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Sialidase-2 (EC 3.2.1.18) (Cytosolic sialidase) (Mouse skeletal muscle sialidase) (MSS) (Murine thymic sialidase) (MTS) (N-acetyl-alpha-neuraminidase 2)

 NEUR2_MOUSE             Reviewed;         379 AA.
Q9JMH3; Q99NA3;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
12-SEP-2018, entry version 133.
RecName: Full=Sialidase-2;
EC=3.2.1.18;
AltName: Full=Cytosolic sialidase;
AltName: Full=Mouse skeletal muscle sialidase;
Short=MSS;
AltName: Full=Murine thymic sialidase;
Short=MTS;
AltName: Full=N-acetyl-alpha-neuraminidase 2;
Name=Neu2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
TISSUE=Brain;
PubMed=10329453; DOI=10.1006/bbrc.1999.0698;
Fronda C.L., Zeng G., Gao L., Yu R.K.;
"Molecular cloning and expression of mouse brain sialidase.";
Biochem. Biophys. Res. Commun. 258:727-731(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Skeletal muscle;
PubMed=10713120; DOI=10.1074/jbc.275.11.8007;
Hasegawa T., Yamaguchi K., Wada T., Takeda A., Itoyama Y., Miyagi T.;
"Molecular cloning of mouse ganglioside sialidase and its increased
expression in Neuro2a cell differentiation.";
J. Biol. Chem. 275:8007-8015(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Thymus;
PubMed=11500029; DOI=10.1006/bbrc.2001.5374;
Kotani K., Kuroiwa A., Saito T., Matsuda Y., Koda T.,
Kijimoto-Ochiai S.;
"Cloning, chromosomal mapping, and characteristic 5'-UTR sequence of
murine cytosolic sialidase.";
Biochem. Biophys. Res. Commun. 286:250-258(2001).
-!- FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic
acid) moities from glycoproteins, oligosaccharides and
gangliosides.
-!- 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. {ECO:0000269|PubMed:10329453}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Highly expressed in heart.
{ECO:0000269|PubMed:10713120}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB39152.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF139059; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AB028023; BAA92867.1; -; mRNA.
EMBL; AB048604; BAB39152.1; ALT_INIT; mRNA.
CCDS; CCDS15135.1; -.
RefSeq; NP_001153635.1; NM_001160163.1.
RefSeq; NP_001153636.1; NM_001160164.1.
RefSeq; NP_001153637.1; NM_001160165.1.
RefSeq; NP_056565.1; NM_015750.3.
RefSeq; XP_006529587.1; XM_006529524.3.
UniGene; Mm.143717; -.
ProteinModelPortal; Q9JMH3; -.
SMR; Q9JMH3; -.
STRING; 10090.ENSMUSP00000131409; -.
CAZy; GH33; Glycoside Hydrolase Family 33.
iPTMnet; Q9JMH3; -.
PhosphoSitePlus; Q9JMH3; -.
MaxQB; Q9JMH3; -.
PaxDb; Q9JMH3; -.
PRIDE; Q9JMH3; -.
Ensembl; ENSMUST00000070898; ENSMUSP00000065439; ENSMUSG00000079434.
Ensembl; ENSMUST00000165109; ENSMUSP00000126509; ENSMUSG00000079434.
Ensembl; ENSMUST00000166259; ENSMUSP00000132513; ENSMUSG00000079434.
GeneID; 23956; -.
KEGG; mmu:23956; -.
UCSC; uc007bxa.2; mouse.
CTD; 4759; -.
MGI; MGI:1344417; Neu2.
eggNOG; ENOG410IFVF; Eukaryota.
eggNOG; ENOG410Y74Z; LUCA.
GeneTree; ENSGT00390000011171; -.
HOGENOM; HOG000233778; -.
HOVERGEN; HBG052608; -.
InParanoid; Q9JMH3; -.
KO; K12357; -.
PhylomeDB; Q9JMH3; -.
