Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Neuraminidase (EC 3.2.1.18)

 NRAM_I66A1              Reviewed;         469 AA.
Q0A456; Q3SBF3;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 1.
12-SEP-2018, entry version 63.
RecName: Full=Neuraminidase {ECO:0000255|HAMAP-Rule:MF_04071};
EC=3.2.1.18 {ECO:0000255|HAMAP-Rule:MF_04071};
Name=NA {ECO:0000255|HAMAP-Rule:MF_04071};
Influenza A virus (strain A/Turkey/Wisconsin/1/1966 H9N2).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Alphainfluenzavirus.
NCBI_TaxID=385620;
NCBI_TaxID=8782; Aves.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Rousset J.A.F., Louboutin K., Beven V., de Boisseson C., Bureau E.,
Hars J., Jestin V.;
"Characterization of avian influenza viruses isolated from wild birds
and sentinel ducks during the winter seasons 2000-2001 and 2001-2002
in France.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16026813; DOI=10.1016/j.virol.2005.06.025;
Li C., Yu K., Tian G., Yu D., Liu L., Jing B., Ping J., Chen H.;
"Evolution of H9N2 influenza viruses from domestic poultry in Mainland
China.";
Virology 340:70-83(2005).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16439620; DOI=10.1126/science.1121586;
Obenauer J.C., Denson J., Mehta P.K., Su X., Mukatira S.,
Finkelstein D.B., Xu X., Wang J., Ma J., Fan Y., Rakestraw K.M.,
Webster R.G., Hoffmann E., Krauss S., Zheng J., Zhang Z., Naeve C.W.;
"Large-scale sequence analysis of avian influenza isolates.";
Science 311:1576-1580(2006).
[4]
REVIEW.
PubMed=15567494; DOI=10.1016/j.virusres.2004.08.012;
Nayak D.P., Hui E.K., Barman S.;
"Assembly and budding of influenza virus.";
Virus Res. 106:147-165(2004).
[5]
REVIEW.
PubMed=16192481; DOI=10.1056/NEJMra050740;
Moscona A.;
"Neuraminidase inhibitors for influenza.";
N. Engl. J. Med. 353:1363-1373(2005).
[6]
REVIEW.
PubMed=15744059; DOI=10.1248/bpb.28.399;
Suzuki Y.;
"Sialobiology of influenza: molecular mechanism of host range
variation of influenza viruses.";
Biol. Pharm. Bull. 28:399-408(2005).
-!- FUNCTION: Catalyzes the removal of terminal sialic acid residues
from viral and cellular glycoconjugates. Cleaves off the terminal
sialic acids on the glycosylated HA during virus budding to
facilitate virus release. Additionally helps virus spread through
the circulation by further removing sialic acids from the cell
surface. These cleavages prevent self-aggregation and ensure the
efficient spread of the progeny virus from cell to cell.
Otherwise, infection would be limited to one round of replication.
Described as a receptor-destroying enzyme because it cleaves a
terminal sialic acid from the cellular receptors. May facilitate
viral invasion of the upper airways by cleaving the sialic acid
moities on the mucin of the airway epithelial cells. Likely to
plays a role in the budding process through its association with
lipid rafts during intracellular transport. May additionally
display a raft-association independent effect on budding. Plays a
role in the determination of host range restriction on replication
and virulence. Sialidase activity in late endosome/lysosome
traffic seems to enhance virus replication. {ECO:0000255|HAMAP-
Rule:MF_04071}.
-!- CATALYTIC ACTIVITY: 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. {ECO:0000255|HAMAP-Rule:MF_04071}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000255|HAMAP-Rule:MF_04071};
-!- ACTIVITY REGULATION: Inhibited by the neuraminidase inhibitors
zanamivir (Relenza) and oseltamivir (Tamiflu). These drugs
interfere with the release of progeny virus from infected cells
and are effective against all influenza strains. Resistance to
neuraminidase inhibitors is quite rare. {ECO:0000255|HAMAP-
Rule:MF_04071}.
-!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_04071}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
Rule:MF_04071}. Host apical cell membrane {ECO:0000255|HAMAP-
Rule:MF_04071}; Single-pass type II membrane protein
{ECO:0000255|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates
at the apical plasma membrane in infected polarized epithelial
cells, which is the virus assembly site. Uses lipid rafts for cell
surface transport and apical sorting. In the virion, forms a
mushroom-shaped spike on the surface of the membrane.
{ECO:0000255|HAMAP-Rule:MF_04071}.
-!- DOMAIN: Intact N-terminus is essential for virion morphogenesis.
Possess two apical sorting signals, one in the ectodomain, which
is likely to be a glycan, and the other in the transmembrane
domain. The transmembrane domain also plays a role in lipid raft
association. {ECO:0000255|HAMAP-Rule:MF_04071}.
-!- PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04071}.
-!- MISCELLANEOUS: The influenza A genome consist of 8 RNA segments.
Genetic variation of hemagglutinin and/or neuraminidase genes
results in the emergence of new influenza strains. The mechanism
of variation can be the result of point mutations or the result of
genetic reassortment between segments of two different strains.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
{ECO:0000255|HAMAP-Rule:MF_04071}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AJ574907; CAE00569.1; -; Genomic_RNA.
EMBL; DQ067439; AAY52603.1; -; Genomic_RNA.
EMBL; CY014665; ABI84526.1; -; Genomic_RNA.
ProteinModelPortal; Q0A456; -.
SMR; Q0A456; -.
CAZy; GH34; Glycoside Hydrolase Family 34.
OrthoDB; VOG0900006X; -.
PRO; PR:Q0A456; -.
Proteomes; UP000115522; Genome.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC.
GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC.
GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0046761; P:viral budding from plasma membrane; IEA:InterPro.
CDD; cd15483; Influenza_NA; 1.
HAMAP; MF_04071; INFV_NRAM; 1.
InterPro; IPR001860; Glyco_hydro_34.
InterPro; IPR033654; Sialidase_Influenza_A/B.
InterPro; IPR036278; Sialidase_sf.
Pfam; PF00064; Neur; 1.
SUPFAM; SSF50939; SSF50939; 1.
3: Inferred from homology;
Calcium; Complete proteome; Disulfide bond; Glycoprotein; Glycosidase;
Host cell membrane; Host membrane; Hydrolase; Membrane; Metal-binding;
Signal-anchor; Transmembrane; Transmembrane helix; Virion.
CHAIN 1 469 Neuraminidase.
/FTId=PRO_0000280154.
TOPO_DOM 1 6 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04071}.
TRANSMEM 7 29 Helical. {ECO:0000255|HAMAP-
Rule:MF_04071}.
TOPO_DOM 30 469 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04071}.
REGION 11 33 Involved in apical transport and lipid
raft association. {ECO:0000255|HAMAP-
Rule:MF_04071}.
REGION 36 88 Hypervariable stalk region.
{ECO:0000255|HAMAP-Rule:MF_04071}.
REGION 91 469 Head of neuraminidase.
{ECO:0000255|HAMAP-Rule:MF_04071}.
REGION 276 277 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_04071}.
COMPBIAS 331 335 Poly-Ser.
ACT_SITE 151 151 Proton donor/acceptor.
{ECO:0000255|HAMAP-Rule:MF_04071}.
ACT_SITE 406 406 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_04071}.
METAL 293 293 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071}.
METAL 297 297 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071}.
METAL 324 324 Calcium. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 118 118 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 152 152 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 292 292 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 371 371 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 200 200 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 402 402 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 92 417 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 124 129 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 183 230 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 232 237 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 278 291 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 280 289 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 318 337 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 421 447 {ECO:0000255|HAMAP-Rule:MF_04071}.
CONFLICT 33 33 V -> M (in Ref. 2; AAY52603).
CONFLICT 193 193 C -> R (in Ref. 2; AAY52603).
CONFLICT 211 211 L -> P (in Ref. 2; AAY52603).
CONFLICT 232 232 C -> G (in Ref. 2; AAY52603).
