ID H3AXU1_LATCH Unreviewed; 381 AA.
AC H3AXU1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=NEU2 {ECO:0000313|Ensembl:ENSLACP00000014462.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000014462.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000014462.1}
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 EMBL; AFYH01137725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01137726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01137727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01137728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01137729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3AXU1; -.
DR STRING; 7897.ENSLACP00000014462; -.
DR Ensembl; ENSLACT00000014562.1; ENSLACP00000014462.1; ENSLACG00000012725.2.
DR eggNOG; ENOG502QSFT; Eukaryota.
DR GeneTree; ENSGT00950000182944; -.
DR InParanoid; H3AXU1; -.
DR OMA; NEYAVEC; -.
DR TreeFam; TF331063; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000012725; Expressed in post-anal tail muscle and 6 other cell types or tissues.
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:UP000008672};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 46..336
FT /note="Sialidase"
FT /evidence="ECO:0000259|Pfam:PF13088"
SQ SEQUENCE 381 AA; 42816 MW; 540C0A3DCE41E491 CRC64;
MHSVLHLQQQ PLFRKGEKAY RIPALLYLSQ SSEFLAFAEE RADLVDEHAE RLVVSRGRFD
NDRFFAEWDS PERIASARLP DHRSMNPCPI YDRKTQTIFL FFIAVKGTTS EAQQINAKRN
ATRLCYVTSM DMGKTWSSAM DLTEPAVGQT YSKWATFAIG PGHGVQLQNS TESLVVPAYA
YWIHSATERP KPKAFCFISH DHGKTWSIGH CIPNEYAVEC QMASIEVDGK QFLYCNARSL
GSRVQAVSHD GGGKFEKGHR ASNLVEPPHG CQGSIVGFPE PGPSQAAKTW MLFSHPTDEN
KRRDLGIYLN QSPRDHTSWT APIIIHHGPC AYSDLQYLGL NSEGYPAFAC LFECGKQLEY
EEIAFVLFTL KLLFPALFVG Q
//