TreeFam; TF331063; -.
Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
Reactome; R-MMU-4085001; Sialic acid metabolism.
PRO; PR:Q9JMH3; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000079434; Expressed in 71 organ(s), highest expression level in zone of skin.
CleanEx; MM_NEU2; -.
ExpressionAtlas; Q9JMH3; baseline and differential.
Genevisible; Q9JMH3; MM.
GO; GO:1902494; C:catalytic complex; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0016020; C:membrane; IBA:GO_Central.
GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; ISS:UniProtKB.
GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC.
GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC.
GO; GO:0004308; F:exo-alpha-sialidase activity; ISO:MGI.
GO; GO:0051692; P:cellular oligosaccharide catabolic process; ISO:MGI.
GO; GO:0006689; P:ganglioside catabolic process; ISS:UniProtKB.
GO; GO:0009313; P:oligosaccharide catabolic process; ISS:UniProtKB.
GO; GO:0045663; P:positive regulation of myoblast differentiation; ISO:MGI.
GO; GO:0010831; P:positive regulation of myotube differentiation; ISO:MGI.
InterPro; IPR011040; Sialidase.
InterPro; IPR026945; Sialidase-2.
InterPro; IPR026856; Sialidase_fam.
InterPro; IPR036278; Sialidase_sf.
PANTHER; PTHR10628; PTHR10628; 1.
PANTHER; PTHR10628:SF6; PTHR10628:SF6; 1.
Pfam; PF13088; BNR_2; 1.
SUPFAM; SSF50939; SSF50939; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Complete proteome; Cytoplasm; Glycosidase;
Hydrolase; Lipid degradation; Lipid metabolism; Reference proteome;
Repeat.
CHAIN 1 379 Sialidase-2.
/FTId=PRO_0000208900.
REPEAT 127 138 BNR 1.
REPEAT 197 208 BNR 2.
MOTIF 20 23 FRIP motif.
ACT_SITE 46 46 Proton acceptor. {ECO:0000250}.
ACT_SITE 303 303 {ECO:0000250}.
ACT_SITE 333 333 Nucleophile. {ECO:0000250}.
ACT_SITE 354 354 {ECO:0000255}.
BINDING 21 21 Substrate. {ECO:0000250}.
BINDING 41 41 Substrate. {ECO:0000250}.
BINDING 179 179 Substrate. {ECO:0000250}.
BINDING 181 181 Substrate. {ECO:0000250}.
BINDING 218 218 Substrate. {ECO:0000250}.
BINDING 237 237 Substrate. {ECO:0000255}.
BINDING 303 303 Substrate. {ECO:0000250}.
CONFLICT 40 40 K -> R (in Ref. 1; AF139059).
{ECO:0000305}.
CONFLICT 91 97 YDKQTKT -> MTSKKD (in Ref. 1; AF139059).
{ECO:0000305}.
SEQUENCE 379 AA; 42403 MW; 02124A46398F6793 CRC64;
MATCPVLQKE TLFRTGVHAY RIPALLYLKK QKTLLAFAEK RASKTDEHAE LIVLRRGSYN
EATNRVKWQP EEVVTQAQLE GHRSMNPCPL YDKQTKTLFL FFIAVPGRVS EHHQLHTKVN
VTRLCCVSST DHGRTWSPIQ DLTETTIGST HQEWATFAVG PGHCLQLRNP AGSLLVPAYA
YRKLHPAQKP TPFAFCFISL DHGHTWKLGN FVAENSLECQ VAEVGTGAQR MVYLNARSFL
GARVQAQSPN DGLDFQDNRV VSKLVEPPHG CHGSVVAFHN PISKPHALDT WLLYTHPTDS
RNRTNLGVYL NQMPLDPTAW SEPTLLAMGI CAYSDLQNMG QGPDGSPQFG CLYESGNYEE
IIFLIFTLKQ AFPTVFDAQ


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