CONFLICT 237 238 CT -> GP (in Ref. 2; AAY52603).
CONFLICT 244 245 GS -> EG (in Ref. 2; AAY52603).
CONFLICT 257 257 I -> N (in Ref. 2; AAY52603).
SEQUENCE 469 AA; 51787 MW; 387CF49A4915DDD6 CRC64;
MNPNQKIITI GSVSLTIATV CFLMQIAILA TTVTLHFKQN ECNPPANNQV VPCEPIIIER
NITEIVYLNN ITIEKEVCPE VAEYRNWSKP QCQITGFAPF SKDNSVRLSA GGDIWVTREP
YVSCDPGKCY QFALGQGTTL DNKHSNGTIH DRIPHRTLLM NELGVPFHLG TKQVCIAWSS
SSCHDGKAWL HVCVTGDDRN ATASFIYDGM LVDSIGSWSQ NILRTQESEC VCINGTCTVV
MTDGSASGNA DTRVLFIREG KIIHISPLSG SAQHIEECSC YPRYPDVRCV CRDNWKGSNR
PVIDIKMADY SINSGYVCSG LVGDTPRSDD SSSNSNCRDP NNERGNPGVK GWAFDNGDDV
WMGRTISKDS RSGYETFRVI GGWTTPNSKS QVNRQVIVDS NNWSGYSGIF SVEGKSCINR
CFYVELIRGR PQETRVWWTS NSIVVFCGTS GTYGTGSWPD GANINFMPI


Related products :

Catalog number Product name Quantity
ENEU-100 EnzyChrom™ Neuraminidase Assay Kit, Quantitative determination of neuraminidase activity or screening for neuraminidase inhibitor by colorimetric (570nm) or fluorimetric (530nm_590nm) methods 100Tests
ENEU-100 EnzyChrom™ Neuraminidase Assay Kit, Quantitative determination of neuraminidase activity or screening for neuraminidase inhibitor by colorimetric (570nm) or fluorimetric (530nm_590nm) methods. Procedu 100tests
EIAAB27004 Mouse,Mus musculus,N-acetyl-alpha-neuraminidase 4,Neu4,Neuraminidase 4,Sialidase-4
'AP30773PU-N Seasonal H1N1 Neuraminidase (Neuraminidase) IgG antibody Ab host: Rabbit 0.1 mg
9001-67-6 Neuraminidase from arthrobacter ureafa Neuraminidase from art 1g
X2616P Neuraminidase Neuraminidase (Avian Influenza A (H5N1), Influenza A NA, Neuroaminidase) Polyclonal Antibody 100
X2615P Neuraminidase Neuraminidase (Avian Influenza A (H5N1), Influenza A NA, Neuroaminidase) Polyclonal Antibody 100
orb82551 Influenza A H5N1 Neuraminidase protein Influenza A H5N1 (Avian) Neuraminidase (Middle Region) is an infectious disease antigen_toxin. For research use only. 50
orb82550 Influenza A H5N1 Neuraminidase protein Influenza A H5N1 (Avian) Neuraminidase, C-terminal is an infectious disease antigen_toxin. For research use only. 50
E02N0063 Rat Neuraminidase 96 Tests/kit
BP941 Neuraminidase 1 ml
BP941 Neuraminidase 1 ml
BP941 Neuraminidase 1 ml
NB100-94433 Neuraminidase 0.1 mg
E02N0003 Rat Neuraminidase elisa kit 96 Tests/kit
E13N0063 Anserine Neuraminidase 96 Tests/kit
E02N0003 Rat Neuraminidase ELISA , NA
E07N0063 Porcine Neuraminidase 96 Tests/kit
EC-32118-S Neuraminidase (Isoenzyme S), 1U
E02N0003 Rat Neuraminidase ELISA 96T/kit
E04N0063 Rabbit Neuraminidase 96 Tests/kit
NLS004761 Neuraminidase, Purified 10U
NLS004759 Neuraminidase, Purified 5U
GWB-73EE7F Influenza A Neuraminidase N1
NB100-94432 Neuraminidase 0.1 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur