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Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: NEUR2_MOUSE Q0VGI4_MOUSE Q3ULV6_MOUSE
LinkDB: NEUR2_MOUSE Q0VGI4_MOUSE Q3ULV6_MOUSE
Original site: NEUR2_MOUSE Q0VGI4_MOUSE Q3ULV6_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   07-JUN-2017, entry version 130.
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; IBA:GO_Central.
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   InterPro; IPR026945; Sialidase-2.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR011040; Sialidases.
DR   PANTHER; PTHR10628; PTHR10628; 1.
DR   PANTHER; PTHR10628:SF27; PTHR10628:SF27; 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
//
  All links  
Ontology (13)   
   GO (12)   
   CAZY (1)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (12)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
   ENSEMBL-UP (7)   
   MGI-MMU (1)   
Protein sequence (5)   
   RefSeq(pep) (5)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (4)   
   InterPro (3)   
   Pfam (1)   
Literature (3)   
   PubMed (3)   
All databases (41)   

Download RDF
ID   Q0VGI4_MOUSE            Unreviewed;       379 AA.
AC   Q0VGI4;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   05-JUL-2017, entry version 92.
DE   SubName: Full=Neu2 protein {ECO:0000313|EMBL:AAI05662.1};
DE   SubName: Full=Neuraminidase 2 {ECO:0000313|EMBL:AAI05658.1};
DE   SubName: Full=Neuraminidase 2, isoform CRA_a {ECO:0000313|EMBL:EDL40156.1};
GN   Name=Neu2 {ECO:0000313|EMBL:AAI05662.1, ECO:0000313|MGI:MGI:1344417};
GN   ORFNames=mCG_16214 {ECO:0000313|EMBL:EDL40156.1};
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 {ECO:0000313|EMBL:AAI05662.1};
RN   [1] {ECO:0000313|EMBL:EDL40156.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed {ECO:0000313|EMBL:EDL40156.1};
RX   PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [2] {ECO:0000313|EMBL:AAI05662.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones {ECO:0000313|EMBL:AAI05662.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M.,
RA   Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S.,
RA   Feolo M., Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F.,
RA   Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J.,
RA   Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N.,
RA   Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B.,
RA   Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B.,
RA   Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S.,
RA   Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R.,
RA   Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L.,
RA   Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E.,
RA   Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D.,
RA   Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G.,
RA   Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J.,
RA   Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L.,
RA   Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D.,
RA   Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A.,
RA   Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S.,
RA   Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3] {ECO:0000313|EMBL:EDL40156.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed {ECO:0000313|EMBL:EDL40156.1};
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC105657; AAI05658.1; -; mRNA.
DR   EMBL; BC105658; AAI05659.1; -; mRNA.
DR   EMBL; BC105659; AAI05660.1; -; mRNA.
DR   EMBL; BC105661; AAI05662.1; -; mRNA.
DR   EMBL; CH466520; EDL40156.1; -; Genomic_DNA.
DR   EMBL; CH466520; EDL40158.1; -; Genomic_DNA.
DR   RefSeq; NP_001153636.1; NM_001160164.1.
DR   RefSeq; NP_056565.1; NM_015750.3.
DR   RefSeq; XP_006529587.1; XM_006529524.3.
DR   UniGene; Mm.143717; -.
DR   SMR; Q0VGI4; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   GeneID; 23956; -.
DR   KEGG; mmu:23956; -.
DR   CTD; 4759; -.
DR   MGI; MGI:1344417; Neu2.
DR   eggNOG; ENOG410IFVF; Eukaryota.
DR   eggNOG; ENOG410Y74Z; LUCA.
DR   HOVERGEN; HBG052608; -.
DR   KO; K12357; -.
DR   Bgee; ENSMUSG00000079434; -.
DR   ExpressionAtlas; Q0VGI4; baseline and differential.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro.
DR   InterPro; IPR026945; Sialidase-2.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR011040; Sialidases.
DR   PANTHER; PTHR10628; PTHR10628; 1.
DR   PANTHER; PTHR10628:SF27; PTHR10628:SF27; 1.
DR   Pfam; PF13088; BNR_2; 1.
DR   SUPFAM; SSF50939; SSF50939; 1.
PE   2: Evidence at transcript level;
FT   DOMAIN       33    342       Sialidases. {ECO:0000259|Pfam:PF13088}.
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
//
  All links  
Ontology (2)   
   GO (1)   
   CAZY (1)   
Gene (5)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
   MGI-MMU (1)   
Protein sequence (3)   
   RefSeq(pep) (3)   
DNA sequence (5)   
   EMBL (5)   
Protein domain (4)   
   InterPro (3)   
   Pfam (1)   
Literature (2)   
   PubMed (2)   
All databases (21)   

