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Q99PW3 (NEUR1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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):
Lysosomal sialidase
N-acetyl-alpha-neuraminidase 1
Gene names
Name:Neu1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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

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

Subunit structure

Interacts with cathepsin A (protective protein), beta-galactosidase and N-acetylgalactosamine-6-sulfate sulfatase in a multienzyme complex By similarity.

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.1

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
   Biological processCarbohydrate metabolism
Lipid degradation
Lipid metabolism
   Cellular componentCell membrane
Cytoplasmic vesicle
Lysosome
Membrane
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oligosaccharide catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neuron projection development

Inferred from mutant phenotype PubMed 20347965. Source: RGD

regulation of myoblast proliferation

Inferred from mutant phenotype PubMed 20100694. Source: RGD

   Cellular_componentcell surface

Inferred from direct assay PubMed 20347965. Source: RGD

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 PubMed 2393382. Source: RGD

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionexo-alpha-(2->3)-sialidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

exo-alpha-(2->6)-sialidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

exo-alpha-(2->8)-sialidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

exo-alpha-sialidase activity

Inferred from direct assay PubMed 2393382. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3939 Potential
Chain40 – 409370Sialidase-1
PRO_0000012028

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

Sequences

Sequence LengthMass (Da)Tools
Q99PW3 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: F912FA1E1F0991A9

FASTA40944,695
        10         20         30         40         50         60 
MVGAEPSRPP GPPSYWTGRR GQGLAAIFLL LVSAAGSEAR TEDDFSLVQP LVTMEQLLWV 

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

       130        140        150        160        170        180 
IVDDGEASDG LNLGAVVNDV DTGVVFLIYT LCAHKVNCQV ASTMLVWSKD DGVSWSPPRN 

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

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

       310        320        330        340        350        360 
VTFDPELVDP VVAAGALATS SGIVFFSNPA HPEYRVNLTL RWSFSNGTFW QKERVQLWPG 

       370        380        390        400 
PSGYSSLTAL ENSTDGKKQP PQLFVLYEKG LNRYTESISM VKISVYGTL 

« Hide

References

[1]"Differential expression of three sialidase genes in rat development."
Hasegawa T., Feijoo Carnero C., Wada T., Itoyama Y., Miyagi T.
Biochem. Biophys. Res. Commun. 280:726-732(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
Strain: Sprague-Dawley.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB035722 mRNA. Translation: BAB21443.1.
UniGeneRn.128560.

3D structure databases

ProteinModelPortalQ99PW3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ99PW3. 1 interaction.

Protein family/group databases

CAZyGH33. Glycoside Hydrolase Family 33.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:3163. rat.

Organism-specific databases

RGD3163. Neu1.

Phylogenomic databases

HOVERGENHBG057314.
PhylomeDBQ99PW3.

Gene expression databases

GenevestigatorQ99PW3.

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

PROQ99PW3.

Entry information

Entry nameNEUR1_RAT
AccessionPrimary (citable) accession number: Q99PW3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 93 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries