Skip Header

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

Q64393

- NEUR2_CRIGR

UniProt

Q64393 - NEUR2_CRIGR

(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-2

Gene

NEU2

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moities from glycoproteins, oligosaccharides and gangliosides.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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211SubstrateBy similarity
Binding sitei41 – 411SubstrateBy similarity
Active sitei46 – 461Proton acceptorBy similarity
Binding sitei179 – 1791SubstrateBy similarity
Binding sitei181 – 1811SubstrateBy similarity
Binding sitei218 – 2181SubstrateBy similarity
Binding sitei237 – 2371SubstrateSequence Analysis
Binding sitei303 – 3031SubstrateBy similarity
Active sitei333 – 3331NucleophileBy similarity
Active sitei354 – 3541Sequence Analysis

GO - Molecular functioni

  1. exo-alpha-(2->3)-sialidase activity Source: UniProtKB
  2. exo-alpha-(2->6)-sialidase activity Source: UniProtKB-EC
  3. exo-alpha-(2->8)-sialidase activity Source: UniProtKB-EC

GO - Biological processi

  1. ganglioside catabolic process Source: UniProtKB
  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-2 (EC:3.2.1.18)
Alternative name(s):
Cytosolic sialidase
N-acetyl-alpha-neuraminidase 2
Gene namesi
Name:NEU2
OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifieri10029 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379Sialidase-2PRO_0000208898Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ64393.
SMRiQ64393. Positions 1-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati127 – 13812BNR 1Add
BLAST
Repeati197 – 20812BNR 2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi20 – 234FRIP motif

Sequence similaritiesi

Belongs to the glycosyl hydrolase 33 family.Curated
Contains 2 BNR repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG052608.
KOiK12357.

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR026945. Sialidase-2.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
[Graphical view]
PANTHERiPTHR10628. PTHR10628. 1 hit.
PTHR10628:SF6. PTHR10628:SF6. 1 hit.
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Complete.

Q64393-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATCPVLQKE TLFQTGDYAY RIPALIYLSK QKTLLAFAEK RLTKTDEHAD
60 70 80 90 100
LFVLRRGSYN ADTHQVQWQA EEVVTQAYLE GHRSMSPCPL YDKQTRTLFL
110 120 130 140 150
FFIAVRGQIS EHHQLQTGVN VTRLCHITST DHGKTWSAVQ DLTDTTIGST
160 170 180 190 200
HQDWATFGVG PGHCLQLRNT AGSLLVPAYA YRKQPPIHAP APSAFCFLSH
210 220 230 240 250
DHGSTWELGH FVSQNSLECQ VAEVGTGAER VVYLNARSCL GARVQAQSPN
260 270 280 290 300
SGLDFQDNQV VSKLVEPPKG CHGSVIAFPN PTSKADALDV WLLYTHPTDS
310 320 330 340 350
RKRTNLGVYL NQKPLDPTTW SAPTLLATGI CAYSDLQNMG HGPDGSPQFG
360 370
CLYESNNYEE IVFLMFTLKQ AFPAVFGAQ
Length:379
Mass (Da):41,962
Last modified:November 1, 1996 - v1
Checksum:iB5AFFBC6B6BE88B1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U06143 mRNA. Translation: AAA19746.1.
PIRiA54961.
RefSeqiNP_001233664.1. NM_001246735.2.

Genome annotation databases

GeneIDi100689301.
KEGGicge:100689301.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U06143 mRNA. Translation: AAA19746.1 .
PIRi A54961.
RefSeqi NP_001233664.1. NM_001246735.2.

3D structure databases

ProteinModelPortali Q64393.
SMRi Q64393. Positions 1-376.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH33. Glycoside Hydrolase Family 33.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100689301.
KEGGi cge:100689301.

Organism-specific databases

CTDi 4759.

Phylogenomic databases

HOVERGENi HBG052608.
KOi K12357.

Family and domain databases

Gene3Di 2.120.10.10. 1 hit.
InterProi IPR026945. Sialidase-2.
IPR026856. Sialidase_fam.
IPR011040. Sialidases.
[Graphical view ]
PANTHERi PTHR10628. PTHR10628. 1 hit.
PTHR10628:SF6. PTHR10628:SF6. 1 hit.
SUPFAMi SSF50939. SSF50939. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Cloning and expression of a soluble sialidase from Chinese hamster ovary cells: sequence alignment similarities to bacterial sialidases."
    Ferrari J., Harris R., Warner T.G.
    Glycobiology 4:367-373(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ovary.
  2. "Characterization of cytosolic sialidase from Chinese hamster ovary cells: part I: cloning and expression of soluble sialidase in Escherichia coli."
    Burg M., Muthing J.
    Carbohydr. Res. 330:335-346(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  3. "Characterization of cytosolic sialidase from Chinese hamster ovary cells: part II. Substrate specificity for gangliosides."
    Muthing J., Burg M.
    Carbohydr. Res. 330:347-356(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiNEUR2_CRIGR
AccessioniPrimary (citable) accession number: Q64393
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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