ID   Q0VGI4_MOUSE            Unreviewed;       379 AA.
AC   Q0VGI4;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 130.
DE   RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE            EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
GN   Name=Neu2 {ECO:0000313|EMBL:AAI05662.1, ECO:0000313|MGI:MGI:1344417};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAI05662.1};
RN   [1] {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., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., 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., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-
CC         (2->8)- glycosidic linkages of terminal sialic acid residues in
CC         oligosaccharides, glycoproteins, glycolipids, colominic acid and
CC         synthetic substrates.; EC=3.2.1.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00000427};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC       {ECO:0000256|ARBA:ARBA00009348}.
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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   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   AlphaFoldDB; Q0VGI4; -.
DR   SMR; Q0VGI4; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   Antibodypedia; 34447; 310 antibodies from 27 providers.
DR   DNASU; 23956; -.
DR   GeneID; 23956; -.
DR   KEGG; mmu:23956; -.
DR   AGR; MGI:1344417; -.
DR   CTD; 4759; -.
DR   MGI; MGI:1344417; Neu2.
DR   VEuPathDB; HostDB:ENSMUSG00000079434; -.
DR   HOGENOM; CLU_024620_2_1_1; -.
DR   OrthoDB; 5482010at2759; -.
DR   BioGRID-ORCS; 23956; 3 hits in 78 CRISPR screens.
DR   ChiTaRS; Neu2; mouse.
DR   ExpressionAtlas; Q0VGI4; baseline and differential.
DR   GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC.
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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   Gene3D; 2.120.10.10; -; 1.
DR   InterPro; IPR011040; Sialidase.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   PANTHER; PTHR10628; SIALIDASE; 1.
DR   PANTHER; PTHR10628:SF6; SIALIDASE-2; 1.
DR   Pfam; PF13088; BNR_2; 1.
DR   SUPFAM; SSF50939; Sialidases; 1.
PE   2: Evidence at transcript level;
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          33..342
FT                   /note="Sialidase"
FT                   /evidence="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
//