SubmitCancel

Skip Header

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

Q99PW3

- NEUR1_RAT

UniProt

Q99PW3 - NEUR1_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Sialidase-1
Gene
Neu1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 – 721Substrate By similarity
Binding sitei91 – 911Substrate By similarity
Active sitei97 – 971Proton acceptor By similarity
Active sitei258 – 2581 Reviewed prediction
Binding sitei258 – 2581Substrate By similarity
Binding sitei274 – 2741Substrate By similarity
Binding sitei335 – 3351Substrate By similarity
Active sitei364 – 3641Nucleophile By similarity
Active sitei388 – 3881 Reviewed prediction

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
Complete GO annotation...

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
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: Unplaced

Organism-specific databases

RGDi3163. Neu1.

Subcellular locationi

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

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
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3939 Reviewed prediction
Add
BLAST
Chaini40 – 409370Sialidase-1
PRO_0000012028Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi180 – 1801N-linked (GlcNAc...) Reviewed prediction
Glycosylationi337 – 3371N-linked (GlcNAc...) Reviewed prediction
Glycosylationi346 – 3461N-linked (GlcNAc...) Reviewed prediction
Glycosylationi372 – 3721N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

N-glycosylated Inferred.
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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati106 – 11712BNR 1
Add
BLAST
Repeati166 – 17712BNR 2
Add
BLAST
Repeati225 – 23612BNR 3
Add
BLAST
Repeati341 – 35212BNR 4
Add
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

Contains 4 BNR repeats.

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

« Hide

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...

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: June 11, 2014
This is version 95 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