LinkDB: NEUR1_MOUSE Q3UL64_MOUSE
Original site: NEUR1_MOUSE Q3UL64_MOUSE
ID NEUR1_MOUSE Reviewed; 409 AA. AC O35657; O55220; Q99KG9; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 24-JAN-2024, entry version 190. DE RecName: Full=Sialidase-1; DE EC=3.2.1.18; DE AltName: Full=G9 sialidase; DE AltName: Full=Lysosomal sialidase; DE AltName: Full=N-acetyl-alpha-neuraminidase 1; DE Flags: Precursor; GN Name=Neu1; Synonyms=Neu; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND FUNCTION. RC STRAIN=C57BL/RIJ; RX PubMed=9363440; DOI=10.1093/glycob/7.7.975; RA Carrillo M.B., Milner C.M., Ball S.T., Snoek M., Campbell R.D.; RT "Cloning and characterization of a sialidase from the murine RT histocompatibility-2 complex: low levels of mRNA and a single amino acid RT mutation are responsible for reduced sialidase activity in mice carrying RT the Neu1a allele."; RL Glycobiology 7:975-986(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6J; RX PubMed=9384611; DOI=10.1093/hmg/7.1.115; RA Igdoura S.A., Gafuik C., Mertineit C., Saberi F., Pshezhetsky A.V., RA Potier M., Trasler J.M., Gravel R.A.; RT "Cloning of the cDNA and gene encoding mouse lysosomal sialidase and RT correction of sialidase deficiency in human sialidosis and mouse SM/J RT fibroblasts."; RL Hum. Mol. Genet. 7:115-121(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=129; RX PubMed=14656967; DOI=10.1101/gr.1736803; RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., RA Hood L.; RT "Analysis of the gene-dense major histocompatibility complex class III RT region and its comparison to mouse."; RL Genome Res. 13:2621-2636(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Kidney; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [6] RP VARIANT ILE-209. RX PubMed=9425240; DOI=10.1093/hmg/7.2.313; RA Rottier R.J., Bonten E.J., d'Azzo A.; RT "A point mutation in the neu-1 locus causes the neuraminidase defect in the RT SM/J mouse."; RL Hum. Mol. Genet. 7:313-321(1998). 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:0000269|PubMed:9363440, ECO:0000269|PubMed:9384611}. 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:0000269|PubMed:9363440, ECO:0000269|PubMed:9384611}; CC -!- SUBUNIT: Interacts with cathepsin A (protective protein), beta- CC galactosidase and N-acetylgalactosamine-6-sulfate sulfatase in a CC multienzyme complex. CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:9384611}; CC Peripheral membrane protein {ECO:0000269|PubMed:9384611}; Lumenal side CC {ECO:0000269|PubMed:9384611}. Lysosome lumen CC {ECO:0000269|PubMed:9384611}. Cell membrane CC {ECO:0000269|PubMed:9384611}. Cytoplasmic vesicle CC {ECO:0000269|PubMed:9384611}. Note=Localized not only on the inner side CC of the lysosomal membrane and in the lysosomal lumen, but also on the CC plasma membrane and in intracellular vesicles. CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, epididymis, followed by CC brain, spinal cord and weakly expressed in adrenal, heart, liver, lung CC and spleen. {ECO:0000269|PubMed:9384611}. CC -!- DOMAIN: A C-terminal internalization signal (YGTL) appears to allow the CC targeting of plasma membrane proteins to endosomes. CC -!- PTM: N-glycosylated. {ECO:0000305}. CC -!- PTM: Phosphorylation of tyrosine within the internalization signal CC results in inhibition of sialidase internalization and blockage on the CC plasma membrane. 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; Y11412; CAA72215.1; -; mRNA. DR EMBL; U93702; AAC53536.1; -; mRNA. DR EMBL; AF109906; AAC84167.1; -; Genomic_DNA. DR EMBL; BC004666; AAH04666.1; -; mRNA. DR CCDS; CCDS28668.1; -. DR RefSeq; NP_035023.3; NM_010893.3. DR PDB; 8DU5; X-ray; 3.50 A; A/B=42-409. DR PDBsum; 8DU5; -. DR AlphaFoldDB; O35657; -. DR SMR; O35657; -. DR BioGRID; 201731; 1. DR IntAct; O35657; 2. DR STRING; 10090.ENSMUSP00000007253; -. DR ChEMBL; CHEMBL4105926; -. DR CAZy; GH33; Glycoside Hydrolase Family 33. DR GlyConnect; 2710; 1 N-Linked glycan (1 site). DR GlyCosmos; O35657; 4 sites, 1 glycan. DR GlyGen; O35657; 4 sites, 1 N-linked glycan (1 site). DR iPTMnet; O35657; -. DR PhosphoSitePlus; O35657; -. DR SwissPalm; O35657; -. DR EPD; O35657; -. DR PaxDb; 10090-ENSMUSP00000007253; -. DR PeptideAtlas; O35657; -. DR ProteomicsDB; 287388; -. DR