Sialidase-1 precursor - Mus musculus (Mouse)

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O35657 (NEUR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 115. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Sialidase-1
EC=3.2.1.18

Alternative name(s):
G9 sialidase
Lysosomal sialidase
N-acetyl-alpha-neuraminidase 1

Gene names

Name:	Neu1
Synonyms:	Neu

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	409 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the removal of sialic acid (N-acetylneuramic acid) moities from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage By similarity.
Catalytic activity	Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Subunit structure	Interacts with cathepsin A (protective protein), beta-galactosidase and N-acetylgalactosamine-6-sulfate sulfatase in a multienzyme complex.
Subcellular location	Lysosome membrane; Peripheral membrane protein; Lumenal side. Lysosome lumen. Cell membrane. Cytoplasmic vesicle. Note: Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but also on the plasma membrane and in intracellular vesicles.
Tissue specificity	Highly expressed in kidney, epididymis, followed by brain, spinal cord and weakly expressed in adrenal, heart, liver, lung and spleen.
Domain	A C-terminal internalization signal (YGTL) appears to allow the targeting of plasma membrane proteins to endosomes.
Post-translational modification	N-glycosylated Probable. Phosphorylation of tyrosine within the internalization signal results in inhibition of sialidase internalization and blockage on the plasma membrane.
Sequence similarities	Belongs to the glycosyl hydrolase 33 family. Contains 4 BNR repeats.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasmic vesicle Lysosome Membrane
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cell junction Inferred from electronic annotation. Source: Compara cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell lysosomal lumen Inferred from electronic annotation. Source: UniProtKB-SubCell lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from direct assay Ref.5. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	exo-alpha-(2->3)-sialidase activity Inferred from electronic annotation. Source: EC exo-alpha-(2->6)-sialidase activity Inferred from electronic annotation. Source: EC exo-alpha-(2->8)-sialidase activity Inferred from electronic annotation. Source: EC exo-alpha-sialidase activity Inferred from direct assay Ref.5. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 41

Potential

Chain

42 – 409

368

Sialidase-1

PRO_0000012027

Regions

Repeat

106 – 117

BNR 1

Repeat

166 – 177

BNR 2

Repeat

225 – 236

BNR 3

Repeat

341 – 352

BNR 4

Motif

71 – 74

FRIP motif

Motif

406 – 409

Internalization signal

Sites

Active site

Proton acceptor By similarity

Active site

258

Potential

Active site

364

Nucleophile By similarity

Binding site

Substrate By similarity

Binding site

274

Substrate By similarity

Binding site

335

Substrate By similarity

Amino acid modifications

Glycosylation

180

N-linked (GlcNAc...) Potential

Glycosylation

337

N-linked (GlcNAc...) Potential

Glycosylation

346

N-linked (GlcNAc...) Potential

Glycosylation

372

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

209

L → I Reduced activity. Ref.5

Experimental info

Sequence conflict

107

R → K in AAC53536. Ref.2

Sequence conflict

113

S → C in AAC53536. Ref.2

Sequence conflict

117 – 121

STAFI → PTGFM in AAC53536. Ref.2

Sequence conflict

172 – 173

GI → AF in AAC53536. Ref.2

Sequence conflict

344

F → L in AAC53536. Ref.2

Sequence conflict

351

Q → L in AAH04666. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

O35657 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 416BFD5BE27B8893
Show »

FASTA

409

44,591

        10         20         30         40         50         60 
MVGADPTRPR GPLSYWAGRR GQGLAAIFLL LVSAAESEAR AEDDFSLVQP LVTMEQLLWV 

        70         80         90        100        110        120 
SGKQIGSVDT FRIPLITATP RGTLLAFAEA RKKSASDEGA KFIAMRRSTD QGSTWSSTAF 

       130        140        150        160        170        180 
IVDDGEASDG LNLGAVVNDV DTGIVFLIYT LCAHKVNCQV ASTMLVWSKD DGISWSPPRN 

       190        200        210        220        230        240 
LSVDIGTEMF APGPGSGIQK QREPGKGRLI VCGHGTLERD GVFCLLSDDH GASWHYGTGV 

       250        260        270        280        290        300 
SGIPFGQPKH DHDFNPDECQ PYELPDGSVI INARNQNNYH CRCRIVLRSY DACDTLRPRD 

       310        320        330        340        350        360 
VTFDPELVDP VVAAGALATS SGIVFFSNPA HPEFRVNLTL RWSFSNGTSW QKERVQVWPG 

       370        380        390        400 
PSGYSSLTAL ENSTDGKKQP PQLFVLYEKG LNRYTESISM VKISVYGTL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a sialidase from the murine histocompatibility-2 complex: low levels of mRNA and a single amino acid mutation are responsible for reduced sialidase activity in mice carrying the Neu1a allele." Carrillo M.B., Milner C.M., Ball S.T., Snoek M., Campbell R.D. Glycobiology 7:975-986(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/RIJ.
[2]	"Cloning of the cDNA and gene encoding mouse lysosomal sialidase and correction of sialidase deficiency in human sialidosis and mouse SM/J fibroblasts." Igdoura S.A., Gafuik C., Mertineit C., Saberi F., Pshezhetsky A.V., Potier M., Trasler J.M., Gravel R.A. Hum. Mol. Genet. 7:115-121(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6.
[3]	"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse." Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L. Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 129.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"A point mutation in the neu-1 locus causes the neuraminidase defect in the SM/J mouse." Rottier R.J., Bonten E.J., d'Azzo A. Hum. Mol. Genet. 7:313-321(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ILE-209.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y11412 mRNA. Translation: CAA72215.1. U93702 mRNA. Translation: AAC53536.1. AF109906 Genomic DNA. Translation: AAC84167.1. BC004666 mRNA. Translation: AAH04666.1.
IPI	IPI00315576.
RefSeq	NP_035023.3. NM_010893.3.
UniGene	Mm.8856.
3D structure databases
ProteinModelPortal	O35657.
SMR	O35657. Positions 49-390.
ModBase	Search...
Protein family/group databases
CAZy	GH33. Glycoside Hydrolase Family 33.
PTM databases
PhosphoSite	O35657.
Proteomic databases
PaxDb	O35657.
PRIDE	O35657.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000007253; ENSMUSP00000007253; ENSMUSG00000007038.
GeneID	18010.
KEGG	mmu:18010.
UCSC	uc008cei.2. mouse.
Organism-specific databases
CTD	4758.
MGI	MGI:97305. Neu1.
Phylogenomic databases
eggNOG	COG4409.
HOGENOM	HOG000007651.
HOVERGEN	HBG057314.
InParanoid	O35657.
KO	K01186.
OMA	YEKGRNQ.
OrthoDB	EOG4DJJWX.
Gene expression databases
ArrayExpress	O35657.
Bgee	O35657.
CleanEx	MM_NEU1.
Genevestigator	O35657.
GermOnline	ENSMUSG00000007038. Mus musculus.
Family and domain databases
Gene3D	2.120.10.10. 1 hit.
InterPro	IPR026942. Sialidase-1. IPR026856. Sialidase_fam. IPR011040. Sialidases. [Graphical view]
PANTHER	PTHR10628. PTHR10628. 1 hit. PTHR10628:SF9. PTHR10628:SF9. 1 hit.
SUPFAM	SSF50939. Sialidase. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	NEU1. mouse.
NextBio	293029.
SOURCE	Search...

Entry information

Entry name

NEUR1_MOUSE

Accession

Primary (citable) accession number: O35657
Secondary accession number(s): O55220, Q99KG9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	January 1, 1998
Last modified:	May 29, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents