NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
TISSUE=Brain;
DOI=10.1074/jbc.274.8.5004; PubMed=9988745 [NCBI, ExPASy, EBI, Israel, Japan]
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).

Comments

FUNCTION: Plays a role in modulating the ganglioside content of the lipid bilayer at the level of membrane-bound sialyl glycoconjugates.
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.
SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By similarity).
TISSUE SPECIFICITY: Expressed in brain.
SIMILARITY: Belongs to the glycosyl hydrolase 33 family [view classification].
SIMILARITY: Contains 3 BNR repeats.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB008184; BAA75071.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_776547.1; -.

UniGene

Bt.477

3D structure databases

ModBase

O97859.

Ontologies

GO:0004308;	Molecular function: exo-alpha-sialidase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR002860; BNR.
Graphical view of domain structure.

Pfam

PF02012; BNR; 3.
Pfam graphical view of domain structure.

Genome annotation databases

Ensembl

ENSBTAG00000025931; Bos taurus. [Contig view]

GeneID

281349; -.

KEGG

bta:281349; -.

Phylogenomic databases

HOVERGEN

O97859; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Glycosidase; Hydrolase; Membrane; Repeat.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 428`	`428`	`Sialidase-3.`	`PRO_0000208902`
`REPEAT`	`129 140`	`12`	`BNR 1.`
`REPEAT`	`203 214`	`12`	`BNR 2.`
`REPEAT`	`254 265`	`12`	`BNR 3.`
`MOTIF`	`24 27`	`4`	`FRIP motif.`
`ACT_SITE`	`50 50`		`Proton acceptor (By similarity).`
`ACT_SITE`	`371 371`		`Nucleophile (By similarity).`
`ACT_SITE`	`388 388`		`Potential.`
`BINDING`	`25 25`		`Substrate (By similarity).`
`BINDING`	`245 245`		`Substrate (Potential).`
`BINDING`	`341 341`		`Substrate (By similarity).`

Sequence information

Length: 428 AA [This is the length of the unprocessed precursor]

Molecular weight: 47917 Da [This is the MW of the unprocessed precursor]

CRC64: 418B34F3245A8F21 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEEVTSCSFS SPLFQQEDKR GVTYRIPALI YVPPAHTFLA FAEKRSSSKD EDALHLVLRR 

        70         80         90        100        110        120 
GLRTGQSVQW EPLKSLMKAT LPGHRTMNPC PVWERKSGYV YLFFICVQGH VTERQQIMSG 

       130        140        150        160        170        180 
RNPARLCFIC SQDAGYSWSD VRDLTEEVIG PEVTHWATFA VGPGHGIQLQ SGRLIIPAYA 

       190        200        210        220        230        240 
YYIPFWFFCF RLPYRARPHS LMIYSDDLGA TWHHGRLIKP MVTVECEVAE VIGKAGHPVL 

       250        260        270        280        290        300 
YCSARTPNRH RAEALSIDHG ECFQKPVLSH QLCEPPHGCQ GSVVSFCPLE IPGGCQDLAG 

       310        320        330        340        350        360 
EDAPAIQQSP LLCSSVRPEP EAGTLSESWL LYSHPTNKKR RVDLGIYLNQ SPLEAACWSR 

       370        380        390        400        410        420 
PWILHCGPCG YSDLAALENE GLFGCLFECG TKQECEQIAF RLFTDREILS HVQGDCSTPG 


MNSEPSKK

O97859 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools