosylation site, 2 aspartic acid block consensus sequences, and an N-terminal F/YRIP sequence motif which is part of the active site of other sialidase enzymes.

Reference

"Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases."
Genomics 57:137-143(1999) [PubMed] [Europe PMC] [Abstract]

"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Properties of recombinant human cytosolic sialidase HsNEU2. The enzyme hydrolyzes monomerically dispersed GM1 ganglioside molecules."
J. Biol. Chem. 279:3169-3179(2004) [PubMed] [Europe PMC] [Abstract]

"Molecular insight into substrate recognition by human cytosolic sialidase NEU2."
Proteins 80:1123-1132(2012) [PubMed] [Europe PMC] [Abstract]

"Crystal structure of the human cytosolic sialidase Neu2. Evidence for the dynamic nature of substrate recognition."
J. Biol. Chem. 280:469-475(2005) [PubMed] [Europe PMC] [Abstract]

"Tuning mechanism-based inactivators of neuraminidases: mechanistic and structural insights."
Submitted (NOV-2013) to the PDB data bank

"A nonsynonymous SNP in human cytosolic sialidase in a small Asian population results in reduced enzyme activity: potential link with severe adverse reactions to oseltamivir."
Cell Res. 17:357-362(2007) [PubMed] [Europe PMC] [Abstract]