Sialidase-3

NEU3
Identifiers
Aliases	NEU3, SIAL3, neuraminidase 3 (membrane sialidase), neuraminidase 3, membrane sialidase, neuraminidase 3
External IDs	OMIM: 604617; MGI: 1355305; HomoloGene: 4847; GeneCards: NEU3; OMA:NEU3 - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11q13.4 Start 74,988,134 bp End 75,018,893 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7|7 E1 Start 99,460,646 bp End 99,477,624 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Skeletal muscle tissue of rectus abdominis gastrocnemius muscle muscle of thigh right adrenal gland left adrenal cortex right adrenal cortex sural nerve biceps brachii Skeletal muscle tissue of biceps brachii right testis Top expressed in cumulus cell epithelium of small intestine thymus embryo muscle of thigh left lung lobe transitional epithelium of urinary bladder ectoderm otic vesicle saccule More reference expression data BioGPS More reference expression data
Gene ontology Molecular function alpha-sialidase activity exo-alpha-(2->6)-sialidase activity exo-alpha-(2->8)-sialidase activity hydrolase activity, acting on glycosyl bonds exo-alpha-(2->3)-sialidase activity hydrolase activity exo-alpha-sialidase activity Cellular component cytoplasm intracellular membrane-bounded organelle membrane plasma membrane integral component of plasma membrane Biological process glycosphingolipid metabolic process lipid metabolism lipid catabolic process oligosaccharide catabolic process metabolism ganglioside catabolic process carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10825 50877 Ensembl ENSG00000162139 ENSMUSG00000035239 UniProt Q9UQ49 Q9JMH7 RefSeq (mRNA) NM_006656 NM_016720 RefSeq (protein) NP_006647 NP_001354789 NP_001354790 NP_001354791 NP_001354792 NP_001354793 NP_001354794 NP_001354795 NP_001354796 NP_057929 Location (UCSC) Chr 11: 74.99 – 75.02 Mb Chr 7: 99.46 – 99.48 Mb PubMed search
Wikidata
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Sialidase-3 is an enzyme that in humans is encoded by the NEU3 gene.

Function

This gene product belongs to a family of glycohydrolytic enzymes which remove sialic acid residues from glycoproteins and glycolipids. It is localized in the plasma membrane, and its activity is specific for gangliosides. It may play a role in modulating the ganglioside content of the lipid bilayer.

Interactions

Sialidase-3 has been shown to interact with Grb2.

