ID L9KG35_TUPCH Unreviewed; 420 AA.
AC L9KG35;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=TREES_T100017789 {ECO:0000313|EMBL:ELW61875.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW61875.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(2013).
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 EMBL; KB320852; ELW61875.1; -; Genomic_DNA.
DR RefSeq; XP_006154359.1; XM_006154297.2.
DR AlphaFoldDB; L9KG35; -.
DR STRING; 246437.L9KG35; -.
DR GeneID; 102478896; -.
DR KEGG; tup:102478896; -.
DR CTD; 4758; -.
DR eggNOG; ENOG502QSIT; Eukaryota.
DR InParanoid; L9KG35; -.
DR OrthoDB; 2900690at2759; -.
DR Proteomes; UP000011518; Unassembled WGS sequence.
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:UP000011518};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 94..382
FT /note="Sialidase"
FT /evidence="ECO:0000259|Pfam:PF13088"
SQ SEQUENCE 420 AA; 45373 MW; 3A7640A7CD3B9AB0 CRC64;
MTGKRLDTSL PGTASRGTAW RLRALGFGAG RRVPVLAAVF PLLLCLAGFG AGAQDDFSLG
EARGTMEQLL WVSGRQIGAV DTFRIPLITA TPRGTLLAFA EARKMSASDE GAKFIALRRS
LDQGSTWSPT AFIVDDGETP DGLNLGAVVC DVETGVVFLF YTLCAHKAGC QVASTMLVWS
KDDGVSWSPP RNLSLDIGTE MFAPGPGSGI QKQREPRKGR LIVCGHGTLE RDGVYCLLSD
DHGASWRYGS GVSGIPFGQP KRENDFNPDE CQPYELPDGS VAINARNQNN YHCHCRIVLR
SYDACDTLRP RDVTFDPELV DPVVAAGAIA TSSGIVFFSN PAHPEFRVNL TLRWSFSNGT
SWQKETVQLW PGPSGYSSLA ALEGMEGGEQ GPQLYVLYEK GRNYCTESIS MVKVSVYGSL
//