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Q9Q2W5 (HN_NDVK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Hemagglutinin-neuraminidase
EC=3.2.1.18
Gene names
Name:HN
OrganismNewcastle disease virus (strain Kansas) (NDV)
Taxonomic identifier332244 [NCBI]
Taxonomic lineageViruses › ssRNA negative-strand viruses › Mononegavirales › Paramyxoviridae › Paramyxovirinae › Avulavirus
Virus hostGallus gallus (Chicken) [TaxID: 9031]

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion By similarity.

Neuraminidase activity ensures the efficient spread of the virus by dissociating the mature virions from the neuraminic acid containing glycoproteins By similarity.

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.

Subcellular location

Virion membrane; Single-pass type II membrane protein Potential. Host cell membrane; Single-pass type II membrane protein Potential.

Sequence similarities

Belongs to the paramyxoviruses hemagglutinin-neuraminidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 577577Hemagglutinin-neuraminidase
PRO_0000142614

Regions

Topological domain1 – 2222Cytoplasmic Potential
Transmembrane23 – 4523Helical; Potential
Topological domain46 – 571526Extracellular Potential

Amino acid modifications

Glycosylation1191N-linked (GlcNAc...); by host Potential
Glycosylation1441N-linked (GlcNAc...); by host Potential
Glycosylation3411N-linked (GlcNAc...); by host Potential
Glycosylation4331N-linked (GlcNAc...); by host Potential
Glycosylation4811N-linked (GlcNAc...); by host Potential
Glycosylation5381N-linked (GlcNAc...); by host Potential

Secondary structure

1 ............................................................................. 577
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Q2W5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6A1F03C8DD3F7753

FASTA57763,111
        10         20         30         40         50         60 
MDRAVSQVAL ENDEREAKNT WRLIFRIAIL LLTVVTLATS VASLVYSMGA STPSDLVGIP 

        70         80         90        100        110        120 
TRISRAEEKI TSALGSNQDV VDRIYKQVAL ESPLALLNTE TTIMNAITSL SYQINGAANN 

       130        140        150        160        170        180 
SGWGAPIHDP DFIGGIGKEL IVDNASDVTS FYPSAFQEHL NFIPAPTTGS GCTRIPSFDM 

       190        200        210        220        230        240 
SATHYCYTHN VILSGCRDHS HSHQYLALGV LRTTATGRIF FSTLRSISLD DTQNRKSCSV 

       250        260        270        280        290        300 
SATPLGCDML CSKVTETEEE DYNSAVPTLM AHGRLGFDGQ YHEKDLDVTT LFEDWVANYP 

       310        320        330        340        350        360 
GVGGGSFIDG RVWFSVYGGL KPNSPSDTVQ EGKYVIYKRY NDTCPDEQDY QIRMAKSSYK 

       370        380        390        400        410        420 
PGRFGGKRIQ QAILSIKVST SLGEDPVLTV PPNTVTLMGA EGRILTVGTS HFLYQRGSSY 

       430        440        450        460        470        480 
FSPALLYPMT VSNKTATLHS PYTFNAFTRP GSIPCQASAR CPNSCVTGVY TDPYPLIFYR 

       490        500        510        520        530        540 
NHTLRGVFGT MLDSEQARLN PASAVFDSTS RSRITRVSSS STKAAYTTST CFKVVKTNKT 

       550        560        570 
YCLSIAEISN TLFGEFRIVP LLVEILKNDG VREARSG

« Hide

References

[1]"Crystallization of Newcastle disease virus hemagglutinin-neuraminidase glycoprotein."
Takimoto T., Taylor G.L., Crennell S.J., Scroggs R.A., Portner A.
Virology 270:208-214(2000) [PubMed: 10772993] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase."
Crennell S., Takimoto T., Portner A., Taylor G.
Nat. Struct. Biol. 7:1068-1074(2000) [PubMed: 11062565] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 124-577.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF212323 Genomic RNA. Translation: AAF19984.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E8TX-ray2.50A/B124-577[»]
1E8UX-ray2.00A/B124-577[»]
1E8VX-ray2.00A/B124-577[»]
ProteinModelPortalQ9Q2W5.
SMRQ9Q2W5. Positions 124-572.
ModBaseSearch...

Protein family/group databases

CAZyGH83. Glycoside Hydrolase Family 83.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000665. Hemagglutn-neuramid_glycoprot.
IPR016285. Hemagglutn-neuramid_paramyxo.
IPR011040. Neuraminidase.
[Graphical view]
Gene3DG3DSA:2.120.10.10. Neuraminidase. 1 hit.
PfamPF00423. HN. 1 hit.
[Graphical view]
PIRSFPIRSF001072. Hemagglut-neuramid_paramyxoV. 1 hit.
SUPFAMSSF50939. Sialidase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHN_NDVK
AccessionPrimary (citable) accession number: Q9Q2W5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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