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
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 (By similarity).By similarity

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791SubstrateBy similarity
Binding sitei98 – 981SubstrateBy similarity
Active sitei104 – 1041Proton acceptorBy similarity
Binding sitei265 – 2651SubstrateBy similarity
Binding sitei281 – 2811SubstrateBy similarity
Binding sitei342 – 3421SubstrateBy similarity
Active sitei371 – 3711NucleophileBy similarity
Active sitei395 – 3951Sequence 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: UniProtKB

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

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):
Acetylneuraminyl hydrolase
Lysosomal sialidase
N-acetyl-alpha-neuraminidase 1
Gene namesi
Name:NEU1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

Lysosome membrane By similarity; Peripheral membrane protein By similarity; Lumenal side By similarity. Lysosome lumen By similarity. Cell membrane By similarity. Cytoplasmic vesicle By similarity
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.By similarity

GO - Cellular componenti

  1. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  2. lysosomal lumen Source: UniProtKB-SubCell
  3. lysosomal membrane Source: UniProtKB-SubCell
  4. lysosome Source: UniProtKB
  5. 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 – 4848By similarityAdd
BLAST
Chaini49 – 416368Sialidase-1PRO_0000304727Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi353 – 3531N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiA5PF10.

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

STRINGi9823.ENSSSCP00000001513.

Structurei

3D structure databases

ProteinModelPortaliA5PF10.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati113 – 12412BNR 1Add
BLAST
Repeati173 – 18412BNR 2Add
BLAST
Repeati232 – 24312BNR 3Add
BLAST
Repeati348 – 35912BNR 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi78 – 814FRIP motif
Motifi413 – 4164Internalization signal

Domaini

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

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG4409.
HOGENOMiHOG000007651.
HOVERGENiHBG057314.
InParanoidiA5PF10.
KOiK01186.

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.

A5PF10-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTAERPGAVP LGRPGRPPML GLGEAYRAQV FASIFLLLLS PAGVGARAKN
60 70 80 90 100
DFNLVHPLVT MEQLLWVSGK QIGSVDTFRI PLITTTPRGT LLAFAEARKM
110 120 130 140 150
SASDKGAKFI ALRRSMDQGS TWSPTAFIVD DGETPDGLNL GAVVSDTTTG
160 170 180 190 200
VVFLFYSLCA HKAGCRVAST MLVWSKDDGI SWSSPRNLSL DIGTEMFAPG
210 220 230 240 250
PGSGIQKQWA PQKGRLIVCG HGTLERDGVF CLLSDDHGAS WRYGSGISGI
260 270 280 290 300
PYGQPKREND FNPDECQPYE LPDGSVVINA RNQNNYHCRC RIVLRSYDAC
310 320 330 340 350
DTLRPRDVTF DPELVDPVVA AGAVATSSGI IFFSNPAHPE FRVNLTLRWS
360 370 380 390 400
FSNGTSWRKE TVQIWPGPSG YSSLATLEGS VGGEDQAPQL YVLYEKGRNR
410
YTESISLAKV SVYGTL
Length:416
Mass (Da):45,159
Last modified:July 10, 2007 - v1
Checksum:i65E99172C69F3EB8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL773527 Genomic DNA. Translation: CAN87707.1.
RefSeqiNP_001095292.1. NM_001101822.1.
UniGeneiSsc.51944.

Genome annotation databases

GeneIDi100124381.
KEGGissc:100124381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL773527 Genomic DNA. Translation: CAN87707.1.
RefSeqiNP_001095292.1. NM_001101822.1.
UniGeneiSsc.51944.

3D structure databases

ProteinModelPortaliA5PF10.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000001513.

Protein family/group databases

CAZyiGH33. Glycoside Hydrolase Family 33.

Proteomic databases

PaxDbiA5PF10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100124381.
KEGGissc:100124381.

Organism-specific databases

CTDi4758.

Phylogenomic databases

eggNOGiCOG4409.
HOGENOMiHOG000007651.
HOVERGENiHBG057314.
InParanoidiA5PF10.
KOiK01186.

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. Porcine genome sequencing project
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiNEUR1_PIG
AccessioniPrimary (citable) accession number: A5PF10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 10, 2007
Last modified: January 7, 2015
This is version 56 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.