ID   NEUR4_MOUSE             Reviewed;         478 AA.
AC   Q8BZL1;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   16-JUN-2009, entry version 46.
DE   RecName: Full=Sialidase-4;
DE            EC=3.2.1.18;
DE   AltName: Full=Neuraminidase 4;
DE   AltName: Full=N-acetyl-alpha-neuraminidase 4;
GN   Name=Neu4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=14637003; DOI=10.1016/j.gene.2003.08.005;
RA   Comelli E.M., Amado M., Lustig S.R., Paulson J.C.;
RT   "Identification and expression of Neu4, a novel murine sialidase.";
RL   Gene 321:155-161(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: May function in lysosomal catabolism of sialylated
CC       glycoconjugates. Has sialidase activity towards synthetic
CC       substrates, such as 2'-(4-methylumbelliferyl)-alpha-D-N-
CC       acetylneuraminic acid (4-MU-NANA or 4MU-NeuAc). Has a broad
CC       substrate specificity being active on glycoproteins,
CC       oligosaccharides and sialylated glycolipids (By similarity).
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.
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BZL1-2; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BZL1-1; Sequence=VSP_037492;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in brain.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC   -!- SIMILARITY: Contains 3 BNR repeats.
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DR   EMBL; AY258421; AAP81169.1; -; mRNA.
DR   EMBL; AK034236; BAC28641.1; -; mRNA.
DR   IPI; IPI00227589; -.
DR   IPI; IPI00416833; -.
DR   UniGene; Mm.214565; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   Ensembl; ENSMUSG00000034000; Mus musculus.
DR   MGI; MGI:2661364; Neu4.
DR   HOGENOM; Q8BZL1; -.
DR   HOVERGEN; Q8BZL1; -.
DR   OMA; Q8BZL1; LTEEAIG.
DR   BRENDA; 3.2.1.18; 244.
DR   ArrayExpress; Q8BZL1; -.
DR   Bgee; Q8BZL1; -.
DR   CleanEx; MM_NEU4; -.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0019866; C:organelle inner membrane; ISS:UniProtKB.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; IDA:MGI.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycosidase; Hydrolase; Membrane; Repeat.
FT   CHAIN         1    478       Sialidase-4.
FT                                /FTId=PRO_0000208907.
FT   REPEAT      127    138       BNR 1.
FT   REPEAT      200    211       BNR 2.
FT   REPEAT      247    258       BNR 3.
FT   MOTIF        22     25       FRIP motif.
FT   ACT_SITE     48     48       Proton acceptor (By similarity).
FT   ACT_SITE    413    413       Nucleophile (By similarity).
FT   ACT_SITE    434    434       Potential.
FT   BINDING      23     23       Substrate (By similarity).
FT   BINDING     383    383       Substrate (By similarity).
FT   VAR_SEQ       1      1       M -> METAGAPFCFHVDSLVPCSYWKVM (in isoform
FT                                2).
FT                                /FTId=VSP_037492.
SQ   SEQUENCE   478 AA;  52426 MW;  E1833F5DBFBFD08F CRC64;
     MGPTRVPRRT VLFQRERTGL TYRVPALLCV PPRPTLLAFA EQRLSPDDSH AHRLVLRRGT
     LTRGSVRWGT LSVLETAVLE EHRSMNPCPV LDEHSGTIFL FFIAVLGHTP EAVQIATGKN
     AARLCCVTSC DAGLTWGSVR DLTEEAIGAA LQDWATFAVG PGHGVQLRSG RLLVPAYTYH
     VDRRECFGKI CWTSPHSLAF YSDDHGISWH CGGLVPNLRS GECQLAAVDG DFLYCNARSP
     LGNRVQALSA DEGTSFLPGE LVPTLAETAR GCQGSIVGFL APPSIEPQDD RWTGSPRNTP
     HSPCFNLRVQ ESSGEGARGL LERWMPRLPL CYPQSRSPEN HGLEPGSDGD KTSWTPECPM
     SSDSMLQSPT WLLYSHPAGR RARLHMGIYL SRSPLDPHSW TEPWVIYEGP SGYSDLAFLG
     PMPGASLVFA CLFESGTRTS YEDISFCLFS LADVLENVPT GLEMLSLRDK AQGHCWPS
//