ID   NEUR3_BOVIN             Reviewed;         428 AA.
AC   O97859;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=Sialidase-3;
DE            EC=3.2.1.18;
DE   AltName: Full=Membrane sialidase;
DE   AltName: Full=Ganglioside sialidase;
DE   AltName: Full=N-acetyl-alpha-neuraminidase 3;
GN   Name=NEU3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
RP   CHARACTERIZATION.
RC   TISSUE=Brain;
RX   MEDLINE=99143165; PubMed=9988745; DOI=10.1074/jbc.274.8.5004;
RA   Miyagi T., Wada T., Iwamatsu A., Hata K., Yoshikawa Y., Tokuyama S.,
RA   Sawada M.;
RT   "Molecular cloning and characterization of a plasma membrane-
RT   associated sialidase specific for gangliosides.";
RL   J. Biol. Chem. 274:5004-5011(1999).
CC   -!- FUNCTION: Plays a role in modulating the ganglioside content of
CC       the lipid bilayer at the level of membrane-bound sialyl
CC       glycoconjugates.
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   -!- TISSUE SPECIFICITY: Expressed in brain.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC   -!- SIMILARITY: Contains 3 BNR repeats.
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DR   EMBL; AB008184; BAA75071.1; -; mRNA.
DR   IPI; IPI00687458; -.
DR   RefSeq; NP_776547.1; -.
DR   UniGene; Bt.477; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   Ensembl; ENSBTAG00000025931; Bos taurus.
DR   GeneID; 281349; -.
DR   KEGG; bta:281349; -.
DR   HOVERGEN; O97859; -.
DR   BRENDA; 3.2.1.18; 251.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Membrane; Repeat.
FT   CHAIN         1    428       Sialidase-3.
FT                                /FTId=PRO_0000208902.
FT   REPEAT      129    140       BNR 1.
FT   REPEAT      203    214       BNR 2.
FT   REPEAT      254    265       BNR 3.
FT   MOTIF        24     27       FRIP motif.
FT   ACT_SITE     50     50       Proton acceptor (By similarity).
FT   ACT_SITE    371    371       Nucleophile (By similarity).
FT   ACT_SITE    388    388       Potential.
FT   BINDING      25     25       Substrate (By similarity).
FT   BINDING     245    245       Substrate (Potential).
FT   BINDING     341    341       Substrate (By similarity).
SQ   SEQUENCE   428 AA;  47917 MW;  418B34F3245A8F21 CRC64;
     MEEVTSCSFS SPLFQQEDKR GVTYRIPALI YVPPAHTFLA FAEKRSSSKD EDALHLVLRR
     GLRTGQSVQW EPLKSLMKAT LPGHRTMNPC PVWERKSGYV YLFFICVQGH VTERQQIMSG
     RNPARLCFIC SQDAGYSWSD VRDLTEEVIG PEVTHWATFA VGPGHGIQLQ SGRLIIPAYA
     YYIPFWFFCF RLPYRARPHS LMIYSDDLGA TWHHGRLIKP MVTVECEVAE VIGKAGHPVL
     YCSARTPNRH RAEALSIDHG ECFQKPVLSH QLCEPPHGCQ GSVVSFCPLE IPGGCQDLAG
     EDAPAIQQSP LLCSSVRPEP EAGTLSESWL LYSHPTNKKR RVDLGIYLNQ SPLEAACWSR
     PWILHCGPCG YSDLAALENE GLFGCLFECG TKQECEQIAF RLFTDREILS HVQGDCSTPG
     MNSEPSKK
//