ID   Q3UL64_MOUSE            Unreviewed;       409 AA.
AC   Q3UL64;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 148.
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}.
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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:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal 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: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   Repeat {ECO:0000256|ARBA:ARBA00022737};
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
//