Q64627
uniprot
Q64627
canonical
amino_acid_sequence
METCPVLQKETLFHTEVYAYRIPALLYLKKQKTLLAFAEKRASRTDEHAELIVLRRGSYNGATNHVKWQPEEVVTQAQLEGHRSMNPCPLYDKQTKTLFLFFIAVPGRVSEQHQLQTRVNVTRLCRVTSTDYGMNWSPVQDLTETTIGSTHQDWATFAVGPGHCLQLRNRAGSLLVPAYAYRKLHPVHKPTPFAFCFISLDHGHTWELGNFVSENSLECQVAEVGTGAHRVVYLNARSFIGARVQAQSPNDGLDFQDNQVVSKLVEPPHGCHGSVVAFHSPTSKPDCLRHVAAYTHPTDSRNRTNLGVYLNQTPLDPTAWSEPTLLATGTCAYSDLQIWGLGPDGSPQFGCLYESGNYDEIIFLMFTLKQAFPTVHGAQ
uniprot
proteins
ec_number
3.2.1.18
uniprot
proteins
function
FUNCTION: Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan moiety in the catabolism of glycolipids, glycoproteins and oligosaccharides. Recognizes sialyl linkage positions of the glycan moiety as well as the supramolecular organization of the sialoglycoconjugate. Displays preference for alpha-(2->3)-sialylated GD1a and GT1B gangliosides over alpha-(2->8)-sialylated GD1b, in both monomeric forms and micelles. Hydrolyzes monomeric GM1 ganglioside, but has no activity toward the miscellar form. Has lower sialidase activity for glycoproteins such as fetuin and TF/transferrin that carry a mixture of alpha-(2->3) and alpha-(2->6)-sialyl linkages. Cleaves milk oligosaccharide alpha-(2->3)-sialyllactose, but is inactive toward alpha-(2->6)-sialyllactose isomer. Has no activity toward colominic acid, a homomer of alpha-(2->8)-linked Neu5Ac residues. {ECO:0000250|UniProtKB:Q9Y3R4}.
uniprot
proteins
mass_dalton
42382
uniprot
proteins
protein_family
Glycosyl hydrolase 33 family
uniprot
proteins
pubmed
8253770
uniprot
proteins
pubmed
8563137
uniprot
proteins
sequence_length
379
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y3R4}.
uniprot
proteins