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Q5RAF4 (NEUR1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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·Alt products·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):
Acetylneuraminyl hydrolase
Lysosomal sialidase
N-acetyl-alpha-neuraminidase 1
Gene names
Name:NEU1
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 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 By similarity. Lysosome lumen By similarity. Cell membrane By similarity. Cytoplasmic vesicle By similarity. 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.

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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5RAF4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q5RAF4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     267-414: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4747 By similarity
Chain48 – 415368Sialidase-1
PRO_0000304728

Regions

Repeat112 – 12312BNR 1
Repeat172 – 18312BNR 2
Repeat231 – 24212BNR 3
Repeat347 – 35812BNR 4
Motif77 – 804FRIP motif
Motif412 – 4154Internalization signal

Sites

Active site1031Proton acceptor By similarity
Active site3701Nucleophile By similarity
Active site3941 Potential
Binding site781Substrate By similarity
Binding site971Substrate By similarity
Binding site2641Substrate By similarity
Binding site2801Substrate By similarity
Binding site3411Substrate By similarity

Amino acid modifications

Glycosylation1861N-linked (GlcNAc...) Potential
Glycosylation3431N-linked (GlcNAc...) Potential
Glycosylation3521N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence267 – 414148Missing in isoform 2.
VSP_028119

Experimental info

Sequence conflict51R → Q in CAH89635. Ref.1
Sequence conflict51R → Q in CAH91396. Ref.1
Sequence conflict121D → G in CAH89635. Ref.1
Sequence conflict121D → G in CAH91396. Ref.1
Sequence conflict291W → R in CAH89635. Ref.1
Sequence conflict291W → R in CAH91396. Ref.1
Sequence conflict571L → P in CAH91396. Ref.1
Sequence conflict2561Q → H in CAH89635. Ref.1
Sequence conflict2561Q → H in CAH91396. Ref.1
Sequence conflict3441L → P in CAH89635. Ref.1
Sequence conflict4061V → M in CAH89635. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 360E60A256DEA07F

FASTA41545,467
        10         20         30         40         50         60 
MTGERPSTAL PDRRWGPRIL GFWGGCRVWV FAAIFLLLSL AASWSKAEND FGLVQPLVTM 

        70         80         90        100        110        120 
EQLLWVSGRQ IGSVDTFRIP LITATPRGTL LAFAEARKMS SSDEGAKFIA LRRSMDQGST 

       130        140        150        160        170        180 
WSPTAFIVND GDVPDGLNLG AVVSDVETGV VFLFYSLCAH KAGCQVASTM LVWSKDDGVS 

       190        200        210        220        230        240 
WSTPRNLSLD IGTEVFAPGP GSGIQKQREP RKGRLIVCGH GTLERDGVFC LLSDDHGASW 

       250        260        270        280        290        300 
RYGSGVSGIP YGQPKQENDF NPDECQPYEL PDGSVVINAR NQNNYHCHCR IVLRSYDACD 

       310        320        330        340        350        360 
TLRPRDVTFD PELVDPVVAA GAVVTSSGIV FFSNPAHPEF RVNLTLRWSF SNGTSWRKET 

       370        380        390        400        410 
VQLWPGPSGY SSLATLEGSM DGEEQAPQLY VLYEKGRNHY TESISVAKIS VYGTL 

« Hide

Isoform 2 [UniParc].

Checksum: FFE761254DE87C3A
Show »

FASTA26729,000

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain cortex, Heart and Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR857339 mRNA. Translation: CAH89635.1.
CR859063 mRNA. Translation: CAH91256.1.
CR859212 mRNA. Translation: CAH91396.1.
RefSeqNP_001125743.1. NM_001132271.1.
NP_001128939.1. NM_001135467.1.

3D structure databases

ProteinModelPortalQ5RAF4.
SMRQ5RAF4. Positions 55-396.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ5RAF4.

Protein family/group databases

CAZyGH33. Glycoside Hydrolase Family 33.

Proteomic databases

PRIDEQ5RAF4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100172668.
KEGGpon:100172668.

Organism-specific databases

CTD4758.

Phylogenomic databases

HOVERGENHBG057314.
InParanoidQ5RAF4.
KOK01186.

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...

Entry information

Entry nameNEUR1_PONAB
AccessionPrimary (citable) accession number: Q5RAF4
Secondary accession number(s): Q5RA14, Q5RF22
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: December 21, 2004
Last modified: February 19, 2014
This is version 63 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