Sialidase-3

NEU3

Identifiers

NEU3, SIAL3, neuraminidase 3 (membrane sialidase), neuraminidase 3, membrane sialidase, neuraminidase 3

External IDs

OMIM: 604617 MGI: 1355305 HomoloGene: 4847 GeneCards: NEU3

Gene location (Human)

Chr.	Chromosome 11 (human)^[1]

Band	11q13.4	Start	74,988,134 bp^[1]
Band	11q13.4	End	75,018,893 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 7 (mouse)^[2]

Band	7\|7 E1	Start	99,460,646 bp^[2]
Band	7\|7 E1	End	99,477,624 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

gastrocnemius muscle

right adrenal gland

sural nerve

biceps brachii

monocyte

tibialis anterior muscle

right lobe of liver

deltoid muscle

endothelial cell

body of pancreas

Top expressed in

cumulus cell

thymus

left lung lobe

ectoderm

saccule

otic placode

soleus muscle

ovary

knee joint

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

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Sialidase-3 is an enzyme that in humans is encoded by the NEU3 gene.^[5]^[6]

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.^[6]

Interactions

Sialidase-3 has been shown to interact with Grb2.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000162139 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000035239 - Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Wada T, Yoshikawa Y, Tokuyama S, Kuwabara M, Akita H, Miyagi T (Aug 1999). "Cloning, expression, and chromosomal mapping of a human ganglioside sialidase". Biochem Biophys Res Commun. 261 (1): 21–7. doi:10.1006/bbrc.1999.0973. PMID 10405317.
^ ^a ^b "Entrez Gene: NEU3 sialidase 3 (membrane sialidase)".
^ Sasaki A, Hata K, Suzuki S, Sawada M, Wada T, Yamaguchi K, Obinata M, Tateno H, Suzuki H, Miyagi T (Jul 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.

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.

Hydrolase: sugar hydrolases (EC 3.2)

3.2.1: Glycoside hydrolases

Disaccharidase	Sucrase/Sucrase-isomaltase/Invertase Maltase Trehalase Lactase
Glucosidases	Cellulase Alpha-glucosidase Acid Neutral AB Neutral C Beta-glucosidase cytosolic Debranching enzyme
Other	Amylase Alpha-amylase Chitinase Lysozyme Neuraminidase NEU1 NEU2 NEU3 NEU4 Bacterial neuraminidase Viral neuraminidase Galactosidases Alpha Beta alpha-Mannosidase Glucuronidase Klotho Hyaluronidase Pullulanase Glucosylceramidase lysosomal non-lysosomal Galactosylceramidase Alpha-N-acetylgalactosaminidase NAGA Alpha-N-acetylglucosaminidase Fucosidase Hexosaminidase HEXA HEXB Iduronidase Maltase-glucoamylase Heparanase HPSE2

3.2.2: Hydrolysing
N-Glycosyl compounds

DNA glycosylases: Oxoguanine glycosylase

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This page was last edited on 5 January 2024, at 22:20

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Function

Interactions

References

Further reading