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Protein

Sialidase-2

Gene

Neu2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

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
Active sitei303 – 3031By similarity
Binding sitei303 – 3031SubstrateBy similarity
Active sitei333 – 3331NucleophileBy similarity
Active sitei354 – 3541Sequence Analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Lipid degradation, Lipid metabolism

Enzyme and pathway databases

ReactomeiREACT_310546. Sialic acid metabolism.
REACT_339900. Glycosphingolipid 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
Mouse skeletal muscle sialidase
Short name:
MSS
Murine thymic sialidase
Short name:
MTS
N-acetyl-alpha-neuraminidase 2
Gene namesi
Name:Neu2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1344417. Neu2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379Sialidase-2PRO_0000208900Add
BLAST

Proteomic databases

PaxDbiQ9JMH3.
PRIDEiQ9JMH3.

PTM databases

PhosphoSiteiQ9JMH3.

Expressioni

Tissue specificityi

Highly expressed in heart.1 Publication

Gene expression databases

BgeeiQ9JMH3.
CleanExiMM_NEU2.
ExpressionAtlasiQ9JMH3. baseline and differential.
GenevestigatoriQ9JMH3.

Structurei

3D structure databases

ProteinModelPortaliQ9JMH3.
SMRiQ9JMH3. Positions 1-376.
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.
GeneTreeiENSGT00390000011171.
HOGENOMiHOG000233778.
HOVERGENiHBG052608.
InParanoidiQ9JMH3.
KOiK12357.
PhylomeDBiQ9JMH3.
TreeFamiTF331063.

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.

Q9JMH3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATCPVLQKE TLFRTGVHAY RIPALLYLKK QKTLLAFAEK RASKTDEHAE
60 70 80 90 100
LIVLRRGSYN EATNRVKWQP EEVVTQAQLE GHRSMNPCPL YDKQTKTLFL
110 120 130 140 150
FFIAVPGRVS EHHQLHTKVN VTRLCCVSST DHGRTWSPIQ DLTETTIGST
160 170 180 190 200
HQEWATFAVG PGHCLQLRNP AGSLLVPAYA YRKLHPAQKP TPFAFCFISL
210 220 230 240 250
DHGHTWKLGN FVAENSLECQ VAEVGTGAQR MVYLNARSFL GARVQAQSPN
260 270 280 290 300
DGLDFQDNRV VSKLVEPPHG CHGSVVAFHN PISKPHALDT WLLYTHPTDS
310 320 330 340 350
RNRTNLGVYL NQMPLDPTAW SEPTLLAMGI CAYSDLQNMG QGPDGSPQFG
360 370
CLYESGNYEE IIFLIFTLKQ AFPTVFDAQ
Length:379
Mass (Da):42,403
Last modified:October 1, 2000 - v1
Checksum:i02124A46398F6793
GO

Sequence cautioni

The sequence BAB39152.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401K → R in AF139059 (PubMed:10329453).Curated
Sequence conflicti91 – 977YDKQTKT → MTSKKD in AF139059 (PubMed:10329453).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF139059 mRNA. No translation available.
AB028023 mRNA. Translation: BAA92867.1.
AB048604 mRNA. Translation: BAB39152.1. Different initiation.
CCDSiCCDS15135.1.
RefSeqiNP_001153635.1. NM_001160163.1.
NP_001153636.1. NM_001160164.1.
NP_001153637.1. NM_001160165.1.
NP_056565.1. NM_015750.3.
XP_006529587.1. XM_006529524.2.
UniGeneiMm.143717.

Genome annotation databases

EnsembliENSMUST00000070898; ENSMUSP00000065439; ENSMUSG00000079434.
ENSMUST00000165109; ENSMUSP00000126509; ENSMUSG00000079434.
ENSMUST00000166259; ENSMUSP00000132513; ENSMUSG00000079434.
GeneIDi23956.
KEGGimmu:23956.
UCSCiuc007bxa.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF139059 mRNA. No translation available.
AB028023 mRNA. Translation: BAA92867.1.
AB048604 mRNA. Translation: BAB39152.1. Different initiation.
CCDSiCCDS15135.1.
RefSeqiNP_001153635.1. NM_001160163.1.
NP_001153636.1. NM_001160164.1.
NP_001153637.1. NM_001160165.1.
NP_056565.1. NM_015750.3.
XP_006529587.1. XM_006529524.2.
UniGeneiMm.143717.

3D structure databases

ProteinModelPortaliQ9JMH3.
SMRiQ9JMH3. Positions 1-376.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH33. Glycoside Hydrolase Family 33.

PTM databases

PhosphoSiteiQ9JMH3.

Proteomic databases

PaxDbiQ9JMH3.
PRIDEiQ9JMH3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000070898; ENSMUSP00000065439; ENSMUSG00000079434.
ENSMUST00000165109; ENSMUSP00000126509; ENSMUSG00000079434.
ENSMUST00000166259; ENSMUSP00000132513; ENSMUSG00000079434.
GeneIDi23956.
KEGGimmu:23956.
UCSCiuc007bxa.2. mouse.

Organism-specific databases

CTDi4759.
MGIiMGI:1344417. Neu2.

Phylogenomic databases

eggNOGiNOG84455.
GeneTreeiENSGT00390000011171.
HOGENOMiHOG000233778.
HOVERGENiHBG052608.
InParanoidiQ9JMH3.
KOiK12357.
PhylomeDBiQ9JMH3.
TreeFamiTF331063.

Enzyme and pathway databases

ReactomeiREACT_310546. Sialic acid metabolism.
REACT_339900. Glycosphingolipid metabolism.

Miscellaneous databases

NextBioi303788.
PROiQ9JMH3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JMH3.
CleanExiMM_NEU2.
ExpressionAtlasiQ9JMH3. baseline and differential.
GenevestigatoriQ9JMH3.

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 mouse brain sialidase."
    Fronda C.L., Zeng G., Gao L., Yu R.K.
    Biochem. Biophys. Res. Commun. 258:727-731(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY.
    Tissue: Brain.
  2. "Molecular cloning of mouse ganglioside sialidase and its increased expression in Neuro2a cell differentiation."
    Hasegawa T., Yamaguchi K., Wada T., Takeda A., Itoyama Y., Miyagi T.
    J. Biol. Chem. 275:8007-8015(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Skeletal muscle.
  3. "Cloning, chromosomal mapping, and characteristic 5'-UTR sequence of murine cytosolic sialidase."
    Kotani K., Kuroiwa A., Saito T., Matsuda Y., Koda T., Kijimoto-Ochiai S.
    Biochem. Biophys. Res. Commun. 286:250-258(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Thymus.

Entry informationi

Entry nameiNEUR2_MOUSE
AccessioniPrimary (citable) accession number: Q9JMH3
Secondary accession number(s): Q99NA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: October 1, 2000
Last modified: April 1, 2015
This is version 115 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. 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.