P82450
uniprot
P82450
canonical
activity_regulation
ACTIVITY REGULATION: Inhibited by diisopropyl fluorophosphate and diethyl-P-nitrophenyl phosphate.
uniprot
proteins
amino_acid_sequence
MVSPRPVGLMLLLIIARVSRGAGIGFRFASYIDNYMVLQKEPSGAVIWGFGTAGATVTVTLCQGQETIMKKVTSVKGPSNTWMVVLDPMKPGGPFEVMAQQTLETTNLTLRVHDVLFGDVWLCSGQSNMQMTVLQIFNASKELSDTAAYQSVRIFSVSLTQAEEELADLDGVDLSWSKPTAGNLGHGNFTYMSAVCWLFGRYLYDTLQYPIGLVSSSWGGTPIEVWSSRRALKACGVPNTRDERVLQPEIKPMRNGCESKESSCPFRRFVPCDPVAGPATHSVLWNAMIHPLQNMTLKGVVWYQGENNANYNRDLYACMFPALIAGWRQTFHSGCQGQTERFFPFGFVQLSSYLLMNSSDYGFPEIRWHQTADFGSVPNPKMPNTFMAVAMDLCDRDSPFGSIHPRDKQTVAYRLHLGARAVAYGEKNLTFQGPLPKKIELLARNELLNLTYDQEIQVQRKDNKTFEISCCSDHQCKWLPAPVNTFSTQTLILDLSACLGTVDAVRYAWTTWPCEYKQCAVYHTSSVLPAPPFTARITHRGI
uniprot
proteins
ec_number
3.1.1.53
uniprot
proteins
function
FUNCTION: Catalyzes the removal of O-acetyl ester groups from position 9 of the free diacetylated sialate N-acetyl-9-O-acetylneuraminate (Neu5,9Ac2) in the cytosol and of the diacetylated sialate residues of sialylglycoconjugates in the lysosomes (Probable). Together with the sialate-O-acetyltransferase they regulate the balance of acetylated sialoglycoconjugates, key players in various processes such as cell-cell interactions, host-pathogen recognition, and tumor antigenicity (By similarity). {ECO:0000250|UniProtKB:P70665, ECO:0000305|PubMed:2808434}.
uniprot
proteins
mass_dalton
60466
uniprot
proteins
post_translational_modification
PTM: The two subunits are derived from a single precursor by proteolytic cleavage.; PTM: Glycosylated.
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
2808434
uniprot
proteins
pubmed
8486688
uniprot
proteins
sequence_length
542
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome.
uniprot
proteins