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Q99PW3

- NEUR1_RAT

UniProt

Q99PW3 - NEUR1_RAT

Protein

Sialidase-1

Gene

Neu1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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.1 Publication

    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.1 Publication

    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: RGD
    5. protein binding Source: RGD

    GO - Biological processi

    1. lipid catabolic process Source: UniProtKB-KW
    2. oligosaccharide catabolic process Source: UniProtKB
    3. positive regulation of neuron projection development Source: RGD
    4. regulation of myoblast proliferation Source: RGD

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Lipid degradation, Lipid 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):
    Lysosomal sialidase
    N-acetyl-alpha-neuraminidase 1
    Gene namesi
    Name:Neu1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3163. 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 surface Source: RGD
    2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    3. lysosomal lumen Source: UniProtKB-SubCell
    4. lysosomal membrane Source: UniProtKB-SubCell
    5. lysosome Source: RGD
    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 – 3939Sequence AnalysisAdd
    BLAST
    Chaini40 – 409370Sialidase-1PRO_0000012028Add
    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

    Expressioni

    Gene expression databases

    GenevestigatoriQ99PW3.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    IntActiQ99PW3. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99PW3.
    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

    HOVERGENiHBG057314.
    PhylomeDBiQ99PW3.

    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.

    Q99PW3-1 [UniParc]FASTAAdd to Basket

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    MVGAEPSRPP GPPSYWTGRR GQGLAAIFLL LVSAAGSEAR TEDDFSLVQP    50
    LVTMEQLLWV SGKQIGSVDT FRIPLITATP RGTLLAFAEA RKKSASDEGA 100
    KFIAMRRSTD QGSTWSSTAF IVDDGEASDG LNLGAVVNDV DTGVVFLIYT 150
    LCAHKVNCQV ASTMLVWSKD DGVSWSPPRN LSVDIGTEMF APGPGSGIQK 200
    QREPWKGRLI VCGHGTLERD GVFCLLSDDH GASWHYGTGV SGIPFGQPKH 250
    DHDFNPDECQ PYELPDGSVI INARNQNNYH CRCRIVLRSY DACDTLRPRD 300
    VTFDPELVDP VVAAGALATS SGIVFFSNPA HPEYRVNLTL RWSFSNGTFW 350
    QKERVQLWPG PSGYSSLTAL ENSTDGKKQP PQLFVLYEKG LNRYTESISM 400
    VKISVYGTL 409
    Length:409
    Mass (Da):44,695
    Last modified:June 1, 2001 - v1
    Checksum:iF912FA1E1F0991A9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB035722 mRNA. Translation: BAB21443.1.
    UniGeneiRn.128560.

    Genome annotation databases

    UCSCiRGD:3163. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB035722 mRNA. Translation: BAB21443.1 .
    UniGenei Rn.128560.

    3D structure databases

    ProteinModelPortali Q99PW3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q99PW3. 1 interaction.

    Protein family/group databases

    CAZyi GH33. Glycoside Hydrolase Family 33.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:3163. rat.

    Organism-specific databases

    RGDi 3163. Neu1.

    Phylogenomic databases

    HOVERGENi HBG057314.
    PhylomeDBi Q99PW3.

    Miscellaneous databases

    PROi Q99PW3.

    Gene expression databases

    Genevestigatori Q99PW3.

    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. "Differential expression of three sialidase genes in rat development."
      Hasegawa T., Feijoo Carnero C., Wada T., Itoyama Y., Miyagi T.
      Biochem. Biophys. Res. Commun. 280:726-732(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
      Strain: Sprague-Dawley.
      Tissue: Liver.

    Entry informationi

    Entry nameiNEUR1_RAT
    AccessioniPrimary (citable) accession number: Q99PW3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 96 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3