Further reading

• 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.
• Monti E, Bassi MT, Papini N, Riboni M, Manzoni M, Venerando B, Croci G, Preti A, Ballabio A, Tettamanti G, Borsani G (2001). "Identification and expression of NEU3, a novel human sialidase associated to the plasma membrane". Biochem. J. 349 (Pt 1): 343–51. doi:10.1042/0264-6021:3490343. PMC 1221155. PMID 10861246.
• Wang Y, Yamaguchi K, Wada T, Hata K, Zhao X, Fujimoto T, Miyagi T (2002). "A close association of the ganglioside-specific sialidase Neu3 with caveolin in membrane microdomains". J. Biol. Chem. 277 (29): 26252–9. doi:10.1074/jbc.M110515200. PMID 12011038.
• Kakugawa Y, Wada T, Yamaguchi K, Yamanami H, Ouchi K, Sato I, Miyagi T (2002). "Up-regulation of plasma membrane-associated ganglioside sialidase (Neu3) in human colon cancer and its involvement in apoptosis suppression". Proc. Natl. Acad. Sci. U.S.A. 99 (16): 10718–23. Bibcode:2002PNAS...9910718K. doi:10.1073/pnas.152597199. PMC 125023. PMID 12149448.
• 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): 1311–7. doi:10.1089/088922202320886352. PMID 12487819.
• Oehler C, Kopitz J, Cantz M (2003). "Substrate specificity and inhibitor studies of a membrane-bound ganglioside sialidase isolated from human brain tissue". Biol. Chem. 383 (11): 1735–42. doi:10.1515/BC.2002.194. PMID 12530538. S2CID 44415771.
• Sasaki A, Hata K, Suzuki S, Sawada M, Wada T, Yamaguchi K, Obinata M, Tateno H, Suzuki H, Miyagi T (2003). "Overexpression of plasma membrane-associated sialidase attenuates insulin signaling in transgenic mice". J. Biol. Chem. 278 (30): 27896–902. doi:10.1074/jbc.M212200200. PMID 12730204.
• Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. S2CID 27764390.
• Ha KT, Lee YC, Cho SH, Kim JK, Kim CH (2004). "Molecular characterization of membrane type and ganglioside-specific sialidase (Neu3) expressed in E. coli". Mol. Cells. 17 (2): 267–73. doi:10.1016/S1016-8478(23)13037-8. PMID 15179041.
• Stamatos NM, Liang F, Nan X, Landry K, Cross AS, Wang LX, Pshezhetsky AV (2005). "Differential expression of endogenous sialidases of human monocytes during cellular differentiation into macrophages". FEBS J. 272 (10): 2545–56. doi:10.1111/j.1742-4658.2005.04679.x. PMID 15885103. S2CID 27379898.
• Kato K, Shiga K, Yamaguchi K, Hata K, Kobayashi T, Miyazaki K, Saijo S, Miyagi T (2006). "Plasma-membrane-associated sialidase (NEU3) differentially regulates integrin-mediated cell proliferation through laminin- and fibronectin-derived signalling". Biochem. J. 394 (Pt 3): 647–56. doi:10.1042/BJ20050737. PMC 1383714. PMID 16241905.
• Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Ueno S, Saito S, Wada T, Yamaguchi K, Satoh M, Arai Y, Miyagi T (2006). "Plasma membrane-associated sialidase is up-regulated in renal cell carcinoma and promotes interleukin-6-induced apoptosis suppression and cell motility". J. Biol. Chem. 281 (12): 7756–64. doi:10.1074/jbc.M509668200. PMID 16428383.
• Yamaguchi K, Hata K, Wada T, Moriya S, Miyagi T (2006). "Epidermal growth factor-induced mobilization of a ganglioside-specific sialidase (NEU3) to membrane ruffles". Biochem. Biophys. Res. Commun. 346 (2): 484–90. doi:10.1016/j.bbrc.2006.05.136. PMID 16765317.
• Nan X, Carubelli I, Stamatos NM (2007). "Sialidase expression in activated human T lymphocytes influences production of IFN-gamma". J. Leukoc. Biol. 81 (1): 284–96. CiteSeerX 10.1.1.492.9566. doi:10.1189/jlb.1105692. PMID 17028199. S2CID 36852644.
• Yoshizumi S, Suzuki S, Hirai M, Hinokio Y, Yamada T, Yamada T, Tsunoda U, Aburatani H, Yamaguchi K, Miyagi T, Oka Y (2007). "Increased hepatic expression of ganglioside-specific sialidase, NEU3, improves insulin sensitivity and glucose tolerance in mice". Metab. Clin. Exp. 56 (3): 420–9. doi:10.1016/j.metabol.2006.10.027. PMID 17292733.
• Wada T, Hata K, Yamaguchi K, Shiozaki K, Koseki K, Moriya S, Miyagi T (2007). "A crucial role of plasma membrane-associated sialidase in the survival of human cancer cells". Oncogene. 26 (17): 2483–90. doi:10.1038/sj.onc.1210341. PMID 17334392. S2CID 6962747.
• Azuma Y, Sato H, Higai K, Matsumoto K (2007). "Enhanced expression of membrane-associated sialidase Neu3 decreases GD3 and increases GM3 on the surface of Jurkat cells during etoposide-induced apoptosis". Biol. Pharm. Bull. 30 (9): 1680–4. doi:10.1248/bpb.30.1680. PMID 17827720.