Download RDF
ID   Q3ULV6_MOUSE            Unreviewed;       379 AA.
AC   Q3ULV6;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-AUG-2017, entry version 76.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAE26342.1};
GN   Name=Neu2 {ECO:0000313|MGI:MGI:1344417};
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 {ECO:0000313|EMBL:BAE26342.1};
RN   [1] {ECO:0000313|EMBL:BAE26342.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:BAE26342.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAE26342.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:BAE26342.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAE26342.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:BAE26342.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAE26342.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:BAE26342.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAE26342.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:BAE26342.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [6] {ECO:0000313|EMBL:BAE26342.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:BAE26342.1};
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:BAE26342.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:BAE26342.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8] {ECO:0000313|EMBL:BAE26342.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:BAE26342.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
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DR   EMBL; AK145284; BAE26342.1; -; mRNA.
DR   RefSeq; NP_001153635.1; NM_001160163.1.
DR   RefSeq; NP_001153636.1; NM_001160164.1.
DR   UniGene; Mm.143717; -.
DR   PaxDb; Q3ULV6; -.
DR   GeneID; 23956; -.
DR   KEGG; mmu:23956; -.
DR   CTD; 4759; -.
DR   MGI; MGI:1344417; Neu2.
DR   eggNOG; ENOG410IFVF; Eukaryota.
DR   eggNOG; ENOG410Y74Z; LUCA.
DR   HOVERGEN; HBG052608; -.
DR   KO; K12357; -.
DR   Genevisible; Q3ULV6; MM.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro.
DR   InterPro; IPR026945; Sialidase-2.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR011040; Sialidases.
DR   PANTHER; PTHR10628; PTHR10628; 1.
DR   PANTHER; PTHR10628:SF27; PTHR10628:SF27; 1.
DR   Pfam; PF13088; BNR_2; 1.
DR   SUPFAM; SSF50939; SSF50939; 1.
PE   2: Evidence at transcript level;
FT   DOMAIN       33    342       Sialidases. {ECO:0000259|Pfam:PF13088}.
SQ   SEQUENCE   379 AA;  42436 MW;  7EF748A37DD2292A CRC64;
     MATCPVLQKE TLFRTGVHAY RIPALLYLKK QKTLLAFAEK RASKTDEHAE LIVLRRGSYN
     EATNRVKWQP EEVVTQAQLE GHRSMNPCPL YDKQTKTLFL FFIAVPGRVS EHHQLHTKVN
     VTRLCCVSST DHGRTWSPTQ DLTETTVGST HQEWATFAVG PGHCLQLRNP AGSLLVPAYA
     YRKLHPAQKP TPFAFCFISL DHGHTWKLGN FVAENSLECQ VAEVGTGAQR MVYLNARSFL
     GARVQAQSPN DGLDFQDNRV VSKLVEPPHG CHGSVVAFHN PISKPHALDT WLLYTHRTDS
     RNRTNLGVYL NQMPLDPTAW SEPTLLAMGI CAYSDLQNMG QGPDGSPQFG CLYESGNYEE
     IIFLIFTLKQ AFPTVFDAQ
//
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Ontology (1)   
   GO (1)   
Gene (5)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
   MGI-MMU (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (4)   
   InterPro (3)   
   Pfam (1)   
Literature (6)   
   PubMed (6)   
All databases (19)   

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