NA - Neuraminidase - Influenza A virus (A/Netherlands/2631_1202/2010(H1N1))

Functionⁱ

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.UniRule annotationSAAS annotation

Cofactorⁱ

Ca²⁺UniRule annotationSAAS annotation

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.UniRule annotation

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	118	SubstrateUniRule annotation	1
Active siteⁱ	151	Proton donor/acceptorUniRule annotation	1
Binding siteⁱ	152	SubstrateUniRule annotation	1
Binding siteⁱ	293	SubstrateUniRule annotation	1
Metal bindingⁱ	294	Calcium 1; via carbonyl oxygenCombined sources	1
Metal bindingⁱ	294	Calcium 2; via carbonyl oxygenCombined sources	1
Metal bindingⁱ	294	Calcium; via carbonyl oxygenUniRule annotation	1
Metal bindingⁱ	298	Calcium 1; via carbonyl oxygenCombined sources	1
Metal bindingⁱ	298	Calcium 2; via carbonyl oxygenCombined sources	1
Metal bindingⁱ	298	Calcium; via carbonyl oxygenUniRule annotation	1
Metal bindingⁱ	324	CalciumUniRule annotation	1
Metal bindingⁱ	324	Calcium 1Combined sources	1
Metal bindingⁱ	324	Calcium 2Combined sources	1
Metal bindingⁱ	342	Calcium 1; via carbonyl oxygenCombined sources	1
Metal bindingⁱ	342	Calcium 2; via carbonyl oxygenCombined sources	1
Metal bindingⁱ	344	Calcium 1; via carbonyl oxygenCombined sources	1
Metal bindingⁱ	344	Calcium 2; via carbonyl oxygenCombined sources	1
Metal bindingⁱ	344	Calcium; via carbonyl oxygenUniRule annotation	1
Binding siteⁱ	368	SubstrateUniRule annotation	1
Active siteⁱ	402	NucleophileUniRule annotation	1

GO - Molecular functionⁱ

exo-alpha-(2->3)-sialidase activity Source: UniProtKB-UniRule
exo-alpha-(2->6)-sialidase activity Source: UniProtKB-UniRule
exo-alpha-(2->8)-sialidase activity Source: UniProtKB-UniRule
metal ion binding Source: UniProtKB-UniRule

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

carbohydrate metabolic process Source: UniProtKB-UniRule
viral budding from plasma membrane Source: UniProtKB-UniRule

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	GlycosidaseUniRule annotationSAAS annotation, Hydrolase
Ligand	CalciumUniRule annotationCombined sourcesSAAS annotation, Metal-bindingUniRule annotationCombined sourcesSAAS annotation

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: NeuraminidaseUniRule annotationSAAS annotation (EC:3.2.1.18UniRule annotationSAAS annotation)
Gene namesⁱ	Name:NAUniRule annotationImported
Organismⁱ	Influenza A virus (A/Netherlands/2631_1202/2010(H1N1))Imported
Taxonomic identifierⁱ	1027873 [NCBI]
Taxonomic lineageⁱ	Viruses › ssRNA viruses › ssRNA negative-strand viruses › Orthomyxoviridae › Influenzavirus A › Influenza A virus › H1N1 subtype

Subcellular locationⁱ

Host apical cell membrane
SAAS annotation
Automatic assertion according to rulesⁱ
- SAAS:SAAS00582107
; Single-pass type II membrane protein
SAAS annotation
Automatic assertion according to rulesⁱ
- SAAS:SAAS00582107

Topology

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transmembraneⁱ	7 – 34	HelicalUniRule annotationAdd BLAST		28

GO - Cellular componentⁱ

host cell plasma membrane Source: UniProtKB-SubCell
integral component of membrane Source: UniProtKB-UniRule
virion membrane Source: UniProtKB-UniRule

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Host cell membraneUniRule annotationSAAS annotation, Host membrane, Membrane, VirionUniRule annotationSAAS annotation

