ID NEUR1_PIG Reviewed; 416 AA.
AC A5PF10;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 94.
DE RecName: Full=Sialidase-1;
DE EC=3.2.1.18;
DE AltName: Full=Acetylneuraminyl hydrolase;
DE AltName: Full=Lysosomal sialidase;
DE AltName: Full=N-acetyl-alpha-neuraminidase 1;
DE Flags: Precursor;
GN Name=NEU1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
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 -!- SUBUNIT: Interacts with cathepsin A (protective protein), beta-
CC galactosidase and N-acetylgalactosamine-6-sulfate sulfatase in a
CC multienzyme complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Lumenal side {ECO:0000250}. Lysosome
CC lumen {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasmic vesicle
CC {ECO:0000250}. Note=Localized not only on the inner side of the
CC lysosomal membrane and in the lysosomal lumen, but also on the plasma
CC membrane and in intracellular vesicles. {ECO:0000250}.
CC -!- DOMAIN: A C-terminal internalization signal (YGTL) appears to allow the
CC targeting of plasma membrane proteins to endosomes. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: Phosphorylation of tyrosine within the internalization signal
CC results in inhibition of sialidase internalization and blockage on the
CC plasma membrane. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}.
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DR EMBL; AL773527; CAN87707.1; -; Genomic_DNA.
DR RefSeq; NP_001095292.1; NM_001101822.1.
DR AlphaFoldDB; A5PF10; -.
DR SMR; A5PF10; -.
DR STRING; 9823.ENSSSCP00000001513; -.
DR CAZy; GH33; Glycoside Hydrolase Family 33.
DR GlyCosmos; A5PF10; 3 sites, No reported glycans.
DR PaxDb; 9823-ENSSSCP00000001513; -.
DR PeptideAtlas; A5PF10; -.
DR Ensembl; ENSSSCT00070046815.1; ENSSSCP00070039491.1; ENSSSCG00070023485.1.
DR GeneID; 100124381; -.
DR KEGG; ssc:100124381; -.
DR CTD; 4758; -.
DR eggNOG; ENOG502QSIT; Eukaryota.
DR InParanoid; A5PF10; -.
DR OrthoDB; 2900690at2759; -.
DR Reactome; R-SSC-4085001; Sialic acid metabolism.
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR Reactome; R-SSC-9840310; Glycosphingolipid catabolism.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 7.
DR Proteomes; UP000694570; Unplaced.
DR Proteomes; UP000694571; Unplaced.
DR Proteomes; UP000694720; Unplaced.
DR Proteomes; UP000694722; Unplaced.
DR Proteomes; UP000694723; Unplaced.
DR Proteomes; UP000694724; Unplaced.
DR Proteomes; UP000694725; Unplaced.
DR Proteomes; UP000694726; Unplaced.
DR Proteomes; UP000694727; Unplaced.
DR Proteomes; UP000694728; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
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; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma 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:0004308; F:exo-alpha-sialidase activity; ISS:UniProtKB.
DR GO; GO:0006689; P:ganglioside catabolic process; IBA:GO_Central.
DR GO; GO:0009313; P:oligosaccharide catabolic process; ISS:UniProtKB.
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 Carbohydrate metabolism; Cell membrane; Cytoplasmic vesicle; Glycoprotein;
KW Glycosidase; Hydrolase; Lipid degradation; Lipid metabolism; Lysosome;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Signal.
FT SIGNAL 1..48
FT /evidence="ECO:0000250"
FT CHAIN 49..416
FT /note="Sialidase-1"
FT /id="PRO_0000304727"
FT REPEAT 113..124
FT /note="BNR 1"
FT REPEAT 173..184
FT /note="BNR 2"
FT REPEAT 232..243
FT /note="BNR 3"
FT REPEAT 348..359
FT /note="BNR 4"
FT MOTIF 78..81
FT /note="FRIP motif"
FT MOTIF 413..416
FT /note="Internalization signal"
FT ACT_SITE 104
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 371
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 395
FT /evidence="ECO:0000255"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 416 AA; 45159 MW; 65E99172C69F3EB8 CRC64;
MTAERPGAVP LGRPGRPPML GLGEAYRAQV FASIFLLLLS PAGVGARAKN DFNLVHPLVT
MEQLLWVSGK QIGSVDTFRI PLITTTPRGT LLAFAEARKM SASDKGAKFI ALRRSMDQGS
TWSPTAFIVD DGETPDGLNL GAVVSDTTTG VVFLFYSLCA HKAGCRVAST MLVWSKDDGI
SWSSPRNLSL DIGTEMFAPG PGSGIQKQWA PQKGRLIVCG HGTLERDGVF CLLSDDHGAS
WRYGSGISGI PYGQPKREND FNPDECQPYE LPDGSVVINA RNQNNYHCRC RIVLRSYDAC
DTLRPRDVTF DPELVDPVVA AGAVATSSGI IFFSNPAHPE FRVNLTLRWS FSNGTSWRKE
TVQIWPGPSG YSSLATLEGS VGGEDQAPQL YVLYEKGRNR YTESISLAKV SVYGTL
//
