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O35657

- NEUR1_MOUSE

UniProt

O35657 - NEUR1_MOUSE

Protein

Sialidase-1

Gene

Neu1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moities from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage.2 Publications

    Catalytic activityi

    Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei72 – 721SubstrateBy similarity
    Binding sitei91 – 911SubstrateBy similarity
    Active sitei97 – 971Proton acceptorBy similarity
    Active sitei258 – 2581Sequence Analysis
    Binding sitei258 – 2581SubstrateBy similarity
    Binding sitei274 – 2741SubstrateBy similarity
    Binding sitei335 – 3351SubstrateBy similarity
    Active sitei364 – 3641NucleophileBy similarity
    Active sitei388 – 3881Sequence Analysis

    GO - Molecular functioni

    1. exo-alpha-(2->3)-sialidase activity Source: UniProtKB-EC
    2. exo-alpha-(2->6)-sialidase activity Source: UniProtKB-EC
    3. exo-alpha-(2->8)-sialidase activity Source: UniProtKB-EC
    4. exo-alpha-sialidase activity Source: MGI
    5. protein binding Source: MGI

    GO - Biological processi

    1. lipid catabolic process Source: UniProtKB-KW
    2. oligosaccharide catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Lipid degradation, Lipid metabolism

    Enzyme and pathway databases

    ReactomeiREACT_199008. Glycosphingolipid metabolism.
    REACT_202500. Sialic acid metabolism.

    Protein family/group databases

    CAZyiGH33. Glycoside Hydrolase Family 33.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sialidase-1 (EC:3.2.1.18)
    Alternative name(s):
    G9 sialidase
    Lysosomal sialidase
    N-acetyl-alpha-neuraminidase 1
    Gene namesi
    Name:Neu1
    Synonyms:Neu
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:97305. Neu1.

    Subcellular locationi

    Lysosome membrane 1 Publication; Peripheral membrane protein 1 Publication; Lumenal side 1 Publication. Lysosome lumen 1 Publication. Cell membrane 1 Publication. Cytoplasmic vesicle 1 Publication
    Note: Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but also on the plasma membrane and in intracellular vesicles.

    GO - Cellular componenti

    1. cell junction Source: Ensembl
    2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    3. lysosomal lumen Source: UniProtKB-SubCell
    4. lysosomal membrane Source: UniProtKB-SubCell
    5. lysosome Source: MGI
    6. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4141Sequence AnalysisAdd
    BLAST
    Chaini42 – 409368Sialidase-1PRO_0000012027Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi346 – 3461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi372 – 3721N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.Curated
    Phosphorylation of tyrosine within the internalization signal results in inhibition of sialidase internalization and blockage on the plasma membrane.

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiO35657.
    PaxDbiO35657.
    PRIDEiO35657.

    PTM databases

    PhosphoSiteiO35657.

    Expressioni

    Tissue specificityi

    Highly expressed in kidney, epididymis, followed by brain, spinal cord and weakly expressed in adrenal, heart, liver, lung and spleen.1 Publication

    Gene expression databases

    ArrayExpressiO35657.
    BgeeiO35657.
    CleanExiMM_NEU1.
    GenevestigatoriO35657.

    Interactioni

    Subunit structurei

    Interacts with cathepsin A (protective protein), beta-galactosidase and N-acetylgalactosamine-6-sulfate sulfatase in a multienzyme complex.

    Protein-protein interaction databases

    BioGridi201731. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliO35657.
    SMRiO35657. Positions 49-390.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati106 – 11712BNR 1Add
    BLAST
    Repeati166 – 17712BNR 2Add
    BLAST
    Repeati225 – 23612BNR 3Add
    BLAST
    Repeati341 – 35212BNR 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi71 – 744FRIP motif
    Motifi406 – 4094Internalization signal

    Domaini

    A C-terminal internalization signal (YGTL) appears to allow the targeting of plasma membrane proteins to endosomes.

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 33 family.Curated
    Contains 4 BNR repeats.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG4409.
    HOGENOMiHOG000007651.
    HOVERGENiHBG057314.
    InParanoidiO35657.
    KOiK01186.
    OMAiGTEMFAP.
    OrthoDBiEOG779NXT.
    PhylomeDBiO35657.
    TreeFamiTF331063.

    Family and domain databases

    Gene3Di2.120.10.10. 1 hit.
    InterProiIPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    [Graphical view]
    PANTHERiPTHR10628. PTHR10628. 1 hit.
    SUPFAMiSSF50939. SSF50939. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O35657-1 [UniParc]FASTAAdd to Basket