PTM / Processingⁱ

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Glycosylationⁱ	88	N-linked (GlcNAc...)Combined sources	1
Disulfide bondⁱ	92 ↔ 417	UniRule annotationCombined sources
Disulfide bondⁱ	124 ↔ 129	UniRule annotationCombined sources
Glycosylationⁱ	146	N-linked (GlcNAc...)Combined sources	1
Disulfide bondⁱ	184 ↔ 231	UniRule annotationCombined sources
Disulfide bondⁱ	233 ↔ 238	UniRule annotationCombined sources
Glycosylationⁱ	235	N-linked (GlcNAc...)Combined sources	1
Disulfide bondⁱ	279 ↔ 292	UniRule annotationCombined sources
Disulfide bondⁱ	281 ↔ 290	UniRule annotationCombined sources
Disulfide bondⁱ	318 ↔ 335	UniRule annotationCombined sources
Disulfide bondⁱ	421 ↔ 446	UniRule annotationCombined sources

Post-translational modificationⁱ

N-glycosylated.UniRule annotation

Keywords - PTMⁱ

Disulfide bondUniRule annotationSAAS annotation, GlycoproteinUniRule annotation

Interactionⁱ

Subunit structureⁱ

Homotetramer.UniRule annotationSAAS annotation

Structureⁱ

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4B7J	X-ray	2.42	A	1-469	[»]
	4B7M	X-ray	2.50	A/B	1-469	[»]
	4B7N	X-ray	2.84	A	1-469	[»]
SMRⁱ	F8UU09.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	11 – 33	Involved in apical transport and lipid raft associationUniRule annotationAdd BLAST	23
Regionⁱ	91 – 469	Head of neuraminidaseUniRule annotationAdd BLAST	379
Regionⁱ	277 – 278	Substrate bindingUniRule annotation	2

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.UniRule annotation

Sequence similaritiesⁱ

Belongs to the glycosyl hydrolase 34 family.UniRule annotationSAAS annotation

Keywords - Domainⁱ

Signal-anchorUniRule annotation, Transmembrane, Transmembrane helixUniRule annotationSAAS annotation

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd15483. Influenza_NA. 1 hit.
HAMAPⁱ	MF_04071. INFV_NRAM. 1 hit.
InterProⁱ	View protein in InterPro IPR001860. Glyco_hydro_34. IPR033654. Sialidase_Influenza_A/B. IPR036278. Sialidase_sf.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00064. Neur. 1 hit.
SUPFAMⁱ	SSF50939. SSF50939. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

F8UU09-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MNPNQKIITI GSVCMTIGMA NLILQIGNII SIWISHSIQL GNQNQIETCN 
        60         70         80         90        100
QSVITYENNT WVNQTYVNIS NTNFAAGQSV VSVKLAGNSS LCPVSGWAIY 
       110        120        130        140        150
SKDNSIRIGS KGDVFVIREP FISCSPLECR TFFLTQGALL NDKHSNGTIK 
       160        170        180        190        200
DRSPYRTLMS CPIGEVPSPY NSRFESVAWS ASACHDGINW LTIGISGPDN 
       210        220        230        240        250
GAVAVLKYNG IITDTIKSWR NNRLRTQESE CACVNGSCFT VMTDGPSDGQ 
       260        270        280        290        300
ASYKIFRIEK GKIVKSVEMN APNYHYEECS CYPDSSEITC VCRDNWHGSN 
       310        320        330        340        350
RPWVSFNQNL EYQIGYICSG IFGDNPRPND KTGSCGPVSS NGANGVKGFS 
       360        370        380        390        400
FKYGNGVWIG RTKSISSRNG FEMIWDPNGW TGTDNDFSIK QDIVGINEWS 
       410        420        430        440        450
GYSGSFVQHP ELTGLDCIRP CFWVELIRGR PKENTIWTSG SSISFCGVNS 
       460 
DTVGWSWPDG AELPFTIDK

Length:469

Mass (Da):51,656

Last modified:September 21, 2011 - v1

Checksum:ⁱ48F0F60CD8119D39

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	JF906185 Viral cRNA. Translation: AEE69001.1.

