NEU3
entrez
10825
canonical
uniprot
Q9UQ49
canonical
ensembl
ENSG00000162139
resolver
ensp
ENSP00000294064
resolver
ensp
ENSP00000432097
resolver
ensp
ENSP00000434474
resolver
ensp
ENSP00000434754
resolver
ensp
ENSP00000434907
resolver
ensp
ENSP00000436118
resolver
ensp
ENSP00000436540
resolver
ensp
ENSP00000645147
resolver
ensp
ENSP00000774348
resolver
ensp
ENSP00000777650
resolver
ensp
ENSP00000785387
resolver
enst
ENST00000526068
resolver
enst
ENST00000529024
resolver
enst
ENST00000531619
resolver
enst
ENST00000532963
resolver
enst
ENST00000534628
resolver
genesymbol
NEU3
resolver
hgnc
HGNC:7760
resolver
uniprot
A8K327
resolver
uniprot
B4E0V4
resolver
uniprot
E9PI40
resolver
uniprot
E9PMZ3
resolver
uniprot
E9PNK1
resolver
uniprot
E9PR25
resolver
uniprot
Q9NQE1
resolver
uniprot_entry
B4E0V4_HUMAN
resolver
uniprot_entry
E9PI40_HUMAN
resolver
uniprot_entry
E9PMZ3_HUMAN
resolver
uniprot_entry
E9PNK1_HUMAN
resolver
uniprot_entry
E9PR25_HUMAN
resolver
uniprot_entry
NEUR3_HUMAN
resolver
uniprot_sec
A8K327
resolver
uniprot_sec
Q9NQE1
resolver
amino_acid_sequence
MEEVTTCSFNSPLFRQEDDRGITYRIPALLYIPPTHTFLAFAEKRSTRRDEDALHLVLRRGLRIGQLVQWGPLKPLMEATLPGHRTMNPCPVWEQKSGCVFLFFICVRGHVTERQQIVSGRNAARLCFIYSQDAGCSWSEVRDLTEEVIGSELKHWATFAVGPGHGIQLQSGRLVIPAYTYYIPSWFFCFQLPCKTRPHSLMIYSDDLGVTWHHGRLIRPMVTVECEVAEVTGRAGHPVLYCSARTPNRCRAEALSTDHGEGFQRLALSRQLCEPPHGCQGSVVSFRPLEIPHRCQDSSSKDAPTIQQSSPGSSLRLEEEAGTPSESWLLYSHPTSRKQRVDLGIYLNQTPLEAACWSRPWILHCGPCGYSDLAALEEEGLFGCLFECGTKQECEQIAFRLFTHREILSHLQGDCTSPGRNPSQFKSN
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. Displays high catalytic efficiency for gangliosides including alpha-(2->3)-sialylated GD1a and GM3 and alpha-(2->8)-sialylated GD3 (PubMed:10405317, PubMed:10861246, PubMed:11298736, PubMed:12011038, PubMed:15847605, PubMed:20511247, PubMed:28646141). Plays a role in the regulation of transmembrane signaling through the modulation of ganglioside content of the lipid bilayer and by direct interaction with signaling receptors, such as EGFR (PubMed:17334392, PubMed:25922362). Desialylates EGFR and activates downstream signaling in proliferating cells (PubMed:25922362). Contributes to clathrin-mediated endocytosis by regulating sorting of endocytosed receptors to early and recycling endosomes (PubMed:26251452). {ECO:0000269|PubMed:10405317, ECO:0000269|PubMed:10861246, ECO:0000269|PubMed:11298736, ECO:0000269|PubMed:12011038, ECO:0000269|PubMed:15847605, ECO:0000269|PubMed:17334392, ECO:0000269|PubMed:20511247, ECO:0000269|PubMed:25922362, ECO:0000269|PubMed:26251452, ECO:0000269|PubMed:28646141}.
uniprot
proteins
mass_dalton
48252
uniprot
proteins
mutagenesis
MUTAGEN 25; /note="R->H: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:11298736"; MUTAGEN 45; /note="R->V: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:20511247"; MUTAGEN 50; /note="D->S,A: Nearly abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:20511247, ECO:0000269|PubMed:25922362"; MUTAGEN 51; /note="E->D: Decreases enzyme activity."; /evidence="ECO:0000269|PubMed:11298736"; MUTAGEN 88; /note="N->D: Markedly decreases enzyme activity."; /evidence="ECO:0000269|PubMed:11298736"; MUTAGEN 107; /note="V->M: Markedly decreases enzyme activity."; /evidence="ECO:0000269|PubMed:11298736"; MUTAGEN 114; /note="R->Q: Decreases enzyme activity."; /evidence="ECO:0000269|PubMed:11298736"; MUTAGEN 162; /note="G->A: Markedly decreases enzyme activity."; /evidence="ECO:0000269|PubMed:11298736"; MUTAGEN 179; /note="Y->F: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:20511247"; MUTAGEN 181; /note="Y->A: Markedly decreases the recruitment within caveola."; /evidence="ECO:0000269|PubMed:12011038"; MUTAGEN 181; /note="Y->F: Nearly abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:20511247"; MUTAGEN 187; /note="F->R: Decreases the recruitment within caveola."; /evidence="ECO:0000269|PubMed:12011038"; MUTAGEN 225; /note="E->S: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:20511247"; MUTAGEN 245; /note="R->A: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:20511247"; MUTAGEN 340; /note="R->A: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:20511247"; MUTAGEN 370; /note="Y->F,C: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:11298736, ECO:0000269|PubMed:20511247, ECO:0000269|PubMed:25922362
uniprot
proteins
post_translational_modification
PTM: Palmitoylated; may regulate intracellular trafficking and anchorage to plasma membrane and endomembranes. {ECO:0000269|PubMed:28646141}.
uniprot
proteins
protein_family
Glycosyl hydrolase 33 family
uniprot
proteins
pubmed
10405317
uniprot
proteins
pubmed
10861246
uniprot
proteins
pubmed
11298736
uniprot
proteins
pubmed
12011038
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15847605
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
17334392
uniprot
proteins
pubmed
17708748
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
20511247
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25922362
uniprot
proteins
pubmed
26251452
uniprot
proteins
pubmed
28646141
uniprot
proteins
sequence_length
428
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10861246, ECO:0000269|PubMed:17708748, ECO:0000269|PubMed:26251452, ECO:0000269|PubMed:28646141}; Peripheral membrane protein {ECO:0000269|PubMed:10861246, ECO:0000269|PubMed:17708748}. Membrane, caveola {ECO:0000269|PubMed:12011038}. Early endosome membrane {ECO:0000269|PubMed:26251452}; Peripheral membrane protein {ECO:0000305|PubMed:26251452}. Recycling endosome membrane {ECO:0000269|PubMed:26251452}; Peripheral membrane protein {ECO:0000305|PubMed:26251452}. Lysosome membrane {ECO:0000269|PubMed:26251452}; Peripheral membrane protein {ECO:0000305|PubMed:26251452}. Note=Associates with the external leaflet of the plasma membrane (By similarity). S-acylated NEU3 likely spans the lipid bilayer with a portion of C-terminus exposed to the cytosol and the catalytic region facing the extracellular space (PubMed:28646141). {ECO:0000250|UniProtKB:Q9JMH7, ECO:0000269|PubMed:28646141}.
uniprot
proteins