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Protein

Neuraminidase

Gene

NA

Organism
Influenza A virus (A/Viet Nam/1203/2004(H5N1))
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi274 – 2741Calcium; via carbonyl oxygenCombined sources
Metal bindingi278 – 2781Calcium; via carbonyl oxygenCombined sources
Metal bindingi304 – 3041CalciumCombined sources
Metal bindingi322 – 3221Calcium; via carbonyl oxygenCombined sources
Metal bindingi324 – 3241CalciumCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationSAAS annotation, Hydrolase

Keywords - Ligandi

CalciumUniRule annotationCombined sourcesSAAS annotation, Metal-bindingUniRule annotationCombined sourcesSAAS annotation

Protein family/group databases

CAZyiGH34. Glycoside Hydrolase Family 34.

Names & Taxonomyi

Protein namesi
Recommended name:
NeuraminidaseUniRule annotationSAAS annotation (EC:3.2.1.18UniRule annotationSAAS annotation)
Gene namesi
Name:NAUniRule annotationImported
OrganismiInfluenza A virus (A/Viet Nam/1203/2004(H5N1))Imported
Taxonomic identifieri284218 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A

Subcellular locationi

  • Host apical cell membrane SAAS annotation; Single-pass type II membrane protein SAAS annotation
  • Virion membrane SAAS annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 3428HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi72 ↔ 397Combined sources
Disulfide bondi104 ↔ 109Combined sources
Disulfide bondi164 ↔ 211Combined sources
Disulfide bondi213 ↔ 218Combined sources
Disulfide bondi259 ↔ 272Combined sources
Disulfide bondi261 ↔ 270Combined sources
Disulfide bondi298 ↔ 315Combined sources
Disulfide bondi401 ↔ 426Combined sources

Post-translational modificationi

N-glycosylated.UniRule annotation

Keywords - PTMi

Disulfide bondSAAS annotation, GlycoproteinUniRule annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotationSAAS annotation

Protein-protein interaction databases

DIPiDIP-59842N.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HTYX-ray2.50A/B/C/D/E/F/G/H63-449[»]
2HU0X-ray2.95A/B/C/D/E/F/G/H63-449[»]
2HU4X-ray2.50A/B/C/D/E/F/G/H63-449[»]
3CKZX-ray1.90A63-447[»]
3CL0X-ray2.20A63-447[»]
3CL2X-ray2.54A/B/C/D/E/F/G/H63-447[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 34 family.UniRule annotationSAAS annotation

Keywords - Domaini

Transmembrane, Transmembrane helixSequence analysisSAAS annotation

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.

Q6DPL2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPNQKIITI GSICMVTGIV SLMLQIGNMI SIWVSHSIHT GNQHQSEPIS
60 70 80 90 100
NTNFLTEKAV ASVKLAGNSS LCPINGWAVY SKDNSIRIGS KGDVFVIREP
110 120 130 140 150
FISCSHLECR TFFLTQGALL NDKHSNGTVK DRSPHRTLMS CPVGEAPSPY
160 170 180 190 200
NSRFESVAWS ASACHDGTSW LTIGISGPDN GAVAVLKYNG IITDTIKSWR
210 220 230 240 250
NNILRTQESE CACVNGSCFT VMTDGPSNGQ ASHKIFKMEK GKVVKSVELD
260 270 280 290 300
APNYHYEECS CYPNAGEITC VCRDNWHGSN RPWVSFNQNL EYQIGYICSG
310 320 330 340 350
VFGDNPRPND GTGSCGPVSS NGAYGVKGFS FKYGNGVWIG RTKSTNSRSG
360 370 380 390 400
FEMIWDPNGW TETDSSFSVK QDIVAITDWS GYSGSFVQHP ELTGLDCIRP
410 420 430 440
CFWVELIRGR PKESTIWTSG SSISFCGVNS DTVGWSWPDG AELPFTIDK
Length:449
Mass (Da):49,081
Last modified:August 16, 2004 - v1
Checksum:i5FCFA35BAC5F9902
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY651447 Viral cRNA. Translation: AAT73329.1.
AY818141 Genomic RNA. Translation: AAW80723.1.
EF541467 Viral cRNA. Translation: ABP52008.1.
HM006761 Viral cRNA. Translation: ADD97097.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY651447 Viral cRNA. Translation: AAT73329.1.
AY818141 Genomic RNA. Translation: AAW80723.1.
EF541467 Viral cRNA. Translation: ABP52008.1.
HM006761 Viral cRNA. Translation: ADD97097.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HTYX-ray2.50A/B/C/D/E/F/G/H63-449[»]
2HU0X-ray2.95A/B/C/D/E/F/G/H63-449[»]
2HU4X-ray2.50A/B/C/D/E/F/G/H63-449[»]
3CKZX-ray1.90A63-447[»]
3CL0X-ray2.20A63-447[»]
3CL2X-ray2.54A/B/C/D/E/F/G/H63-447[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59842N.

Protein family/group databases

CAZyiGH34. Glycoside Hydrolase Family 34.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/Viet Nam/1203/2004Imported.
  2. "Evolution of H5N1 avian influenza viruses in Asia."
    World Health Organization Global Influenza Program Surveillance Network
    Emerg. Infect. Dis. 11:1515-1521(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/Viet Nam/1203/2004Imported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/Viet Nam/1203/2004Imported.
  4. "The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design."
    Russell R.J., Haire L.F., Stevens D.J., Collins P.J., Lin Y.P., Blackburn G.M., Hay A.J., Gamblin S.J., Skehel J.J.
    Nature 443:45-49(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 63-449 IN COMPLEX WITH CALCIUM, DISULFIDE BONDS.
  5. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/Viet Nam/1203/2004Imported.
  6. "Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants."
    Collins P.J., Haire L.F., Lin Y.P., Liu J., Russell R.J., Walker P.A., Skehel J.J., Martin S.R., Hay A.J., Gamblin S.J.
    Nature 453:1258-1261(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 63-447 IN COMPLEX WITH CALCIUM, DISULFIDE BONDS.
  7. "Acquisition of virulence mutations in avian H5N1 influenza virus during a single passage in ferrets."
    Butler J., Middleton D., Klippel J., Rockman S., Brown L., Sapats S.
    Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/Viet Nam/1203/2004Imported.

Entry informationi

Entry nameiQ6DPL2_9INFA
AccessioniPrimary (citable) accession number: Q6DPL2
Entry historyi
Integrated into UniProtKB/TrEMBL: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 6, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.