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Protein

Sialidase-1

Gene

NEU1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (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)DescriptionActionsGraphical viewLength
Binding sitei78SubstrateBy similarity1
Binding sitei97SubstrateBy similarity1
Active sitei103Proton acceptorBy similarity1
Binding sitei264SubstrateBy similarity1
Binding sitei280SubstrateBy similarity1
Binding sitei341SubstrateBy similarity1
Active sitei370NucleophileBy similarity1
Active sitei394Sequence analysis1

GO - Molecular functioni

GO - Biological processi

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
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 47By similarityAdd BLAST47
ChainiPRO_000030472848 – 415Sialidase-1Add BLAST368

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi186N-linked (GlcNAc...)Sequence analysis1
Glycosylationi343N-linked (GlcNAc...)Sequence analysis1
Glycosylationi352N-linked (GlcNAc...)Sequence analysis1

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

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ5RAF4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati112 – 123BNR 1Add BLAST12
Repeati172 – 183BNR 2Add BLAST12
Repeati231 – 242BNR 3Add BLAST12
Repeati347 – 358BNR 4Add BLAST12

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi77 – 80FRIP motif4
Motifi412 – 415Internalization signal4

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.
InParanoidiQ5RAF4.
KOiK01186.

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR026856. Sialidase_fam.
IPR011040. Sialidases.
[Graphical view]
PANTHERiPTHR10628. PTHR10628. 1 hit.
PfamiPF13088. BNR_2. 1 hit.
[Graphical view]
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5RAF4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTGERPSTAL PDRRWGPRIL GFWGGCRVWV FAAIFLLLSL AASWSKAEND
60 70 80 90 100
FGLVQPLVTM EQLLWVSGRQ IGSVDTFRIP LITATPRGTL LAFAEARKMS
110 120 130 140 150
SSDEGAKFIA LRRSMDQGST WSPTAFIVND GDVPDGLNLG AVVSDVETGV
160 170 180 190 200
VFLFYSLCAH KAGCQVASTM LVWSKDDGVS WSTPRNLSLD IGTEVFAPGP
210 220 230 240 250
GSGIQKQREP RKGRLIVCGH GTLERDGVFC LLSDDHGASW RYGSGVSGIP
260 270 280 290 300
YGQPKQENDF NPDECQPYEL PDGSVVINAR NQNNYHCHCR IVLRSYDACD
310 320 330 340 350
TLRPRDVTFD PELVDPVVAA GAVVTSSGIV FFSNPAHPEF RVNLTLRWSF
360 370 380 390 400
SNGTSWRKET VQLWPGPSGY SSLATLEGSM DGEEQAPQLY VLYEKGRNHY
410
TESISVAKIS VYGTL
Length:415
Mass (Da):45,467
Last modified:December 21, 2004 - v1
Checksum:i360E60A256DEA07F
GO
Isoform 2 (identifier: Q5RAF4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     267-414: Missing.

Note: No experimental confirmation available.
Show »
Length:267
Mass (Da):29,000
Checksum:iFFE761254DE87C3A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5R → Q in CAH89635 (Ref. 1) Curated1
Sequence conflicti5R → Q in CAH91396 (Ref. 1) Curated1
Sequence conflicti12D → G in CAH89635 (Ref. 1) Curated1
Sequence conflicti12D → G in CAH91396 (Ref. 1) Curated1
Sequence conflicti29W → R in CAH89635 (Ref. 1) Curated1
Sequence conflicti29W → R in CAH91396 (Ref. 1) Curated1
Sequence conflicti57L → P in CAH91396 (Ref. 1) Curated1
Sequence conflicti256Q → H in CAH89635 (Ref. 1) Curated1
Sequence conflicti256Q → H in CAH91396 (Ref. 1) Curated1
Sequence conflicti344L → P in CAH89635 (Ref. 1) Curated1
Sequence conflicti406V → M in CAH89635 (Ref. 1) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_028119267 – 414Missing in isoform 2. 1 PublicationAdd BLAST148

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857339 mRNA. Translation: CAH89635.1.
CR859063 mRNA. Translation: CAH91256.1.
CR859212 mRNA. Translation: CAH91396.1.
RefSeqiNP_001125743.1. NM_001132271.1. [Q5RAF4-1]
NP_001128939.1. NM_001135467.1.

Genome annotation databases

GeneIDi100172668.
KEGGipon:100172668.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857339 mRNA. Translation: CAH89635.1.
CR859063 mRNA. Translation: CAH91256.1.
CR859212 mRNA. Translation: CAH91396.1.
RefSeqiNP_001125743.1. NM_001132271.1. [Q5RAF4-1]
NP_001128939.1. NM_001135467.1.

3D structure databases

ProteinModelPortaliQ5RAF4.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH33. Glycoside Hydrolase Family 33.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100172668.
KEGGipon:100172668.

Organism-specific databases

CTDi4758.

Phylogenomic databases

HOVERGENiHBG057314.
InParanoidiQ5RAF4.
KOiK01186.

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR026856. Sialidase_fam.
IPR011040. Sialidases.
[Graphical view]
PANTHERiPTHR10628. PTHR10628. 1 hit.
PfamiPF13088. BNR_2. 1 hit.
[Graphical view]
SUPFAMiSSF50939. SSF50939. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNEUR1_PONAB
AccessioniPrimary (citable) accession number: Q5RAF4
Secondary accession number(s): Q5RA14, Q5RF22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: December 21, 2004
Last modified: November 2, 2016
This is version 73 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

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 one 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.