ID   A0A2K5J8J2_COLAP        Unreviewed;       416 AA.
AC   A0A2K5J8J2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
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};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000025086.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000025086.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_011800140.1; XM_011944750.1.
DR   AlphaFoldDB; A0A2K5J8J2; -.
DR   STRING; 336983.ENSCANP00000025086; -.
DR   Ensembl; ENSCANT00000048085.1; ENSCANP00000025086.1; ENSCANG00000035966.1.
DR   GeneID; 105513761; -.
DR   KEGG; cang:105513761; -.
DR   CTD; 4758; -.
DR   OMA; IRSYDAC; -.
DR   OrthoDB; 551961at2759; -.
DR   Proteomes; UP000233080; Unplaced.
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:UP000233080};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          89..378
FT                   /note="Sialidase"
FT                   /evidence="ECO:0000259|Pfam:PF13088"
SQ   SEQUENCE   416 AA;  45723 MW;  B1342564A3F9D2B3 CRC64;
     MAGERPGTAL RRRRWGPRIL GFWGGCRVRV FAAIFLLLLS LADSWSRAEN DFGLVQPLVT
     MEQLLWVSGR QIGSVDTFRI PLITATPRGT LLAFAEARKM SSSDEGAKFI ALRRSMDQGS
     TWSPTAFIVN DGDVPDGLNL GAVVSDVETG VVFLFYSLCA HKAGCQVAST MLVWSKDDGV
     SWSTPRNLSL DIGTEVFAPG PGSGIQKQRE PRKGRLIVCG HGTLERDGVF CLLSDDHGAS
     WRYGSGVSGI PYGQPKREND FNPDECQPYE LPDGSVVINA RNQNNYHCHC RIVLRSYDAC
     DTLRPRDVTF DPELVDPVVA AGAVVTSSGI VFFSNPAHPE FRVNLTLRWS FSNGTSWRKE
     TVQLWPGPSG YSSLATLEGS MDGEEQAPQL YVLYEKGRNH YTESISMAKI SVYGTL
//