Sialidase-1

NEU1

Identifiers

NEU1, NANH, NEU, SIAL1, neuraminidase 1 (lysosomal sialidase), neuraminidase 1

External IDs

OMIM: 608272 MGI: 97305 HomoloGene: 375 GeneCards: NEU1

Gene location (Human)

Chr.	Chromosome 6 (human)^[1]

Band	6p21.33	Start	31,857,659 bp^[1]
Band	6p21.33	End	31,862,905 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 17 (mouse)^[2]

Band	17 B1\|17 18.48 cM	Start	35,150,229 bp^[2]
Band	17 B1\|17 18.48 cM	End	35,154,929 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

islet of Langerhans

bone marrow cells

left adrenal gland

placenta

gallbladder

kidney

duodenum

renal cortex

stromal cell of endometrium

pituitary gland

Top expressed in

kidney

proximal tubule

ileum

seminal vesicula

yolk sac

gallbladder

left colon

epithelium of stomach

cingulate gyrus

superior frontal gyrus

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	exo-alpha-(2->3)-sialidase activity exo-alpha-(2->8)-sialidase activity exo-alpha-(2->6)-sialidase activity hydrolase activity hydrolase activity, acting on glycosyl bonds exo-alpha-sialidase activity protein binding alpha-sialidase activity
Cellular component	cytoplasmic vesicle intracellular membrane-bounded organelle lysosomal membrane extracellular exosome lysosome plasma membrane lysosomal lumen cell junction membrane extracellular region specific granule lumen cytoplasm
Biological process	ganglioside catabolic process lipid catabolic process lipid metabolism metabolism oligosaccharide catabolic process glycosphingolipid metabolic process neutrophil degranulation carbohydrate metabolic process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


4758


18010

Ensembl

ENSG00000227129 ENSG00000184494 ENSG00000223957 ENSG00000234846 ENSG00000204386
ENSG00000234343 ENSG00000227315 ENSG00000228691


ENSMUSG00000007038

UniProt


Q99519


O35657

RefSeq (mRNA)


NM_000434


NM_010893

RefSeq (protein)


NP_000425


NP_035023

Location (UCSC)

Chr 6: 31.86 – 31.86 Mb

Chr 17: 35.15 – 35.15 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Sialidase-1, is a mammalian lysosomal neuraminidase enzyme which in humans is encoded by the NEU1 gene.^[5]^[6]

Function

The protein SIALIDASE-1 encoded by the NEU-1 gene encodes the lysosomal enzyme SIALIDASE-1, which cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. In the lysosome, this enzyme is part of a heterotrimeric complex together with beta-galactosidase and cathepsin A (the latter also referred to as 'protective protein'). Mutations in this gene can lead to sialidosis.^[5]

Clinical significance

Mutations in NEU1 leads to sialidosis, a rare lysosomal storage disease.^[7] Sialidase has also been shown to enhance recovery from spinal cord contusion injury when injected in rats.^[8]

Interactions

NEU1 has been shown to interact with Cathepsin A.^[9]

References

^ ^a ^b ^c ENSG00000184494, ENSG00000223957, ENSG00000234846, ENSG00000204386, ENSG00000234343, ENSG00000227315, ENSG00000228691 GRCh38: Ensembl release 89: ENSG00000227129, ENSG00000184494, ENSG00000223957, ENSG00000234846, ENSG00000204386, ENSG00000234343, ENSG00000227315, ENSG00000228691 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000007038 – 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.
^ ^a ^b "Entrez Gene: NEU1 sialidase 1 (lysosomal sialidase)".
^ Pshezhetsky AV, Richard C, Michaud L, Igdoura S, Wang S, Elsliger MA, Qu J, Leclerc D, Gravel R, Dallaire L, Potier M (March 1997). "Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis". Nat. Genet. 15 (3): 316–20. doi:10.1038/ng0397-316. PMID 9054950. S2CID 31588761.
^ Seyrantepe V, Poupetova H, Froissart R, Zabot MT, Maire I, Pshezhetsky AV (November 2003). "Molecular pathology of NEU1 gene in sialidosis". Hum. Mutat. 22 (5): 343–52. doi:10.1002/humu.10268. PMID 14517945. S2CID 22333886.
^ Mountney A, Zahner MR, Lorenzini I, Oudega M, Schramm LP, Schnaar RL (June 2010). "Sialidase enhances recovery from spinal cord contusion injury". PNAS. 107 (25): 11561–6. Bibcode:2010PNAS..10711561M. doi:10.1073/pnas.1006683107. PMC 2895144. PMID 20534525.
^ van der Spoel A, Bonten E, d'Azzo A (Mar 1998). "Transport of human lysosomal neuraminidase to mature lysosomes requires protective protein/cathepsin A". EMBO J. 17 (6): 1588–97. doi:10.1093/emboj/17.6.1588. PMC 1170506. PMID 9501080.

