ID   G1KLY3_ANOCA            Unreviewed;       407 AA.
AC   G1KLY3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 2.
DT   27-MAR-2024, entry version 67.
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 {ECO:0000313|Ensembl:ENSACAP00000011948.2};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000011948.2, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000011948.2, ECO:0000313|Proteomes:UP000001646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000011948.2,
RC   ECO:0000313|Proteomes:UP000001646};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000011948.2}
RP   IDENTIFICATION.
RG   Ensembl;
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}.
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DR   RefSeq; XP_003218036.1; XM_003217988.3.
DR   AlphaFoldDB; G1KLY3; -.
DR   STRING; 28377.ENSACAP00000011948; -.
DR   Ensembl; ENSACAT00000012192.3; ENSACAP00000011948.2; ENSACAG00000012147.3.
DR   GeneID; 100553632; -.
DR   CTD; 4758; -.
DR   eggNOG; ENOG502QSIT; Eukaryota.
DR   GeneTree; ENSGT00950000182944; -.
DR   HOGENOM; CLU_024620_3_0_1; -.
DR   InParanoid; G1KLY3; -.
DR   OrthoDB; 2900690at2759; -.
DR   TreeFam; TF331063; -.
DR   Proteomes; UP000001646; Chromosome 2.
DR   Bgee; ENSACAG00000012147; Expressed in kidney and 11 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0004308; F:exo-alpha-sialidase activity; IBA:GO_Central.
DR   GO; GO:0006689; P:ganglioside catabolic process; IBA:GO_Central.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
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:UP000001646};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          82..369
FT                   /note="Sialidase"
FT                   /evidence="ECO:0000259|Pfam:PF13088"
SQ   SEQUENCE   407 AA;  44692 MW;  35580CA152EEAC5F CRC64;
     MRAGRDPKRR SETWNSLVLS RRGFCLGGLL VLGLCCWDVL GVATPDQVKP IIAMEQLLWV
     SGSVIGEVNT FRIPLIAATP RGTLLAFSEA RKHSSSDIGA KFIALRRSQD KGATWSPTSF
     IVDDGSLADG LNLGAVAVDW EKDIVFLVYT LCAHYHQCTT ASTMIIRSRD DGVTWSVPRN
     LSEDIGTTMF APGPGYGIQK RYAPKKGRLI VCGHGTLTRD GISCLLSDDH GLTWRYGRQP
     LHGIPYGETK LLSDFNPDEC QPYELPDGSV VINARNQNFY HCSCRIVIRS YDACETLPLE
     NVTFDMTLVD PAVAAGALVK SGLVFFSNPA HERERINMTL RWSFTNGSSW WKEPLQIWSG
     ASGYSSMTAL DGSAPEDAQS LFIIYEKGRL TSTDSVSVAK ISIDGKL
//