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O35657 (NEUR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the removal of sialic acid (N-acetylneuraminic 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. Ref.1 Ref.2

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. Ref.1 Ref.2

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. Ref.2

Tissue specificity

Highly expressed in kidney, epididymis, followed by brain, spinal cord and weakly expressed in adrenal, heart, liver, lung and spleen. Ref.2

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141 Potential
Chain42 – 409368Sialidase-1
PRO_0000012027

Regions

Repeat106 – 11712BNR 1
Repeat166 – 17712BNR 2
Repeat225 – 23612BNR 3
Repeat341 – 35212BNR 4
Motif71 – 744FRIP motif
Motif406 – 4094Internalization signal

Sites

Active site971Proton acceptor By similarity
Active site2581 Potential
Active site3641Nucleophile By similarity
Active site3881 Potential
Binding site721Substrate By similarity
Binding site911Substrate By similarity
Binding site2581Substrate By similarity
Binding site2741Substrate By similarity
Binding site3351Substrate By similarity

Amino acid modifications

Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential
Glycosylation3461N-linked (GlcNAc...) Potential
Glycosylation3721N-linked (GlcNAc...) Potential

Natural variations

Natural variant2091L → I Reduced activity. Ref.5

Experimental info

Sequence conflict1071R → K in AAC53536. Ref.2
Sequence conflict1131S → C in AAC53536. Ref.2
Sequence conflict117 – 1215STAFI → PTGFM in AAC53536. Ref.2
Sequence conflict172 – 1732GI → AF in AAC53536. Ref.2
Sequence conflict3441F → L in AAC53536. Ref.2
Sequence conflict3511Q → L in AAH04666. Ref.4

Sequences

Sequence LengthMass (Da)Tools
O35657 [UniParc].

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

FASTA40944,591
        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' 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], CATALYTIC ACTIVITY, FUNCTION.
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], CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
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.
RefSeqNP_035023.3. NM_010893.3.
UniGeneMm.8856.

3D structure databases

ProteinModelPortalO35657.
SMRO35657. Positions 49-390.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201731. 1 interaction.

Protein family/group databases

CAZyGH33. Glycoside Hydrolase Family 33.

PTM databases

PhosphoSiteO35657.

Proteomic databases

PaxDbO35657.
PRIDEO35657.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000007253; ENSMUSP00000007253; ENSMUSG00000007038.
GeneID18010.
KEGGmmu:18010.
UCSCuc008cei.2. mouse.

Organism-specific databases

CTD4758.
MGIMGI:97305. Neu1.

Phylogenomic databases

eggNOGCOG4409.
HOGENOMHOG000007651.
HOVERGENHBG057314.
InParanoidO35657.
KOK01186.
OMAGTEMFAP.
OrthoDBEOG779NXT.
PhylomeDBO35657.
TreeFamTF331063.

Gene expression databases

ArrayExpressO35657.
BgeeO35657.
CleanExMM_NEU1.
GenevestigatorO35657.

Family and domain databases

Gene3D2.120.10.10. 1 hit.
InterProIPR026942. Sialidase-1.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
[Graphical view]
PANTHERPTHR10628. PTHR10628. 1 hit.
PTHR10628:SF9. PTHR10628:SF9. 1 hit.
SUPFAMSSF50939. SSF50939. 1 hit.
ProtoNetSearch...

Other

ChiTaRSNEU1. mouse.
NextBio293029.
PROO35657.
SOURCESearch...

Entry information

Entry nameNEUR1_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries