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Protein

Sialidase-2

Gene

Neu2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moities from glycoproteins, oligosaccharides and gangliosides.1 Publication

Catalytic activityi

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211SubstrateBy similarity
Binding sitei41 – 411SubstrateBy similarity
Active sitei46 – 461Proton acceptorBy similarity
Binding sitei179 – 1791SubstrateBy similarity
Binding sitei181 – 1811SubstrateBy similarity
Binding sitei218 – 2181SubstrateBy similarity
Binding sitei237 – 2371SubstrateSequence Analysis
Binding sitei303 – 3031SubstrateBy similarity
Active sitei333 – 3331NucleophileBy similarity
Active sitei354 – 3541Sequence Analysis

GO - Molecular functioni

  1. exo-alpha-(2->3)-sialidase activity Source: UniProtKB
  2. exo-alpha-(2->6)-sialidase activity Source: UniProtKB-EC
  3. exo-alpha-(2->8)-sialidase activity Source: UniProtKB-EC
  4. exo-alpha-sialidase activity Source: RGD

GO - Biological processi

  1. ganglioside catabolic process Source: UniProtKB
  2. oligosaccharide catabolic process Source: UniProtKB
  3. positive regulation of myoblast differentiation Source: RGD
  4. positive regulation of myotube differentiation Source: RGD
  5. response to ethanol Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Lipid degradation, Lipid metabolism

Protein family/group databases

CAZyiGH33. Glycoside Hydrolase Family 33.

Names & Taxonomyi

Protein namesi
Recommended name:
Sialidase-2 (EC:3.2.1.18)
Alternative name(s):
Cytosolic sialidase
N-acetyl-alpha-neuraminidase 2
Gene namesi
Name:Neu2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3164. Neu2.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. cytosol Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379Sialidase-2PRO_0000208901Add
BLAST

Proteomic databases

PaxDbiQ64627.
PRIDEiQ64627.

PTM databases

PhosphoSiteiQ64627.

Expressioni

Tissue specificityi

Detected in skeletal muscle.1 Publication

Gene expression databases

GenevestigatoriQ64627.

Structurei

3D structure databases

ProteinModelPortaliQ64627.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati127 – 13812BNR 1Add
BLAST
Repeati197 – 20812BNR 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi20 – 234FRIP motif

Sequence similaritiesi

Belongs to the glycosyl hydrolase 33 family.Curated
Contains 2 BNR repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG84455.
HOGENOMiHOG000233778.
HOVERGENiHBG052608.
InParanoidiQ64627.
PhylomeDBiQ64627.

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR026945. Sialidase-2.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
[Graphical view]
PANTHERiPTHR10628. PTHR10628. 1 hit.
PTHR10628:SF6. PTHR10628:SF6. 1 hit.
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Complete.

Q64627-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
METCPVLQKE TLFHTEVYAY RIPALLYLKK QKTLLAFAEK RASRTDEHAE
60 70 80 90 100
LIVLRRGSYN GATNHVKWQP EEVVTQAQLE GHRSMNPCPL YDKQTKTLFL
110 120 130 140 150
FFIAVPGRVS EQHQLQTRVN VTRLCRVTST DYGMNWSPVQ DLTETTIGST
160 170 180 190 200
HQDWATFAVG PGHCLQLRNR AGSLLVPAYA YRKLHPVHKP TPFAFCFISL
210 220 230 240 250
DHGHTWELGN FVSENSLECQ VAEVGTGAHR VVYLNARSFI GARVQAQSPN
260 270 280 290 300
DGLDFQDNQV VSKLVEPPHG CHGSVVAFHS PTSKPDCLRH VAAYTHPTDS
310 320 330 340 350
RNRTNLGVYL NQTPLDPTAW SEPTLLATGT CAYSDLQIWG LGPDGSPQFG
360 370
CLYESGNYDE IIFLMFTLKQ AFPTVHGAQ
Length:379
Mass (Da):42,382
Last modified:November 1, 1996 - v1
Checksum:i55583C7043CA9784
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16300 mRNA. Translation: BAA03805.1.
D50606 Genomic DNA. Translation: BAA09169.1.
PIRiA49679.
UniGeneiRn.9731.

Genome annotation databases

UCSCiRGD:3164. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16300 mRNA. Translation: BAA03805.1.
D50606 Genomic DNA. Translation: BAA09169.1.
PIRiA49679.
UniGeneiRn.9731.

3D structure databases

ProteinModelPortaliQ64627.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH33. Glycoside Hydrolase Family 33.

PTM databases

PhosphoSiteiQ64627.

Proteomic databases

PaxDbiQ64627.
PRIDEiQ64627.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3164. rat.

Organism-specific databases

RGDi3164. Neu2.

Phylogenomic databases

eggNOGiNOG84455.
HOGENOMiHOG000233778.
HOVERGENiHBG052608.
InParanoidiQ64627.
PhylomeDBiQ64627.

Miscellaneous databases

PROiQ64627.

Gene expression databases

GenevestigatoriQ64627.

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR026945. Sialidase-2.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
[Graphical view]
PANTHERiPTHR10628. PTHR10628. 1 hit.
PTHR10628:SF6. PTHR10628:SF6. 1 hit.
SUPFAMiSSF50939. SSF50939. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and expression of cDNA encoding rat skeletal muscle cytosolic sialidase."
    Miyagi T., Konno K., Emori Y., Kawasaki H., Suzuki K., Yasui A., Tsuiki S.
    J. Biol. Chem. 268:26435-26440(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    Strain: Wistar.
    Tissue: Skeletal muscle.
  2. "Genomic organization and the 5'-upstream sequence of the rat cytosolic sialidase gene."
    Sato K., Miyagi T.
    Glycobiology 5:511-516(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
    Strain: Sprague-Dawley.
    Tissue: Liver.

Entry informationi

Entry nameiNEUR2_RAT
AccessioniPrimary (citable) accession number: Q64627
Secondary accession number(s): Q63705
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.