Pumba; O35657; -. DR Antibodypedia; 51599; 437 antibodies from 27 providers. DR DNASU; 18010; -. DR Ensembl; ENSMUST00000007253.6; ENSMUSP00000007253.6; ENSMUSG00000007038.6. DR GeneID; 18010; -. DR KEGG; mmu:18010; -. DR UCSC; uc008cei.2; mouse. DR AGR; MGI:97305; -. DR CTD; 4758; -. DR MGI; MGI:97305; Neu1. DR VEuPathDB; HostDB:ENSMUSG00000007038; -. DR eggNOG; ENOG502QSIT; Eukaryota. DR GeneTree; ENSGT00950000182944; -. DR HOGENOM; CLU_024620_3_0_1; -. DR InParanoid; O35657; -. DR OMA; IRSYDAC; -. DR OrthoDB; 2900690at2759; -. DR PhylomeDB; O35657; -. DR TreeFam; TF331063; -. DR BRENDA; 3.2.1.18; 3474. DR Reactome; R-MMU-4085001; Sialic acid metabolism. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR Reactome; R-MMU-9840310; Glycosphingolipid catabolism. DR BioGRID-ORCS; 18010; 4 hits in 85 CRISPR screens. DR ChiTaRS; Neu1; mouse. DR PRO; PR:O35657; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; O35657; Protein. DR Bgee; ENSMUSG00000007038; Expressed in right kidney and 234 other cell types or tissues. DR ExpressionAtlas; O35657; baseline and differential. DR Genevisible; O35657; MM. DR GO; GO:0030054; C:cell junction; ISO:MGI. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. 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; IDA:MGI. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016997; F:alpha-sialidase activity; ISO:MGI. 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; IDA:MGI. DR GO; GO:0006689; P:ganglioside catabolic process; IBA:GO_Central. DR GO; GO:0009313; P:oligosaccharide catabolic process; ISS:UniProtKB. DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI. DR GO; GO:2000291; P:regulation of myoblast proliferation; ISO:MGI. 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 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cell membrane; Cytoplasmic vesicle; KW Glycoprotein; Glycosidase; Hydrolase; Lipid degradation; Lipid metabolism; KW Lysosome; Membrane; Phosphoprotein; Reference proteome; Repeat; Signal. FT SIGNAL 1..41 FT /evidence="ECO:0000255" FT CHAIN 42..409 FT /note="Sialidase-1" FT /id="PRO_0000012027" FT REPEAT 106..117 FT /note="BNR 1" FT REPEAT 166..177 FT /note="BNR 2" FT REPEAT 225..236 FT /note="BNR 3" FT REPEAT 341..352 FT /note="BNR 4" FT MOTIF 71..74 FT /note="FRIP motif" FT MOTIF 406..409 FT /note="Internalization signal" FT ACT_SITE 97 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 258 FT /evidence="ECO:0000255" FT ACT_SITE 364 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 388 FT /evidence="ECO:0000255" FT BINDING 72 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 91 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 258 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 274 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 335 FT /ligand="substrate" FT /evidence="ECO:0000250" FT CARBOHYD 180 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 337 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 346 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 372 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 209 FT /note="L -> I (reduced activity)" FT /evidence="ECO:0000269|PubMed:9425240" FT CONFLICT 107 FT /note="R -> K (in Ref. 2; AAC53536)" FT /evidence="ECO:0000305" FT CONFLICT 113 FT /note="S -> C (in Ref. 2; AAC53536)" FT /evidence="ECO:0000305" FT CONFLICT 117..121 FT /note="STAFI -> PTGFM (in Ref. 2; AAC53536)" FT /evidence="ECO:0000305" FT CONFLICT 172..173 FT /note="GI -> AF (in Ref. 2; AAC53536)" FT /evidence="ECO:0000305" FT CONFLICT 344 FT /note="F -> L (in Ref. 2; AAC53536)" FT /evidence="ECO:0000305" FT CONFLICT 351 FT /note="Q -> L (in Ref. 4; AAH04666)" FT /evidence="ECO:0000305" SQ SEQUENCE 409 AA; 44591 MW; 416BFD5BE27B8893 CRC64; MVGADPTRPR GPLSYWAGRR GQGLAAIFLL LVSAAESEAR AEDDFSLVQP LVTMEQLLWV SGKQIGSVDT FRIPLITATP RGTLLAFAEA RKKSASDEGA KFIAMRRSTD QGSTWSSTAF IVDDGEASDG LNLGAVVNDV DTGIVFLIYT LCAHKVNCQV ASTMLVWSKD DGISWSPPRN LSVDIGTEMF APGPGSGIQK QREPGKGRLI VCGHGTLERD GVFCLLSDDH GASWHYGTGV SGIPFGQPKH DHDFNPDECQ PYELPDGSVI INARNQNNYH CRCRIVLRSY DACDTLRPRD VTFDPELVDP VVAAGALATS SGIVFFSNPA HPEFRVNLTL RWSFSNGTSW QKERVQVWPG PSGYSSLTAL ENSTDGKKQP PQLFVLYEKG LNRYTESISM VKISVYGTL //
