ID NEUR1_BOVIN Reviewed; 415 AA. AC A6BMK7; A4IFG6; Q5D0G1; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 2. DT 24-JAN-2024, entry version 106. 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 Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Masoudi A.A., Yamato O., Kunieda T.; RT "Evaluation of PPGB and NEU1 genes as candidates for the lysosomal storage RT disorder in Japanese black cattle."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Basal ganglia; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 54-205. RA Heaton M.P., Clawson M.L., Snelling W.M., Keele J.W., Harhay G.P., RA Wiedmann R.T., Bennett G.L., Smith T.P.L., Stone R.T., Freking B.A., RA Van Tassell C.P., Sonstegard T.S., Gasbarre L.C., Carr J., DiBello P., RA Kumar M., Lee M.S., Murthy J., Otto J., Salisbury B., Schulz V., Tracy R., RA Hawk D.A., Kalbfleisch T., Laegreid W.W.; RT "Estimating probability of parentage in U.S. beef and dairy cattle with RT single nucleotide polymorphisms."; RL Submitted (FEB-2005) 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; AB327106; BAF64705.1; -; Genomic_DNA. DR EMBL; BC134571; AAI34572.1; -; mRNA. DR EMBL; AY937242; AAX14675.1; -; Genomic_DNA. DR RefSeq; NP_001077111.1; NM_001083642.1. DR AlphaFoldDB; A6BMK7; -. DR SMR; A6BMK7; -. DR STRING; 9913.ENSBTAP00000073421; -. DR CAZy; GH33; Glycoside Hydrolase Family 33. DR GlyCosmos; A6BMK7; 3 sites, No reported glycans. DR PaxDb; 9913-ENSBTAP00000007454; -. DR Ensembl; ENSBTAT00000007454.5; ENSBTAP00000007454.4; ENSBTAG00000005674.5. DR GeneID; 505554; -. DR KEGG; bta:505554; -. DR CTD; 4758; -. DR VEuPathDB; HostDB:ENSBTAG00000005674; -. DR VGNC; VGNC:50230; NEU1. DR eggNOG; ENOG502QSIT; Eukaryota. DR GeneTree; ENSGT00950000182944; -. DR HOGENOM; CLU_024620_3_0_1; -. DR InParanoid; A6BMK7; -. DR OrthoDB; 2900690at2759; -. DR TreeFam; TF331063; -. DR Reactome; R-BTA-4085001; Sialic acid metabolism. DR Reactome; R-BTA-6798695; Neutrophil degranulation. DR Reactome; R-BTA-9840310; Glycosphingolipid catabolism. DR Proteomes; UP000009136; Chromosome 23. DR Bgee; ENSBTAG00000005674; Expressed in ileocecal valve and 105 other cell types or tissues. DR ExpressionAtlas; A6BMK7; baseline and differential. 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 2: Evidence at transcript level; 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..47 FT /evidence="ECO:0000250" FT CHAIN 48..415 FT /note="Sialidase-1" FT /id="PRO_0000304726" FT REPEAT 112..123 FT /note="BNR 1" FT REPEAT 172..183 FT /note="BNR 2" FT REPEAT 231..242 FT /note="BNR 3" FT REPEAT 347..358 FT /note="BNR 4" FT MOTIF 77..80 FT /note="FRIP motif" FT MOTIF 412..415 FT /note="Internalization signal" FT ACT_SITE 103 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 370 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 394 FT /evidence="ECO:0000255" FT BINDING 78 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 97 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 264 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 280 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 341 FT /ligand="substrate" FT /evidence="ECO:0000250" FT CARBOHYD 186 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 343 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 352 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 410 FT /note="S -> G (in Ref. 1; BAF64705)" FT /evidence="ECO:0000305" SQ SEQUENCE 415 AA; 45433 MW; F670909AF7046428 CRC64; MTEEGPGIVS LGKLRRPRML RLWGICRVQI FSAIFMLMSP AGVGAGAKDD FSLVHPLVTM EQLLWVSGKQ IGSVDTFRIP LITTTPRGTL LAFAEARKMS TSDKGAKFIA LRRSMDQGST WSPTAFIVDD GETPDGLNLG AVVSDTTTGV VFLFYSLCAH KAGCQVASTM LVWSKDDGVS WSSPRNLSLD IGTEMFAPGP GSGIQKQREP RKGRLIVCGH GTLERDGVFC LLSDDHGVSW RYGGGVSGIP YGQPKRENDF NPDECQPYEL PDGSVVINAR NQNNYHCHCR IILRSYDACD TLRPRDVTFD TELVDPVVAA GAVATSSGIV FFSNPAHPEF RVNLTLRWSF SNGTSWRKET VQLWPGPSGY SSLTTLEGNV DGKDEAPQLY VLYEKGRNQY MESISLVKVS VYGTL //