Sialidase-2

Sialidase-2 is an enzyme that in humans is encoded by the NEU2 gene.^[5][6][7]

NEU2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1SNT, 1SO7, 1VCU, 2F0Z, 2F10, 2F11, 2F12, 2F13, 2F24, 2F25, 2F26, 2F27, 2F28, 2F29, 4NC5, 4NCS
Identifiers
Aliases	NEU2, SIAL2, neuraminidase 2 (cytosolic sialidase), neuraminidase 2
External IDs	OMIM: 605528; MGI: 1344417; HomoloGene: 3927; GeneCards: NEU2; OMA:NEU2 - orthologs
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2q37.1 Start 233,032,672 bp[1] End 233,035,057 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 D Start 87,437,611 bp[2] End 87,525,567 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in testicle skin of leg skin of abdomen connective tissue adipose tissue nervous system subcutaneous adipose tissue tibial nerve Top expressed in temporal muscle esophagus triceps brachii muscle right kidney sternocleidomastoid muscle respiratory epithelium olfactory epithelium vastus lateralis muscle lip muscle of thigh More reference expression data BioGPS More reference expression data
Gene ontology Molecular function exo-alpha-(2->6)-sialidase activity exo-alpha-(2->8)-sialidase activity hydrolase activity, acting on glycosyl bonds protein binding exo-alpha-(2->3)-sialidase activity hydrolase activity exo-alpha-sialidase activity Cellular component cytoplasm membrane intracellular membrane-bounded organelle cytosol catalytic complex Biological process glycosphingolipid metabolic process lipid metabolism lipid catabolic process oligosaccharide catabolic process metabolism ganglioside catabolic process cellular oligosaccharide catabolic process carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4759 23956 Ensembl ENSG00000115488 ENSMUSG00000079434 UniProt Q9Y3R4 Q9JMH3 RefSeq (mRNA) NM_005383 NM_001160163 NM_001160164 NM_001160165 NM_015750 RefSeq (protein) NP_005374 NP_001153635 NP_001153636 NP_001153637 NP_056565 Location (UCSC) Chr 2: 233.03 – 233.04 Mb Chr 1: 87.44 – 87.53 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

This gene belongs to a family of glycohydrolytic enzymes which remove sialic acid residues from glycoproteins and glycolipids. Expression studies in COS-7 cells confirmed that this gene encodes a functional sialidase. Its cytosolic localization was demonstrated by cell fractionation experiments.^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000115488 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000079434 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Monti E, Preti A, Rossi E, Ballabio A, Borsani G (Jun 1999). "Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases". Genomics. 57 (1): 137–143. doi:10.1006/geno.1999.5749. PMID 10191093.
6. Tringali C, Papini N, Fusi P, Croci G, Borsani G, Preti A, Tortora P, Tettamanti G, Venerando B, Monti E (Jan 2004). "Properties of recombinant human cytosolic sialidase HsNEU2. The enzyme hydrolyzes monomerically dispersed GM1 ganglioside molecules". J Biol Chem. 279 (5): 3169–3179. doi:10.1074/jbc.M308381200. PMID 14613940.
7. "Entrez Gene: NEU2 sialidase 2 (cytosolic sialidase)".

Further reading

• Li CY, Yu Q, Ye ZQ, Sun Y, He Q, Li XM, Zhang W, Luo J, Gu X (2007). "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 (4): 357–362. doi:10.1038/cr.2007.27. PMID 17426694.
• Chavas LM, Tringali C, Fusi P, Venerando B, Tettamanti G, Kato R, Monti E, Wakatsuki S (2005). "Crystal structure of the human cytosolic sialidase Neu2. Evidence for the dynamic nature of substrate recognition". J. Biol. Chem. 280 (1): 469–75. doi:10.1074/jbc.M411506200. PMID 15501818.
• Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–2127. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Hart ML, Saifuddin M, Uemura K, Bremer EG, Hooker B, Kawasaki T, Spear GT (2003). "High mannose glycans and sialic acid on gp120 regulate binding of mannose-binding lectin (MBL) to HIV type 1". AIDS Res. Hum. Retroviruses. 18 (17): 1311–1317. doi:10.1089/088922202320886352. PMID 12487819.
• Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Bassi MT, Sperandeo MP, Incerti B, Bulfone A, Pepe A, Surace EM, Gattuso C, De Grandi A, Buoninconti A (2000). "SLC7A8, a gene mapping within the lysinuric protein intolerance critical region, encodes a new member of the glycoprotein-associated amino acid transporter family". Genomics. 62 (2): 297–303. doi:10.1006/geno.1999.5978. PMID 10610726.
• Monti E, Preti A, Nesti C, Ballabio A, Borsani G (2000). "Expression of a novel human sialidase encoded by the NEU2 gene". Glycobiology. 9 (12): 1313–1321. doi:10.1093/glycob/9.12.1313. PMID 10561456.
• Hu H, Shioda T, Moriya C, Xin X, Hasan MK, Miyake K, Shimada T, Nagai Y (1996). "Infectivities of human and other primate lentiviruses are activated by desialylation of the virion surface". J. Virol. 70 (11): 7462–70. doi:10.1128/JVI.70.11.7462-7470.1996. PMC 190813. PMID 8892864.
• Miyagi T, Konno K, Emori Y, Kawasaki H, Suzuki K, Yasui A, Tsuik S (1994). "Molecular cloning and expression of cDNA encoding rat skeletal muscle cytosolic sialidase". J. Biol. Chem. 268 (35): 26435–40. doi:10.1016/S0021-9258(19)74333-6. PMID 8253770.

External links

• PDBe-KB provides an overview of all the structure information available in the PDB for Human Sialidase-2