Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Sialidase-1

Gene

Neu1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

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

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.2.1.18. 3474.
ReactomeiREACT_310546. Sialic acid metabolism.
REACT_339900. Glycosphingolipid 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 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:97305. Neu1.

Subcellular locationi

  1. Lysosome membrane 1 Publication; Peripheral membrane protein 1 Publication; Lumenal side 1 Publication
  2. Lysosome lumen 1 Publication
  3. Cell membrane 1 Publication
  4. Cytoplasmic vesicle 1 Publication

  5. 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: MGI
  2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: MGI
  4. intracellular membrane-bounded organelle Source: MGI
  5. lysosomal lumen Source: UniProtKB-SubCell
  6. lysosomal membrane Source: UniProtKB-SubCell
  7. lysosome Source: MGI
  8. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

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

BgeeiO35657.
CleanExiMM_NEU1.
ExpressionAtlasiO35657. baseline and differential.
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

« Hide

        10         20         30         40         50
MVGADPTRPR GPLSYWAGRR GQGLAAIFLL LVSAAESEAR AEDDFSLVQP
60 70 80 90 100
LVTMEQLLWV SGKQIGSVDT FRIPLITATP RGTLLAFAEA RKKSASDEGA
110 120 130 140 150
KFIAMRRSTD QGSTWSSTAF IVDDGEASDG LNLGAVVNDV DTGIVFLIYT
160 170 180 190 200
LCAHKVNCQV ASTMLVWSKD DGISWSPPRN LSVDIGTEMF APGPGSGIQK
210 220 230 240 250
QREPGKGRLI VCGHGTLERD GVFCLLSDDH GASWHYGTGV SGIPFGQPKH
260 270 280 290 300
DHDFNPDECQ PYELPDGSVI INARNQNNYH CRCRIVLRSY DACDTLRPRD
310 320 330 340 350
VTFDPELVDP VVAAGALATS SGIVFFSNPA HPEFRVNLTL RWSFSNGTSW
360 370 380 390 400
QKERVQVWPG PSGYSSLTAL ENSTDGKKQP PQLFVLYEKG LNRYTESISM

VKISVYGTL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi201731. 1 interaction.

Protein family/group databases

CAZyiGH33. Glycoside Hydrolase Family 33.

PTM databases

PhosphoSiteiO35657.

Proteomic databases

MaxQBiO35657.
PaxDbiO35657.
PRIDEiO35657.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4758.
MGIiMGI:97305. Neu1.

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi3.2.1.18. 3474.
ReactomeiREACT_310546. Sialic acid metabolism.
REACT_339900. Glycosphingolipid metabolism.

Miscellaneous databases

ChiTaRSiNeu1. mouse.
NextBioi293029.
PROiO35657.
SOURCEiSearch...

Gene expression databases

BgeeiO35657.
CleanExiMM_NEU1.
ExpressionAtlasiO35657. baseline and differential.
GenevestigatoriO35657.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 1, 2015
This is version 131 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.