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Q2VC95

- NRAM_I80A2

UniProt

Q2VC95 - NRAM_I80A2

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Protein
Neuraminidase
Gene
NA
Organism
Influenza A virus (strain A/Seal/Massachusetts/1/1980 H7N7)
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 sitei116 – 1161Substrate By similarity
Active sitei149 – 1491Proton donor/acceptor By similarity
Binding sitei150 – 1501Substrate By similarity
Binding sitei291 – 2911Substrate By similarity
Metal bindingi292 – 2921Calcium; via carbonyl oxygen By similarity
Metal bindingi296 – 2961Calcium; via carbonyl oxygen By similarity
Metal bindingi323 – 3231Calcium By similarity
Binding sitei370 – 3701Substrate By similarity
Active sitei404 – 4041Nucleophile 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

Names & Taxonomyi

Protein namesi
Recommended name:
Neuraminidase (EC:3.2.1.18)
Gene namesi
Name:NA
OrganismiInfluenza A virus (strain A/Seal/Massachusetts/1/1980 H7N7)
Taxonomic identifieri384493 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
Equus caballus (Horse) [TaxID: 9796]
Homo sapiens (Human) [TaxID: 9606]
Phocidae (true seals) [TaxID: 9709]
ProteomesiUP000008576: Genome

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66Intravirion Reviewed prediction
Transmembranei7 – 2721Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini28 – 470443Virion surface Reviewed prediction
Add
BLAST

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 – 470470Neuraminidase
PRO_0000280149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi32 – 321N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi46 – 461N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi55 – 551N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi56 – 561N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi66 – 661N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi67 – 671N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi86 – 861N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi90 ↔ 418 By similarity
Disulfide bondi122 ↔ 127 By similarity
Glycosylationi144 – 1441N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi174 ↔ 192 By similarity
Disulfide bondi182 ↔ 229 By similarity
Glycosylationi199 – 1991N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi231 ↔ 236 By similarity
Glycosylationi233 – 2331N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi277 ↔ 290 By similarity
Disulfide bondi279 ↔ 288 By similarity
Disulfide bondi317 ↔ 335 By similarity
Glycosylationi400 – 4001N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi422 ↔ 449 By similarity

Post-translational modificationi

N-glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ2VC95.
SMRiQ2VC95. Positions 85-469.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 3323Involved in apical transport and lipid raft association By similarity
Add
BLAST
Regioni36 – 8853Hypervariable stalk region By similarity
Add
BLAST
Regioni89 – 470382Head of neuraminidase By similarity
Add
BLAST
Regioni275 – 2762Substrate binding By similarity

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, Transmembrane helix

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: Complete.

Q2VC95-1 [UniParc]FASTAAdd to Basket

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MNPNQKLFAL SGVAIALSIF NLLIGISNVV LNVSLHLKNN NDQDKNWTCT    50
SITQNNTTLI ENTYVNNTTV INKETEAAKQ NYLMLNKSLC KVEGWVVVAK 100
DNAIRFGESE QVIVTREPYV SCDPLGCRMY ALHQGTTIRN KHSNGTIHDR 150
TALRGLISTP LGSPPVVSNS DFLCVGWSST SCHDGIGRMT ICVQGNNDNA 200
TATVYYDRRL TTTIKTWARN ILRTQESECV CHNGTCVVVM TDGSASSQAH 250
TKVLYFHKGL IIKEEALKGS ARHIEECSCY GHDSKVTCVC RDNWQGANRP 300
VIEIDMNAME HTSQYLCTGV LTDTSRPSDK SIGDCNNPIT GSPGAPGVKG 350
FGFLDSSNTW LGRTISPRSR SGFEMLKIPN AGTDPNSRIT ERQEIVDSNN 400
WSGYSGSFID YWDESSECYN PCFYVELIRG RPEEAKYVWW TSNSLVALCG 450
SPVPVGSGSF PDGAQIQYFS 470
Length:470
Mass (Da):51,769
Last modified:January 10, 2006 - v1
Checksum:i777E7FC7A9695C2F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ266095 Genomic RNA. Translation: ABB90268.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ266095 Genomic RNA. Translation: ABB90268.1 .

3D structure databases

ProteinModelPortali Q2VC95.
SMRi Q2VC95. Positions 85-469.
ModBasei Search...
MobiDBi Search...

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. "The viral polymerase mediates adaptation of an avian influenza virus to a mammalian host."
    Gabriel G., Dauber B., Wolff T., Planz O., Klenk H.D., Stech J.
    Proc. Natl. Acad. Sci. U.S.A. 102:18590-18595(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: SC35M mouse-adapted.
  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_I80A2
AccessioniPrimary (citable) accession number: Q2VC95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: January 10, 2006
Last modified: September 3, 2014
This is version 52 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.
SC35 was derived from A/Seal/Massachussetts/1/80 (H7N7) by serial passages in chicken embryo cells, thereby acquiring a multibasic cleavage site in its hemagglutinin (HA) and becoming 100% lethal for chickens. SC35 was then passaged 11 times in mouse lung, yielding the mouse-adapted variant SC35M.

Keywords - Technical termi

Complete 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

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