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Database: UniProt/SWISS-PROT
Entry: NEUR2_MOUSE
LinkDB: NEUR2_MOUSE
Original site: NEUR2_MOUSE 
ID   NEUR2_MOUSE             Reviewed;         379 AA.
AC   Q9JMH3; Q99NA3;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   20-JUN-2018, entry version 132.
DE   RecName: Full=Sialidase-2;
DE            EC=3.2.1.18;
DE   AltName: Full=Cytosolic sialidase;
DE   AltName: Full=Mouse skeletal muscle sialidase;
DE            Short=MSS;
DE   AltName: Full=Murine thymic sialidase;
DE            Short=MTS;
DE   AltName: Full=N-acetyl-alpha-neuraminidase 2;
GN   Name=Neu2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RC   TISSUE=Brain;
RX   PubMed=10329453; DOI=10.1006/bbrc.1999.0698;
RA   Fronda C.L., Zeng G., Gao L., Yu R.K.;
RT   "Molecular cloning and expression of mouse brain sialidase.";
RL   Biochem. Biophys. Res. Commun. 258:727-731(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Skeletal muscle;
RX   PubMed=10713120; DOI=10.1074/jbc.275.11.8007;
RA   Hasegawa T., Yamaguchi K., Wada T., Takeda A., Itoyama Y., Miyagi T.;
RT   "Molecular cloning of mouse ganglioside sialidase and its increased
RT   expression in Neuro2a cell differentiation.";
RL   J. Biol. Chem. 275:8007-8015(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Thymus;
RX   PubMed=11500029; DOI=10.1006/bbrc.2001.5374;
RA   Kotani K., Kuroiwa A., Saito T., Matsuda Y., Koda T.,
RA   Kijimoto-Ochiai S.;
RT   "Cloning, chromosomal mapping, and characteristic 5'-UTR sequence of
RT   murine cytosolic sialidase.";
RL   Biochem. Biophys. Res. Commun. 286:250-258(2001).
CC   -!- FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic
CC       acid) moities from glycoproteins, oligosaccharides and
CC       gangliosides.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-,
CC       alpha-(2->8)- glycosidic linkages of terminal sialic acid residues
CC       in oligosaccharides, glycoproteins, glycolipids, colominic acid
CC       and synthetic substrates. {ECO:0000269|PubMed:10329453}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart.
CC       {ECO:0000269|PubMed:10713120}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB39152.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AF139059; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AB028023; BAA92867.1; -; mRNA.
DR   EMBL; AB048604; BAB39152.1; ALT_INIT; mRNA.
DR   CCDS; CCDS15135.1; -.
DR   RefSeq; NP_001153635.1; NM_001160163.1.
DR   RefSeq; NP_001153636.1; NM_001160164.1.
DR   RefSeq; NP_001153637.1; NM_001160165.1.
DR   RefSeq; NP_056565.1; NM_015750.3.
DR   RefSeq; XP_006529587.1; XM_006529524.3.
DR   UniGene; Mm.143717; -.
DR   ProteinModelPortal; Q9JMH3; -.
DR   SMR; Q9JMH3; -.
DR   STRING; 10090.ENSMUSP00000131409; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   iPTMnet; Q9JMH3; -.
DR   PhosphoSitePlus; Q9JMH3; -.
DR   MaxQB; Q9JMH3; -.
DR   PaxDb; Q9JMH3; -.
DR   PRIDE; Q9JMH3; -.
DR   Ensembl; ENSMUST00000070898; ENSMUSP00000065439; ENSMUSG00000079434.
DR   Ensembl; ENSMUST00000165109; ENSMUSP00000126509; ENSMUSG00000079434.
DR   Ensembl; ENSMUST00000166259; ENSMUSP00000132513; ENSMUSG00000079434.
DR   GeneID; 23956; -.
DR   KEGG; mmu:23956; -.
DR   UCSC; uc007bxa.2; mouse.
DR   CTD; 4759; -.
DR   MGI; MGI:1344417; Neu2.
DR   eggNOG; ENOG410IFVF; Eukaryota.
DR   eggNOG; ENOG410Y74Z; LUCA.
DR   GeneTree; ENSGT00390000011171; -.
DR   HOGENOM; HOG000233778; -.
DR   HOVERGEN; HBG052608; -.
DR   InParanoid; Q9JMH3; -.
DR   KO; K12357; -.
DR   PhylomeDB; Q9JMH3; -.
DR   TreeFam; TF331063; -.
DR   Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR   Reactome; R-MMU-4085001; Sialic acid metabolism.
DR   PRO; PR:Q9JMH3; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000079434; -.
DR   CleanEx; MM_NEU2; -.
DR   ExpressionAtlas; Q9JMH3; baseline and differential.
DR   Genevisible; Q9JMH3; MM.
DR   GO; GO:1902494; C:catalytic complex; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; ISS:UniProtKB.
DR   GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; ISO:MGI.
DR   GO; GO:0051692; P:cellular oligosaccharide catabolic process; ISO:MGI.
DR   GO; GO:0006689; P:ganglioside catabolic process; ISS:UniProtKB.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; ISS:UniProtKB.
DR   GO; GO:0045663; P:positive regulation of myoblast differentiation; ISO:MGI.
DR   GO; GO:0010831; P:positive regulation of myotube differentiation; ISO:MGI.
DR   InterPro; IPR011040; Sialidase.
DR   InterPro; IPR026945; Sialidase-2.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   PANTHER; PTHR10628; PTHR10628; 1.
DR   PANTHER; PTHR10628:SF6; PTHR10628:SF6; 1.
DR   Pfam; PF13088; BNR_2; 1.
DR   SUPFAM; SSF50939; SSF50939; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Complete proteome; Cytoplasm; Glycosidase;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Reference proteome;
KW   Repeat.
FT   CHAIN         1    379       Sialidase-2.
FT                                /FTId=PRO_0000208900.
FT   REPEAT      127    138       BNR 1.
FT   REPEAT      197    208       BNR 2.
FT   MOTIF        20     23       FRIP motif.
FT   ACT_SITE     46     46       Proton acceptor. {ECO:0000250}.
FT   ACT_SITE    303    303       {ECO:0000250}.
FT   ACT_SITE    333    333       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    354    354       {ECO:0000255}.
FT   BINDING      21     21       Substrate. {ECO:0000250}.
FT   BINDING      41     41       Substrate. {ECO:0000250}.
FT   BINDING     179    179       Substrate. {ECO:0000250}.
FT   BINDING     181    181       Substrate. {ECO:0000250}.
FT   BINDING     218    218       Substrate. {ECO:0000250}.
FT   BINDING     237    237       Substrate. {ECO:0000255}.
FT   BINDING     303    303       Substrate. {ECO:0000250}.
FT   CONFLICT     40     40       K -> R (in Ref. 1; AF139059).
FT                                {ECO:0000305}.
FT   CONFLICT     91     97       YDKQTKT -> MTSKKD (in Ref. 1; AF139059).
FT                                {ECO:0000305}.
SQ   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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