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Sialidase-3 (EC 3.2.1.18) (Ganglioside sialidase) (Membrane sialidase) (N-acetyl-alpha-neuraminidase 3)

 NEUR3_BOVIN             Reviewed;         428 AA.
O97859;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
25-OCT-2017, entry version 102.
RecName: Full=Sialidase-3;
EC=3.2.1.18;
AltName: Full=Ganglioside sialidase;
AltName: Full=Membrane sialidase;
AltName: Full=N-acetyl-alpha-neuraminidase 3;
Name=NEU3;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=9988745; DOI=10.1074/jbc.274.8.5004;
Miyagi T., Wada T., Iwamatsu A., Hata K., Yoshikawa Y., Tokuyama S.,
Sawada M.;
"Molecular cloning and characterization of a plasma membrane-
associated sialidase specific for gangliosides.";
J. Biol. Chem. 274:5004-5011(1999).
-!- FUNCTION: Plays a role in modulating the ganglioside content of
the lipid bilayer at the level of membrane-bound sialyl
glycoconjugates. {ECO:0000269|PubMed:9988745}.
-!- CATALYTIC ACTIVITY: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-,
alpha-(2->8)- glycosidic linkages of terminal sialic acid residues
in oligosaccharides, glycoproteins, glycolipids, colominic acid
and synthetic substrates. {ECO:0000269|PubMed:9988745}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9988745};
Peripheral membrane protein {ECO:0000269|PubMed:9988745}.
-!- TISSUE SPECIFICITY: Expressed in brain.
{ECO:0000269|PubMed:9988745}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
{ECO:0000305}.
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EMBL; AB008184; BAA75071.1; -; mRNA.
RefSeq; NP_776547.2; NM_174122.3.
UniGene; Bt.477; -.
ProteinModelPortal; O97859; -.
STRING; 9913.ENSBTAP00000036593; -.
CAZy; GH33; Glycoside Hydrolase Family 33.
PaxDb; O97859; -.
PRIDE; O97859; -.
GeneID; 281349; -.
KEGG; bta:281349; -.
CTD; 10825; -.
eggNOG; ENOG410IFVF; Eukaryota.
eggNOG; ENOG410Y74Z; LUCA.
HOGENOM; HOG000233778; -.
HOVERGEN; HBG052608; -.
InParanoid; O97859; -.
KO; K12357; -.
BRENDA; 3.2.1.18; 908.
Proteomes; UP000009136; Unplaced.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IDA:UniProtKB.
GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC.
GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IDA:UniProtKB.
GO; GO:0006689; P:ganglioside catabolic process; IDA:UniProtKB.
GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
InterPro; IPR011040; Sialidase.
InterPro; IPR026944; Sialidase-3.
InterPro; IPR026856; Sialidase_fam.
InterPro; IPR036278; Sialidase_sf.
PANTHER; PTHR10628; PTHR10628; 1.
PANTHER; PTHR10628:SF23; PTHR10628:SF23; 1.
Pfam; PF13088; BNR_2; 1.
SUPFAM; SSF50939; SSF50939; 2.
1: Evidence at protein level;
Carbohydrate metabolism; Cell membrane; Complete proteome;
Direct protein sequencing; Glycosidase; Hydrolase; Lipid degradation;
Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
Repeat.
CHAIN 1 428 Sialidase-3.
/FTId=PRO_0000208902.
REPEAT 129 140 BNR 1.
REPEAT 203 214 BNR 2.
REPEAT 254 265 BNR 3.
MOTIF 24 27 FRIP motif.
ACT_SITE 50 50 Proton acceptor. {ECO:0000250}.
ACT_SITE 371 371 Nucleophile. {ECO:0000250}.
ACT_SITE 388 388 {ECO:0000255}.
BINDING 25 25 Substrate. {ECO:0000250}.
BINDING 45 45 Substrate. {ECO:0000250}.
BINDING 179 179 Substrate. {ECO:0000250}.
BINDING 181 181 Substrate. {ECO:0000250}.
BINDING 225 225 Substrate. {ECO:0000250}.
BINDING 245 245 Substrate. {ECO:0000255}.
BINDING 341 341 Substrate. {ECO:0000250}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JMH7}.
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


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