LinkDB: NEUR1_PIG B9TSS6_PIG
Original site: NEUR1_PIG B9TSS6_PIG
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}. 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; 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 //
ID B9TSS6_PIG Unreviewed; 416 AA. AC B9TSS6; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 24-JAN-2024, entry version 66. 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|EMBL:ABX82833.1}; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823 {ECO:0000313|EMBL:ABX82833.1}; RN [1] {ECO:0000313|EMBL:ABX82833.1} RP NUCLEOTIDE SEQUENCE. RA Kim J.H., Jeon J.T.; RT "Identification of single-nucleotide polymorphisms in coding sequences of RT genes in the SLA class III region by direct sequencing."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:HDB98474.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=30723633; DOI=.7717/peerj.6374; RA Gilbert D.G.; RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene."; RL PeerJ 7:E6374-E6374(2019). 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; EU282367; ABX82833.1; -; mRNA. DR EMBL; DQIR01242997; HDB98474.1; -; Transcribed_RNA. DR RefSeq; NP_001095292.1; NM_001101822.1. DR AlphaFoldDB; B9TSS6; -. DR SMR; B9TSS6; -. DR CAZy; GH33; Glycoside Hydrolase Family 33. DR GeneID; 100124381; -. DR KEGG; ssc:100124381; -. DR CTD; 4758; -. DR OrthoDB; 2900690at2759; -. DR Genevisible; B9TSS6; SS. 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 Signal {ECO:0000256|ARBA:ARBA00022729}. FT DOMAIN 89..378 FT /note="Sialidase" FT /evidence="ECO:0000259|Pfam:PF13088" 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 //