Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A5PF10 (NEUR1_PIG)

Last modified February 9, 2010. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Sialidase-1
    EC=3.2.1.18
Alternative name(s):
    Lysosomal sialidase
    N-acetyl-alpha-neuraminidase 1
    Acetylneuraminyl hydrolase
Gene names
Name: NEU1
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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 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 By similarity.

Domain

A C-terminal internalization signal (YGTL) appears to allow the targeting of plasma membrane proteins to endosomes By similarity.

Post-translational modification

N-glycosylated By similarity.

Phosphorylation of tyrosine within the internalization signal results in inhibition of sialidase internalization and blockage on the plasma membrane By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 33 family.

Contains 4 BNR repeats.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4848 By similarity
Chain49 – 416368Sialidase-1
PRO_0000304727

Regions

Repeat113 – 12412BNR 1
Repeat173 – 18412BNR 2
Repeat232 – 24312BNR 3
Repeat348 – 35912BNR 4
Motif78 – 814FRIP motif
Motif413 – 4164Internalization signal

Sites

Active site1041Proton acceptor By similarity
Active site3711Nucleophile By similarity
Active site3951 Potential
Binding site791Substrate By similarity
Binding site2811Substrate By similarity
Binding site3421Substrate By similarity

Amino acid modifications

Modified residue2431Phosphotyrosine By similarity
Modified residue2451Phosphoserine By similarity
Modified residue2521Phosphotyrosine By similarity
Glycosylation1871N-linked (GlcNAc...) Potential
Glycosylation3441N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
A5PF10-1 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 65E99172C69F3EB8

FASTA41645,159
        10         20         30         40         50         60 
MTAERPGAVP LGRPGRPPML GLGEAYRAQV FASIFLLLLS PAGVGARAKN DFNLVHPLVT 

        70         80         90        100        110        120 
MEQLLWVSGK QIGSVDTFRI PLITTTPRGT LLAFAEARKM SASDKGAKFI ALRRSMDQGS 

       130        140        150        160        170        180 
TWSPTAFIVD DGETPDGLNL GAVVSDTTTG VVFLFYSLCA HKAGCRVAST MLVWSKDDGI 

       190        200        210        220        230        240 
SWSSPRNLSL DIGTEMFAPG PGSGIQKQWA PQKGRLIVCG HGTLERDGVF CLLSDDHGAS 

       250        260        270        280        290        300 
WRYGSGISGI PYGQPKREND FNPDECQPYE LPDGSVVINA RNQNNYHCRC RIVLRSYDAC 

       310        320        330        340        350        360 
DTLRPRDVTF DPELVDPVVA AGAVATSSGI IFFSNPAHPE FRVNLTLRWS FSNGTSWRKE 

       370        380        390        400        410 
TVQIWPGPSG YSSLATLEGS VGGEDQAPQL YVLYEKGRNR YTESISLAKV SVYGTL 

« Hide

References

[1]Porcine genome sequencing project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Duroc.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL773527 Genomic DNA. Translation: CAN87707.1.
RefSeqNP_001095292.1.
UniGeneSsc.51944

3D structure databases

SMRA5PF10. Positions 35-410, 75-412.
ModBaseSearch...

Genome annotation databases

EnsemblENSSSCT00000001555; ENSSSCP00000001513; ENSSSCG00000001418; Sus scrofa. [Genome view]
GeneID100124381.
KEGGssc:100124381.

Organism-specific databases

CTD100124381.

Phylogenomic databases

OrthoDBEOG96X1TS.

Enzyme and pathway databases

BRENDA3.2.1.18. 249.

Family and domain databases

InterProIPR011040. Neuraminidase.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNEUR1_PIG
AccessionPrimary (citable) accession number: A5PF10
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 10, 2007
Last modified: February 9, 2010
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents