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Protein

Sialidase-1

Gene

Neu1

Organism
Rattus norvegicus (Rat)
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.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

GO - Biological processi

  • lipid catabolic process Source: UniProtKB-KW
  • oligosaccharide catabolic process Source: UniProtKB
  • positive regulation of neuron projection development Source: RGD
  • regulation of myoblast proliferation Source: RGD
Complete GO annotation...

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 Componenti: Unplaced

Organism-specific databases

RGDi3163. Neu1.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: RGD
  • cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  • lysosomal lumen Source: UniProtKB-SubCell
  • lysosomal membrane Source: UniProtKB-SubCell
  • lysosome Source: RGD
  • 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 – 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

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.
STRINGi10116.ENSRNOP00000050614.

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.
InParanoidiQ99PW3.
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

« Hide

        10         20         30         40         50
MVGAEPSRPP GPPSYWTGRR GQGLAAIFLL LVSAAGSEAR TEDDFSLVQP
60 70 80 90 100
LVTMEQLLWV SGKQIGSVDT FRIPLITATP RGTLLAFAEA RKKSASDEGA
110 120 130 140 150
KFIAMRRSTD QGSTWSSTAF IVDDGEASDG LNLGAVVNDV DTGVVFLIYT
160 170 180 190 200
LCAHKVNCQV ASTMLVWSKD DGVSWSPPRN LSVDIGTEMF APGPGSGIQK
210 220 230 240 250
QREPWKGRLI VCGHGTLERD GVFCLLSDDH GASWHYGTGV SGIPFGQPKH
260 270 280 290 300
DHDFNPDECQ PYELPDGSVI INARNQNNYH CRCRIVLRSY DACDTLRPRD
310 320 330 340 350
VTFDPELVDP VVAAGALATS SGIVFFSNPA HPEYRVNLTL RWSFSNGTFW
360 370 380 390 400
QKERVQLWPG PSGYSSLTAL ENSTDGKKQP PQLFVLYEKG LNRYTESISM

VKISVYGTL
Length:409
Mass (Da):44,695
Last modified:June 1, 2001 - v1
Checksum:iF912FA1E1F0991A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035722 mRNA. Translation: BAB21443.1.
UniGeneiRn.128560.

Genome annotation databases

UCSCiRGD:3163. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035722 mRNA. Translation: BAB21443.1.
UniGeneiRn.128560.

3D structure databases

ProteinModelPortaliQ99PW3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99PW3. 1 interaction.
STRINGi10116.ENSRNOP00000050614.

Protein family/group databases

CAZyiGH33. Glycoside Hydrolase Family 33.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3163. rat.

Organism-specific databases

RGDi3163. Neu1.

Phylogenomic databases

HOVERGENiHBG057314.
InParanoidiQ99PW3.
PhylomeDBiQ99PW3.

Miscellaneous databases

PROiQ99PW3.

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

  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: June 24, 2015
This is version 99 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

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.