UniProtKB - F8UU09 (F8UU09_9INFA)
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Protein
Neuraminidase
Gene
NA
Organism
Influenza A virus (A/Netherlands/2631_1202/2010(H1N1))
Status
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 | Graphical view | 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
GO - Biological processi
- carbohydrate metabolic process Source: UniProtKB-UniRule
- viral budding from plasma membrane Source: UniProtKB-UniRule
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 › |
Subcellular locationi
- Host apical cell membrane SAAS annotation; Single-pass type II membrane protein SAAS annotation
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
Keywords - Cellular componenti
Host cell membraneUniRule annotationSAAS annotation, Host membrane, Membrane, VirionUniRule annotationSAAS annotationPTM / Processingi
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | 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 annotationInteractioni
Subunit structurei
Homotetramer.UniRule annotationSAAS annotation
Structurei
3D structure databases
Select the link destinations: PDBei RCSB PDBi 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 | Graphical view | 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
Keywords - Domaini
Signal-anchorUniRule annotation, Transmembrane, Transmembrane helixUniRule annotationSAAS annotationFamily and domain databases
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. |
Pfami | View protein in Pfam PF00064. Neur. 1 hit. |
SUPFAMi | SSF50939. SSF50939. 1 hit. |
i Sequence
Sequence statusi: Complete.
F8UU09-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | JF906185 Viral cRNA. Translation: AEE69001.1. |
Similar proteinsi
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