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

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F8UU09 (F8UU09_9INFA) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 16. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Submitted name:
Neuraminidase EMBL AEE69001.1

Gene names

Name:

NA EMBL AEE69001.1

Organism

Influenza A virus (A/Netherlands/2631_1202/2010(H1N1)) EMBL AEE69001.1

Taxonomic identifier

Taxonomic lineage

Viruses › ssRNA negative-strand viruses › Orthomyxoviridae › Influenzavirus A ›

Protein attributes

Sequence length	469 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	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. SAAS SAAS011040
Subunit structure	Homotetramer By similarity. SAAS SAAS011040
Subcellular location	Virion membrane. Host apical cell membrane; Single-pass type II membrane protein By similarity SAAS SAAS011040.

Ontologies

Keywords
Cellular component	Host cell membrane SAAS SAAS011040 Host membrane Membrane Virion SAAS SAAS011040
Domain	Transmembrane Transmembrane helix SAAS SAAS011040
Ligand	Calcium PDB 4B7J PDB 4B7M PDB 4B7N Metal-binding PDB 4B7J PDB 4B7M PDB 4B7N
Molecular function	Glycosidase SAAS SAAS011040 Hydrolase
PTM	Disulfide bond SAAS SAAS011040
Technical term	3D-structure PDB 4B7J PDB 4B7M PDB 4B7N
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral component of membrane Inferred from electronic annotation. Source: UniProtKB-KW virion membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	exo-alpha-sialidase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

1

Calcium; via carbonyl oxygen PDB 4B7J PDB 4B7M PDB 4B7N

Metal binding

1

Calcium; via carbonyl oxygen PDB 4B7J PDB 4B7M PDB 4B7N

Metal binding

1

Calcium PDB 4B7J PDB 4B7M PDB 4B7N

Metal binding

1

Calcium; via carbonyl oxygen PDB 4B7J PDB 4B7M PDB 4B7N

Metal binding

1

Calcium; via carbonyl oxygen PDB 4B7J PDB 4B7M PDB 4B7N

Binding site

1

Phosphate 1

Binding site

1

Phosphate 1; via amide nitrogen

Binding site

1

Phosphate 2

Binding site

1

Phosphate 2

Binding site

1

Phosphate 2

Binding site

1

Phosphate 1

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...)

Glycosylation

1

N-linked (GlcNAc...)

Glycosylation

1

N-linked (GlcNAc...)

Sequences

Sequence

Length

Mass (Da)

Tools

F8UU09 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: 48F0F60CD8119D39
Show »

469

51,656

        10         20         30         40         50         60 
MNPNQKIITI GSVCMTIGMA NLILQIGNII SIWISHSIQL GNQNQIETCN QSVITYENNT 

        70         80         90        100        110        120 
WVNQTYVNIS NTNFAAGQSV VSVKLAGNSS LCPVSGWAIY SKDNSIRIGS KGDVFVIREP 

       130        140        150        160        170        180 
FISCSPLECR TFFLTQGALL NDKHSNGTIK DRSPYRTLMS CPIGEVPSPY NSRFESVAWS 

       190        200        210        220        230        240 
ASACHDGINW LTIGISGPDN GAVAVLKYNG IITDTIKSWR NNRLRTQESE CACVNGSCFT 

       250        260        270        280        290        300 
VMTDGPSDGQ ASYKIFRIEK GKIVKSVEMN APNYHYEECS CYPDSSEITC VCRDNWHGSN 

       310        320        330        340        350        360 
RPWVSFNQNL EYQIGYICSG IFGDNPRPND KTGSCGPVSS NGANGVKGFS FKYGNGVWIG 

       370        380        390        400        410        420 
RTKSISSRNG FEMIWDPNGW TGTDNDFSIK QDIVGINEWS GYSGSFVQHP ELTGLDCIRP 

       430        440        450        460 
CFWVELIRGR PKENTIWTSG SSISFCGVNS DTVGWSWPDG AELPFTIDK

References

[1]

"Multidrug Resistant 2009 A/H1N1 Influenza Clinical Isolate with a Neuraminidase I223R Mutation Retains Its Virulence and Transmissibility in Ferrets."
van der Vries E., Veldhuis Kroeze E.J., Stittelaar K.J., Linster M., Van der Linden A., Schrauwen E.J., Leijten L.M., van Amerongen G., Schutten M., Kuiken T., Osterhaus A.D., Fouchier R.A., Boucher C.A., Herfst S.
PLoS Pathog. 7:E1002276-E1002276(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A/Netherlands/2631_1202/2010 EMBL AEE69001.1.

[2]

"H1N1 2009 pandemic influenza virus: resistance of the I223R neuraminidase mutant explained by kinetic and structural analysis."
van der Vries E., Collins P.J., Vachieri S.G., Xiong X., Liu J., Walker P.A., Haire L.F., Hay A.J., Schutten M., Osterhaus A.D., Martin S.R., Boucher C.A., Skehel J.J., Gamblin S.J.
PLoS Pathog. 8:e1002914-e1002914(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) IN COMPLEX WITH CALCIUM AND PHOSPHATE, GLYCOSYLATION AT ASN-88; ASN-146 AND ASN-235.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

JF906185 Viral cRNA. Translation: AEE69001.1.

3D structure databases

PDBe
RCSB-PDB
PDBj

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	[»]

ModBase

MobiDB

Protocols and materials databases

StructuralBiologyKnowledgebase

Family and domain databases

Gene3D

2.120.10.10. 1 hit.

InterPro

IPR001860. Glyco_hydro_34.
IPR011040. Sialidases.
[Graphical view]

Pfam

PF00064. Neur. 1 hit.
[Graphical view]

SUPFAM

SSF50939. SSF50939. 1 hit.

ProtoNet

Entry information

Entry name

F8UU09_9INFA

Accession

Primary (citable) accession number: F8UU09

Entry history

Integrated into UniProtKB/TrEMBL:	September 21, 2011
Last sequence update:	September 21, 2011
Last modified:	June 11, 2014
This is version 16 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info