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Q64393 (NEUR2_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. 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-2

EC=3.2.1.18
Alternative name(s):
Cytosolic sialidase
N-acetyl-alpha-neuraminidase 2
Gene names
Name:NEU2
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moities from glycoproteins, oligosaccharides and gangliosides. Ref.3

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.2 Ref.3

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 33 family.

Contains 2 BNR repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 379379Sialidase-2
PRO_0000208898

Regions

Repeat127 – 13812BNR 1
Repeat197 – 20812BNR 2
Motif20 – 234FRIP motif

Sites

Active site461Proton acceptor By similarity
Active site3331Nucleophile By similarity
Active site3541 Potential
Binding site211Substrate By similarity
Binding site411Substrate By similarity
Binding site1791Substrate By similarity
Binding site1811Substrate By similarity
Binding site2181Substrate By similarity
Binding site2371Substrate Potential
Binding site3031Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64393 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B5AFFBC6B6BE88B1

FASTA37941,962
        10         20         30         40         50         60 
MATCPVLQKE TLFQTGDYAY RIPALIYLSK QKTLLAFAEK RLTKTDEHAD LFVLRRGSYN 

        70         80         90        100        110        120 
ADTHQVQWQA EEVVTQAYLE GHRSMSPCPL YDKQTRTLFL FFIAVRGQIS EHHQLQTGVN 

       130        140        150        160        170        180 
VTRLCHITST DHGKTWSAVQ DLTDTTIGST HQDWATFGVG PGHCLQLRNT AGSLLVPAYA 

       190        200        210        220        230        240 
YRKQPPIHAP APSAFCFLSH DHGSTWELGH FVSQNSLECQ VAEVGTGAER VVYLNARSCL 

       250        260        270        280        290        300 
GARVQAQSPN SGLDFQDNQV VSKLVEPPKG CHGSVIAFPN PTSKADALDV WLLYTHPTDS 

       310        320        330        340        350        360 
RKRTNLGVYL NQKPLDPTTW SAPTLLATGI CAYSDLQNMG HGPDGSPQFG CLYESNNYEE 

       370 
IVFLMFTLKQ AFPAVFGAQ 

« Hide

References

[1]"Cloning and expression of a soluble sialidase from Chinese hamster ovary cells: sequence alignment similarities to bacterial sialidases."
Ferrari J., Harris R., Warner T.G.
Glycobiology 4:367-373(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.
[2]"Characterization of cytosolic sialidase from Chinese hamster ovary cells: part I: cloning and expression of soluble sialidase in Escherichia coli."
Burg M., Muthing J.
Carbohydr. Res. 330:335-346(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
[3]"Characterization of cytosolic sialidase from Chinese hamster ovary cells: part II. Substrate specificity for gangliosides."
Muthing J., Burg M.
Carbohydr. Res. 330:347-356(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U06143 mRNA. Translation: AAA19746.1.
PIRA54961.
RefSeqNP_001233664.1. NM_001246735.2.

3D structure databases

ProteinModelPortalQ64393.
SMRQ64393. Positions 1-376.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH33. Glycoside Hydrolase Family 33.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100689301.
KEGGcge:100689301.

Organism-specific databases

CTD4759.

Phylogenomic databases

HOVERGENHBG052608.
KOK12357.

Family and domain databases

Gene3D2.120.10.10. 1 hit.
InterProIPR026945. Sialidase-2.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
[Graphical view]
PANTHERPTHR10628. PTHR10628. 1 hit.
PTHR10628:SF6. PTHR10628:SF6. 1 hit.
SUPFAMSSF50939. SSF50939. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNEUR2_CRIGR
AccessionPrimary (citable) accession number: Q64393
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 74 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