Select the link destinations:
EMBLⁱ
GenBankⁱ
DDBJⁱ

Links Updated

JF906185 Viral cRNA. Translation: AEE69001.1.

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
F8UU09	F6GLH6 D8KRX1	Influenza A virus (A/Netherlands/2631c/2010(H1N1)) Influenza A virus (A/Netherlands/2631b/2010(H1N1))	469	UniRef100_F6GLH6	Cluster: Neuraminidase	3

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
F8UU09	Q710U6 D1LPI6 C6S3U9 C6S3U7 C6S3V0 A0A088F3V9 A0A088F7G3 A0A0U3TVR5 A0A0U3TUR2 A0A0U3S922 +13354	Influenza A virus (strain A/Chicken/Scotland/1959 H5N1) Influenza A virus (A/swine/Cotes d'Armor/0227/2005(H1N1)) Influenza A virus (A/swine/Cotes d'Armor/60293/2001(H1N1)) Influenza A virus (A/swine/Cotes d'Armor/002007/2006(H1N1)) Influenza A virus (A/Wyoming/07/2013(H1N1)) Influenza A virus (A/Wyoming/09/2013(H1N1)) Influenza A virus (A/Beijing/58/2014(H1N1)) Influenza A virus (A/Beijing/21/2013(H1N1)) Influenza A virus (A/Beijing/FL61/2014(H1N1)) Influenza A virus (A/Netherlands/602/2009(H1N1)) And more	469	UniRef90_Q710U6	Cluster: Neuraminidase	13,365

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
F8UU09	P03468 Q8JMH6 Q8JMH7 A4U6V5 R9WM92 A1ILR4 A4GZB7 Q289C6 E0AGJ0 Q0HD57 +26942	Influenza A virus (strain A/Puerto Rico/8/1934 H1N1) Influenza A virus (A/Rhodes/47(H1N1)) Influenza A virus (A/Marton/43(H1N1)) Influenza A virus (strain A/USA:Huston/AA/1945 H1N1) Influenza A virus (A/Bellamy/JY2/1942(H1N1)) Influenza A virus (A/R(Japan/305/57-Bellamy/42)(H2N1)) Influenza A virus (A/R(equine/Prague/1/56-Bellamy/1942)(H7N1)) Influenza A virus (A/Bellamy/1942(H1N1)) Influenza A virus (strain A/Hickox/1940 H1N1) Influenza A virus (A/Cameron/JY2/1946(H1N1)) And more	454	UniRef50_P03468	Cluster: Neuraminidase	26,953

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	JF906185 Viral cRNA. Translation: AEE69001.1.

Select the link destinations:
EMBLⁱ
GenBankⁱ
DDBJⁱ

Links Updated

JF906185 Viral cRNA. Translation: AEE69001.1.

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4B7J	X-ray	2.42	A	1-469	[»]
	4B7M	X-ray	2.50	A/B	1-469	[»]
	4B7N	X-ray	2.84	A	1-469	[»]
SMRⁱ	F8UU09.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd15483. Influenza_NA. 1 hit.
HAMAPⁱ	MF_04071. INFV_NRAM. 1 hit.
InterProⁱ	View protein in InterPro IPR001860. Glyco_hydro_34. IPR033654. Sialidase_Influenza_A/B. IPR036278. Sialidase_sf.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00064. Neur. 1 hit.
SUPFAMⁱ	SSF50939. SSF50939. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	F8UU09_9INFA
Accessionⁱ	F8UU09Primary (citable) accession number: F8UU09
Entry historyⁱ	Integrated into UniProtKB/TrEMBL:	September 21, 2011
	Last sequence update:	September 21, 2011
	Last modified:	March 28, 2018
	This is version 51 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Unreviewed (UniProtKB/TrEMBL)

Miscellaneousⁱ

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation

Keywords - Technical termⁱ

3D-structureCombined sources

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - F8UU09 (F8UU09_9INFA)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Neuraminidase

NA

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Amino acid modifications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Family and domain databases

Sequence databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Caution

Your basket is currently empty. ⁱ

Functionⁱ

Enzyme regulationⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