Ontology (20) GO (19) CAZY (1) Drug (1) CHEMBL-UP (1) Chemical reaction (1) KEGG ENZYME (1) Gene (6) KEGG GENES (1) NCBI-Gene (1) ENSEMBL-UP (3) MGI-MMU (1) Protein sequence (1) RefSeq(pep) (1) DNA sequence (4) EMBL (4) 3D Structure (1) PDB (1) Protein domain (4) InterPro (3) Pfam (1) Literature (6) PubMed (6) Enzyme (1) BRENDA (1) All databases (45)
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ID Q3UL64_MOUSE Unreviewed; 409 AA. AC Q3UL64; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 24-JAN-2024, entry version 147. 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|MGI:MGI:97305}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAE26586.1}; RN [1] {ECO:0000313|EMBL:BAE26586.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE26586.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [2] {ECO:0000313|EMBL:BAE26586.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE26586.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare RT full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] {ECO:0000313|EMBL:BAE26586.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE26586.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N., RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R., RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S., RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y., RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y., RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing RT pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] {ECO:0000313|EMBL:BAE26586.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE26586.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [5] {ECO:0000313|EMBL:BAE26586.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE26586.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [6] {ECO:0000313|EMBL:BAE26586.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE26586.1}; RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F., RA Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M., RA Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K., RA Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T., RA Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:BAE26586.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE26586.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [8] {ECO:0000313|EMBL:BAE26586.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE26586.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). RN [9] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). 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; AK145680; BAE26586.1; -; mRNA. DR RefSeq; NP_035023.3; NM_010893.3. DR AlphaFoldDB; Q3UL64; -. DR SMR; Q3UL64; -. DR CAZy; GH33; Glycoside Hydrolase Family 33. DR EPD; Q3UL64; -. DR MaxQB; Q3UL64; -. DR Antibodypedia; 51599; 437 antibodies from 27 providers. DR DNASU; 18010; -. DR GeneID; 18010; -. DR KEGG; mmu:18010; -. DR AGR; MGI:97305; -. DR CTD; 4758; -. DR MGI; MGI:97305; Neu1. DR VEuPathDB; HostDB:ENSMUSG00000007038; -. DR HOGENOM; CLU_024620_3_0_1; -. DR OMA; IRSYDAC; -. DR OrthoDB; 2900690at2759; -. DR PhylomeDB; Q3UL64; -. DR BioGRID-ORCS; 18010; 4 hits in 85 CRISPR screens. DR ChiTaRS; Neu1; mouse. DR ExpressionAtlas; Q3UL64; baseline and differential. DR GO; GO:0030054; C:cell junction; IEA:Ensembl. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. 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 GO; GO:0009313; P:oligosaccharide catabolic process; IEA:Ensembl. 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 1: Evidence at protein level; KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..41 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 42..409 FT /note="Sialidase-1" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5014309168" FT DOMAIN 82..372 FT /note="Sialidase" FT /evidence="ECO:0000259|Pfam:PF13088" SQ SEQUENCE 409 AA; 44591 MW; 416BFD5BE27B8893 CRC64; MVGADPTRPR GPLSYWAGRR GQGLAAIFLL LVSAAESEAR AEDDFSLVQP LVTMEQLLWV SGKQIGSVDT FRIPLITATP RGTLLAFAEA RKKSASDEGA KFIAMRRSTD QGSTWSSTAF IVDDGEASDG LNLGAVVNDV DTGIVFLIYT LCAHKVNCQV ASTMLVWSKD DGISWSPPRN LSVDIGTEMF APGPGSGIQK QREPGKGRLI VCGHGTLERD GVFCLLSDDH GASWHYGTGV SGIPFGQPKH DHDFNPDECQ PYELPDGSVI INARNQNNYH CRCRIVLRSY DACDTLRPRD VTFDPELVDP VVAAGALATS SGIVFFSNPA HPEFRVNLTL RWSFSNGTSW QKERVQVWPG PSGYSSLTAL ENSTDGKKQP PQLFVLYEKG LNRYTESISM VKISVYGTL //