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    MVGADPTRPR GPLSYWAGRR GQGLAAIFLL LVSAAESEAR AEDDFSLVQP    50
    LVTMEQLLWV SGKQIGSVDT FRIPLITATP RGTLLAFAEA RKKSASDEGA 100
    KFIAMRRSTD QGSTWSSTAF IVDDGEASDG LNLGAVVNDV DTGIVFLIYT 150
    LCAHKVNCQV ASTMLVWSKD DGISWSPPRN LSVDIGTEMF APGPGSGIQK 200
    QREPGKGRLI VCGHGTLERD GVFCLLSDDH GASWHYGTGV SGIPFGQPKH 250
    DHDFNPDECQ PYELPDGSVI INARNQNNYH CRCRIVLRSY DACDTLRPRD 300
    VTFDPELVDP VVAAGALATS SGIVFFSNPA HPEFRVNLTL RWSFSNGTSW 350
    QKERVQVWPG PSGYSSLTAL ENSTDGKKQP PQLFVLYEKG LNRYTESISM 400
    VKISVYGTL 409
    Length:409
    Mass (Da):44,591
    Last modified:January 1, 1998 - v1
    Checksum:i416BFD5BE27B8893
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti107 – 1071R → K in AAC53536. (PubMed:9384611)Curated
    Sequence conflicti113 – 1131S → C in AAC53536. (PubMed:9384611)Curated
    Sequence conflicti117 – 1215STAFI → PTGFM in AAC53536. (PubMed:9384611)Curated
    Sequence conflicti172 – 1732GI → AF in AAC53536. (PubMed:9384611)Curated
    Sequence conflicti344 – 3441F → L in AAC53536. (PubMed:9384611)Curated
    Sequence conflicti351 – 3511Q → L in AAH04666. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti209 – 2091L → I Reduced activity. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11412 mRNA. Translation: CAA72215.1.
    U93702 mRNA. Translation: AAC53536.1.
    AF109906 Genomic DNA. Translation: AAC84167.1.
    BC004666 mRNA. Translation: AAH04666.1.
    CCDSiCCDS28668.1.
    RefSeqiNP_035023.3. NM_010893.3.
    UniGeneiMm.8856.

    Genome annotation databases

    EnsembliENSMUST00000007253; ENSMUSP00000007253; ENSMUSG00000007038.
    GeneIDi18010.
    KEGGimmu:18010.
    UCSCiuc008cei.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11412 mRNA. Translation: CAA72215.1 .
    U93702 mRNA. Translation: AAC53536.1 .
    AF109906 Genomic DNA. Translation: AAC84167.1 .
    BC004666 mRNA. Translation: AAH04666.1 .
    CCDSi CCDS28668.1.
    RefSeqi NP_035023.3. NM_010893.3.
    UniGenei Mm.8856.

    3D structure databases

    ProteinModelPortali O35657.
    SMRi O35657. Positions 49-390.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201731. 1 interaction.

    Protein family/group databases

    CAZyi GH33. Glycoside Hydrolase Family 33.

    PTM databases

    PhosphoSitei O35657.

    Proteomic databases

    MaxQBi O35657.
    PaxDbi O35657.
    PRIDEi O35657.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000007253 ; ENSMUSP00000007253 ; ENSMUSG00000007038 .
    GeneIDi 18010.
    KEGGi mmu:18010.
    UCSCi uc008cei.2. mouse.

    Organism-specific databases

    CTDi 4758.
    MGIi MGI:97305. Neu1.

    Phylogenomic databases

    eggNOGi COG4409.
    HOGENOMi HOG000007651.
    HOVERGENi HBG057314.
    InParanoidi O35657.
    KOi K01186.
    OMAi GTEMFAP.
    OrthoDBi EOG779NXT.
    PhylomeDBi O35657.
    TreeFami TF331063.

    Enzyme and pathway databases

    Reactomei REACT_199008. Glycosphingolipid metabolism.
    REACT_202500. Sialic acid metabolism.

    Miscellaneous databases

    ChiTaRSi NEU1. mouse.
    NextBioi 293029.
    PROi O35657.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O35657.
    Bgeei O35657.
    CleanExi MM_NEU1.
    Genevestigatori O35657.

    Family and domain databases

    Gene3Di 2.120.10.10. 1 hit.
    InterProi IPR026856. Sialidase_fam.
    IPR011040. Sialidases.
    [Graphical view ]
    PANTHERi PTHR10628. PTHR10628. 1 hit.
    SUPFAMi SSF50939. SSF50939. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a sialidase from the murine histocompatibility-2 complex: low levels of mRNA and a single amino acid mutation are responsible for reduced sialidase activity in mice carrying the Neu1a allele."
      Carrillo M.B., Milner C.M., Ball S.T., Snoek M., Campbell R.D.
      Glycobiology 7:975-986(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION.
      Strain: C57BL/RIJ.
    2. "Cloning of the cDNA and gene encoding mouse lysosomal sialidase and correction of sialidase deficiency in human sialidosis and mouse SM/J fibroblasts."
      Igdoura S.A., Gafuik C., Mertineit C., Saberi F., Pshezhetsky A.V., Potier M., Trasler J.M., Gravel R.A.
      Hum. Mol. Genet. 7:115-121(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Strain: C57BL/6.
    3. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
      Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
      Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 129.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "A point mutation in the neu-1 locus causes the neuraminidase defect in the SM/J mouse."
      Rottier R.J., Bonten E.J., d'Azzo A.
      Hum. Mol. Genet. 7:313-321(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ILE-209.

    Entry informationi

    Entry nameiNEUR1_MOUSE
    AccessioniPrimary (citable) accession number: O35657
    Secondary accession number(s): O55220, Q99KG9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3