ID A0A0Q3PIC0_AMAAE Unreviewed; 150 AA.
AC A0A0Q3PIC0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Sialidase-1 {ECO:0000256|ARBA:ARBA00040509};
DE EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
DE AltName: Full=Lysosomal sialidase {ECO:0000256|ARBA:ARBA00041413};
DE AltName: Full=N-acetyl-alpha-neuraminidase 1 {ECO:0000256|ARBA:ARBA00041332};
GN ORFNames=AAES_139072 {ECO:0000313|EMBL:KQK76060.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK76060.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK76060.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK76060.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic
CC acid) moieties from glycoproteins and glycolipids. To be active, it is
CC strictly dependent on its presence in the multienzyme complex. Appears
CC to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage.
CC {ECO:0000256|ARBA:ARBA00037235}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-
CC (2->8)- glycosidic linkages of terminal sialic acid residues in
CC oligosaccharides, glycoproteins, glycolipids, colominic acid and
CC synthetic substrates.; EC=3.2.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00000427};
CC -!- SUBUNIT: Interacts with cathepsin A (protective protein), beta-
CC galactosidase and N-acetylgalactosamine-6-sulfate sulfatase in a
CC multienzyme complex. {ECO:0000256|ARBA:ARBA00038519}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000256|ARBA:ARBA00004541}. Lysosome lumen
CC {ECO:0000256|ARBA:ARBA00004227}. Lysosome membrane
CC {ECO:0000256|ARBA:ARBA00004207}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004207}; Lumenal side
CC {ECO:0000256|ARBA:ARBA00004207}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC {ECO:0000256|ARBA:ARBA00009348}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQK76060.1}.
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DR EMBL; LMAW01002883; KQK76060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q3PIC0; -.
DR STRING; 12930.A0A0Q3PIC0; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.120.10.10; -; 1.
DR InterPro; IPR011040; Sialidase.
DR InterPro; IPR026856; Sialidase_fam.
DR InterPro; IPR036278; Sialidase_sf.
DR PANTHER; PTHR10628; SIALIDASE; 1.
DR PANTHER; PTHR10628:SF25; SIALIDASE-1; 1.
DR Pfam; PF13088; BNR_2; 1.
DR SUPFAM; SSF50939; Sialidases; 1.
PE 3: Inferred from homology;
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 3..111
FT /note="Sialidase"
FT /evidence="ECO:0000259|Pfam:PF13088"
SQ SEQUENCE 150 AA; 16211 MW; 578E9AF5FAEEAD23 CRC64;
MDPQPYELPD GSIAINIRNQ NSYRCRCRMV ARSWDGGETL PPTAVTFDPS LVDPAVAAGV
LVTGDLVFFS NPAHESQRVN LTLRWSFTNG TTWWGRGLRV WAGPSGYSSM AAPPPGSQGH
APFLYLIYEK GRNLSTESIS LATISIAGGP
//