Okamura-Oho Y, Zhang S, Callahan JW (1994). "The biochemistry and clinical features of galactosialidosis". Biochim. Biophys. Acta. 1225 (3): 244–54. doi:10.1016/0925-4439(94)90002-7. PMID 8312369.
Seyrantepe V, Poupetova H, Froissart R, Zabot MT, Maire I, Pshezhetsky AV (2004). "Molecular pathology of NEU1 gene in sialidosis". Hum. Mutat. 22 (5): 343–52. doi:10.1002/humu.10268. PMID 14517945. S2CID 22333886.
Verheijen FW, Palmeri S, Galjaard H (1987). "Purification and partial characterization of lysosomal neuraminidase from human placenta". Eur. J. Biochem. 162 (1): 63–7. doi:10.1111/j.1432-1033.1987.tb10542.x. PMID 3102233.
Verheijen FW, Palmeri S, Hoogeveen AT, Galjaard H (1985). "Human placental neuraminidase. Activation, stabilization and association with beta-galactosidase and its protective protein". Eur. J. Biochem. 149 (2): 315–21. doi:10.1111/j.1432-1033.1985.tb08928.x. PMID 3922758.
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.
Pshezhetsky AV, Potier M (1996). "Association of N-acetylgalactosamine-6-sulfate sulfatase with the multienzyme lysosomal complex of beta-galactosidase, cathepsin A, and neuraminidase. Possible implication for intralysosomal catabolism of keratan sulfate". J. Biol. Chem. 271 (45): 28359–65. doi:10.1074/jbc.271.45.28359. PMID 8910459.
Bonten E, van der Spoel A, Fornerod M, Grosveld G, d'Azzo A (1997). "Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis". Genes Dev. 10 (24): 3156–69. doi:10.1101/gad.10.24.3156. PMID 8985184. * Milner CM, Smith SV, Carrillo MB, Taylor GL, Hollinshead M, Campbell RD (1997). "Identification of a sialidase encoded in the human major histocompatibility complex". J. Biol. Chem. 272 (7): 4549–58. doi:10.1074/jbc.272.7.4549. PMID 9020182.
Pshezhetsky AV, Richard C, Michaud L, Igdoura S, Wang S, Elsliger MA, Qu J, Leclerc D, Gravel R, Dallaire L, Potier M (1997). "Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis". Nat. Genet. 15 (3): 316–20. doi:10.1038/ng0397-316. PMID 9054950. S2CID 31588761.
Vinogradova MV, Michaud L, Mezentsev AV, Lukong KE, El-Alfy M, Morales CR, Potier M, Pshezhetsky AV (1998). "Molecular mechanism of lysosomal sialidase deficiency in galactosialidosis involves its rapid degradation". Biochem. J. 330 ( Pt 2) (Pt 2): 641–50. doi:10.1042/bj3300641. PMC 1219185. PMID 9480870.
van der Spoel A, Bonten E, d'Azzo A (1998). "Transport of human lysosomal neuraminidase to mature lysosomes requires protective protein/cathepsin A". EMBO J. 17 (6): 1588–97. doi:10.1093/emboj/17.6.1588. PMC 1170506. PMID 9501080.
Lukong KE, Elsliger MA, Chang Y, Richard C, Thomas G, Carey W, Tylki-Szymanska A, Czartoryska B, Buchholz T, Criado GR, Palmeri S, Pshezhetsky AV (2000). "Characterization of the sialidase molecular defects in sialidosis patients suggests the structural organization of the lysosomal multienzyme complex". Hum. Mol. Genet. 9 (7): 1075–85. doi:10.1093/hmg/9.7.1075. PMID 10767332.
Naganawa Y, Itoh K, Shimmoto M, Takiguchi K, Doi H, Nishizawa Y, Kobayashi T, Kamei S, Lukong KE, Pshezhetsky AV, Sakuraba H (2000). "Molecular and structural studies of Japanese patients with sialidosis type 1". J. Hum. Genet. 45 (4): 241–9. doi:10.1007/s100380070034. PMID 10944856.
Bonten EJ, Arts WF, Beck M, Covanis A, Donati MA, Parini R, Zammarchi E, d'Azzo A (2000). "Novel mutations in lysosomal neuraminidase identify functional domains and determine clinical severity in sialidosis". Hum. Mol. Genet. 9 (18): 2715–25. doi:10.1093/hmg/9.18.2715. PMID 11063730.
Lukong KE, Landry K, Elsliger MA, Chang Y, Lefrancois S, Morales CR, Pshezhetsky AV (2001). "Mutations in sialidosis impair sialidase binding to the lysosomal multienzyme complex". J. Biol. Chem. 276 (20): 17286–90. doi:10.1074/jbc.M100460200. PMID 11279074.
Penzel R, Uhl J, Kopitz J, Beck M, Otto HF, Cantz M (2001). "Splice donor site mutation in the lysosomal neuraminidase gene causing exon skipping and complete loss of enzyme activity in a sialidosis patient". FEBS Lett. 501 (2–3): 135–8. Bibcode:2001FEBSL.501..135P. doi:10.1016/S0014-5793(01)02645-X. PMID 11470272. S2CID 27689049. * Lukong KE, Seyrantepe V, Landry K, Trudel S, Ahmad A, Gahl WA, Lefrancois S, Morales CR, Pshezhetsky AV (2002). "Intracellular distribution of lysosomal sialidase is controlled by the internalization signal in its cytoplasmic tail". J. Biol. Chem. 276 (49): 46172–81. doi:10.1074/jbc.M104547200. PMID 11571282.
Sergi C, Penzel R, Uhl J, Zoubaa S, Dietrich H, Decker N, Rieger P, Kopitz J, Otto HF, Kiessling M, Cantz M (2001). "Prenatal diagnosis and fetal pathology in a Turkish family harboring a novel nonsense mutation in the lysosomal alpha-N-acetyl-neuraminidase (sialidase) gene". Hum. Genet. 109 (4): 421–8. doi:10.1007/s004390100592. PMID 11702224. S2CID 24374154.
Itoh K, Naganawa Y, Matsuzawa F, Aikawa S, Doi H, Sasagasako N, Yamada T, Kira J, Kobayashi T, Pshezhetsky AV, Sakuraba H (2002). "Novel missense mutations in the human lysosomal sialidase gene in sialidosis patients and prediction of structural alterations of mutant enzymes". J. Hum. Genet. 47 (1): 29–37. doi:10.1007/s10038-002-8652-7. PMID 11829139.

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

This page was last edited on 6 May 2024, at 03:35

From Wikipedia, the free encyclopedia

Function

Clinical significance

Interactions

References

Further reading