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P03480

- NRAM_I49A1

UniProt

P03480 - NRAM_I49A1

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Protein

Neuraminidase

Gene
NA
Organism
Influenza A virus (strain A/Duck/Germany/1949 H10N7)
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 sitei117 – 1171Substrate By similarity
Active sitei150 – 1501Proton donor/acceptor By similarity
Binding sitei151 – 1511Substrate By similarity
Binding sitei292 – 2921Substrate By similarity
Metal bindingi293 – 2931Calcium; via carbonyl oxygen By similarity
Metal bindingi297 – 2971Calcium; via carbonyl oxygen By similarity
Metal bindingi324 – 3241Calcium By similarity
Binding sitei371 – 3711Substrate By similarity
Active sitei405 – 4051Nucleophile 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/Duck/Germany/1949 H10N7)
Taxonomic identifieri382838 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostiAves [TaxID: 8782]
ProteomesiUP000008217: 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 predictionAdd
BLAST
Topological domaini28 – 471444Virion surface Reviewed predictionAdd
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 – 471471NeuraminidasePRO_0000078685Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi32 – 321N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi47 – 471N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi56 – 561N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi57 – 571N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi67 – 671N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi68 – 681N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi87 – 871N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi91 ↔ 419 By similarity
Disulfide bondi123 ↔ 128 By similarity
Glycosylationi145 – 1451N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi175 ↔ 193 By similarity
Disulfide bondi183 ↔ 230 By similarity
Glycosylationi200 – 2001N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi232 ↔ 237 By similarity
Glycosylationi234 – 2341N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi278 ↔ 291 By similarity
Disulfide bondi280 ↔ 289 By similarity
Disulfide bondi318 ↔ 336 By similarity
Glycosylationi401 – 4011N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi423 ↔ 450 By similarity

Post-translational modificationi

N-glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer By similarity.

Structurei

3D structure databases

ProteinModelPortaliP03480.
SMRiP03480. Positions 82-470.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 3323Involved in apical transport and lipid raft association By similarityAdd
BLAST
Regioni36 – 8954Hypervariable stalk region By similarityAdd
BLAST
Regioni90 – 471382Head of neuraminidase By similarityAdd
BLAST
Regioni276 – 2772Substrate 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.

P03480-1 [UniParc]FASTAAdd to Basket

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MNPNQKLFAL SGVAIALSVM NLLIGISNVG LNVSLHLKEK GTKQEENLTC    50
TTITQNNTTV VENTYVNNTT IITKEPDLKA PSYLLLNKSL CSVEGWVVIA 100
KDNAIRFGES EQIIVTREPY VSCDPSGCKM YALHQGTTIR NKHSNGTIHD 150
RTAFRGLIST PLGTPPTVSN SDFICVGWSS TSCHDGVGRM TICIQGNNDN 200
ATATVYYNRR LTTTIKPWAR NILRTQESEC VCHNGTCAVV MTDGSASSQA 250
YTKVMYFHKG LVIKEEPLKG SAKHIEECSC YGHNQKITCV CRDNWQGANR 300
PIIEIDMNTL EHTSRYVCTG ILTDTSRPGD KPSGDCSNPI TGSPSAPGVK 350
GFGFLNGDNT WLGRTISPRS RSGFEMLKIP NAGTDPNSRI AERQEIVDNN 400
NWSGYSGSFI DYWDDDNECY NPCFYVELIR GRPEEAKYVW WTSNSLIALC 450
GSPFPVGSGS FPDGAQIQYF S 471
Length:471
Mass (Da):51,800
Last modified:March 6, 2007 - v2
Checksum:i68F6BBACFCDD21A1
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 881K → H in AAA43391. 1 Publication
Sequence conflicti88 – 881K → H in AAA43357. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CY014673 Genomic RNA. Translation: ABI84537.1.
J02099 Genomic RNA. Translation: AAA43391.1.
K01022 Genomic RNA. Translation: AAA43357.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CY014673 Genomic RNA. Translation: ABI84537.1 .
J02099 Genomic RNA. Translation: AAA43391.1 .
K01022 Genomic RNA. Translation: AAA43357.1 .

3D structure databases

ProteinModelPortali P03480.
SMRi P03480. Positions 82-470.
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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Variation in the membrane-insertion and 'stalk' sequences in eight subtypes of influenza type A virus neuraminidase."
    Blok J., Air G.M.
    Biochemistry 21:4001-4007(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-96.
  3. "Sequence variation at the 3' end of the neuraminidase gene from 39 influenza type A viruses."
    Blok J.
    (In) Nayak D., Fox C.F. (eds.); Genetic variation among influenza viruses, pp.45-54, University of California, Los Angeles (1982)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-96.
  4. "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.
  5. "Neuraminidase inhibitors for influenza."
    Moscona A.
    N. Engl. J. Med. 353:1363-1373(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  6. "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_I49A1
AccessioniPrimary (citable) accession number: P03480
Secondary accession number(s): Q0A445, Q6LEJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 6, 2007
Last modified: September 3, 2014
This is version 94 of the entry and version 2 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.

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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