ID   Q6GMA3_XENLA            Unreviewed;       398 AA.
AC   Q6GMA3;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 89.
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   Name=neu1.L {ECO:0000313|RefSeq:NP_001086082.1,
GN   ECO:0000313|Xenbase:XB-GENE-959031};
GN   Synonyms=MGC81958 {ECO:0000313|EMBL:AAH74168.1}, neu1
GN   {ECO:0000313|RefSeq:NP_001086082.1,
GN   ECO:0000313|Xenbase:XB-GENE-959031};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH74168.1};
RN   [1] {ECO:0000313|RefSeq:NP_001086082.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAH74168.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000313|EMBL:AAH74168.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001086082.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC074168; AAH74168.1; -; mRNA.
DR   RefSeq; NP_001086082.1; NM_001092613.1.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   GeneID; 444511; -.
DR   KEGG; xla:444511; -.
DR   AGR; Xenbase:XB-GENE-959031; -.
DR   CTD; 444511; -.
DR   Xenbase; XB-GENE-959031; neu1.L.
DR   OrthoDB; 2900690at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 444511; Expressed in internal ear and 18 other cell types or tissues.
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   2: Evidence at transcript level;
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          75..364
FT                   /note="Sialidase"
FT                   /evidence="ECO:0000259|Pfam:PF13088"
SQ   SEQUENCE   398 AA;  43983 MW;  489FDCAEECEDFC8C CRC64;
     MEKQHHEAAV SRNWKCVIRV WLVLVLPALF SLGRSAPYKQ VAPIVTMEQL LWVSGRVIGE
     VDTFRIPIIT YTPRGHLIAF SEARKHSASD LGAKFIASRR SQDGGYTWTP TSFIVDDGSA
     DDGLNLGSVV VDNETGGIFI VYTLCAHYIR CSVSSLMITN SSDDGLTWSP PRNLSHEIGT
     KMFAPGPGYG IQKMYAPNKG RLIVCGHGTL DEDGVFCLLS DDHGSNWRKG GSLQGLPFNQ
     KKRLGDFSPD ECQPYELPDG TVVVNARNQY FYHCHCRIVV YSTDGCDSLP LENVRFDEGL
     PDPAVAAGAL YKGGVVYFTN PANLNHRVNL TLRWSLNSGI SWEQESIQIW PGPSGYSSLT
     TLSNNVEDNE NIFVVYEKGR EDITESIALV KINLYGLL
//