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Q67344

- NRAM_I82A7

UniProt

Q67344 - NRAM_I82A7

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Protein

Neuraminidase

Gene
NA
Organism
Influenza A virus (strain A/Swine/Hong Kong/127/1982 H3N2)
Status
Reviewed - Annotation score: 5 out of 5 - Protein inferred from homologyi

Functioni

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.

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.

Cofactori

Binds 1 calcium ion per subunit By similarity.

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei95 – 951Substrate By similarity
Active sitei128 – 1281Proton donor/acceptor By similarity
Binding sitei129 – 1291Substrate By similarity
Binding sitei269 – 2691Substrate By similarity
Metal bindingi270 – 2701Calcium; via carbonyl oxygen By similarity
Metal bindingi274 – 2741Calcium; via carbonyl oxygen By similarity
Metal bindingi301 – 3011Calcium By similarity
Binding sitei348 – 3481Substrate By similarity
Active sitei383 – 3831Nucleophile By similarity

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. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

CAZyiGH34. Glycoside Hydrolase Family 34.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuraminidase (EC:3.2.1.18)
Gene namesi
Name:NA
OrganismiInfluenza A virus (strain A/Swine/Hong Kong/127/1982 H3N2)
Taxonomic identifieri384483 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Cetacea (whales) [TaxID: 9721]
Homo sapiens (Human) [TaxID: 9606]
Phocidae (true seals) [TaxID: 9709]
Sus scrofa (Pig) [TaxID: 9823]

Subcellular locationi

Virion membrane By similarity. Host apical cell membrane; Single-pass type II membrane protein By similarity
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 By similarity.

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446NeuraminidasePRO_0000280158Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi47 – 471N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi63 – 631N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi69 ↔ 394 By similarity
Disulfide bondi101 ↔ 106 By similarity
Glycosylationi123 – 1231N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi152 ↔ 170 By similarity
Disulfide bondi160 ↔ 207 By similarity
Glycosylationi177 – 1771N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi209 ↔ 214 By similarity
Glycosylationi211 – 2111N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi255 ↔ 268 By similarity
Disulfide bondi257 ↔ 266 By similarity
Disulfide bondi295 ↔ 314 By similarity
Glycosylationi379 – 3791N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi398 ↔ 424 By similarity

Post-translational modificationi

N-glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ67344.
SMRiQ67344. Positions 59-446.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni13 – 6755Hypervariable stalk region By similarityAdd
BLAST
Regioni68 – 446379Head of neuraminidase By similarityAdd
BLAST
Regioni253 – 2542Substrate binding By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi308 – 3125Poly-Ser

Domaini

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 By similarity.

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane

Family and domain databases

Gene3Di2.120.10.10. 1 hit.
InterProiIPR001860. Glyco_hydro_34.
IPR011040. Sialidases.
[Graphical view]
PfamiPF00064. Neur. 1 hit.
[Graphical view]
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Fragment.

Q67344-1 [UniParc]FASTAAdd to Basket

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MQIAILVTTV TLHFNQYECD SLADNQVMPC EPIIIERNIT EIIYLTNTTI    50
EKEICPKLME YRNWSRPQCK ITGFAPFSKD NSIRLSAGGD IWVTREPYVS 100
CDPGKCYQFA LGQGTTLDNK HSNDTIHDRI PHRTLLMNEL GVPFHLGTRQ 150
VCIAWSSSSC HDGKAWLHVC VTGDDKNATA SFIYDGRLVD SMGSWSQNIL 200
RTQESECVCI NGTCTVVMTD GSASGRADTR ILFIEEGKIV HISPLSGSAQ 250
HVEECSCYPR YPSVRCICRD NWKGSNRPIV DINIKDYSID SRYVCSGLVG 300
DTPRNNDRSS SSDCKNPNND KGNHGVKGWA FDDGNDVWMG RTISKDSRSG 350
YETFKVIDGW STPNSKSQIN RQVIVDRDNR SGYSGIFSVE SKGCINRCFY 400
VELIRGRKQE TRVWWTSSSI VVFCGTSGTY GKGSWPDGAN INFMPI 446
Length:446
Mass (Da):49,915
Last modified:November 1, 1996 - v1
Checksum:iB3E31B09E6728A9D
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D21194 Genomic RNA. Translation: BAA04730.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D21194 Genomic RNA. Translation: BAA04730.1 .

3D structure databases

ProteinModelPortali Q67344.
SMRi Q67344. Positions 59-446.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH34. Glycoside Hydrolase Family 34.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.120.10.10. 1 hit.
InterProi IPR001860. Glyco_hydro_34.
IPR011040. Sialidases.
[Graphical view ]
Pfami PF00064. Neur. 1 hit.
[Graphical view ]
SUPFAMi SSF50939. SSF50939. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Genetic analysis of porcine H3N2 viruses originating in Southern China."
    Nerome K., Kanegae Y., Shortridge K.F., Sugita S., Ishida M.
    J. Gen. Virol. 76:613-624(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Assembly and budding of influenza virus."
    Nayak D.P., Hui E.K., Barman S.
    Virus Res. 106:147-165(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  3. "Neuraminidase inhibitors for influenza."
    Moscona A.
    N. Engl. J. Med. 353:1363-1373(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  4. "Sialobiology of influenza: molecular mechanism of host range variation of influenza viruses."
    Suzuki Y.
    Biol. Pharm. Bull. 28:399-408(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiNRAM_I82A7
AccessioniPrimary (citable) accession number: Q67344
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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.

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

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