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Q6DQ34 (Q6DQ34_9INFA) Unreviewed, UniProtKB/TrEMBL

Last modified March 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein attributes

Sequence length565 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore By similarity. RuleBase RU003324 SAAS SAAS000149

Subunit structure

Homotrimer of disulfide-linked HA1-HA2 By similarity. RuleBase RU003324 SAAS SAAS000149

Subcellular location

Virion membrane; Single-pass type I membrane protein. Host apical cell membrane; Single-pass type I membrane protein By similarity SAAS SAAS000149.

Sequence similarities

Belongs to the influenza viruses hemagglutinin family. RuleBase RU003324

Ontologies

Keywords
   Biological processClathrin- and caveolin-independent endocytosis of virus by host SAAS SAAS000149
Clathrin-mediated endocytosis of virus by host SAAS SAAS000149
Fusion of virus membrane with host endosomal membrane SAAS SAAS000149
Fusion of virus membrane with host membrane
Host-virus interaction
Viral attachment to host cell SAAS SAAS000149
Viral penetration into host cytoplasm
Virus endocytosis by host
Virus entry into host cell
   Cellular componentHost cell membrane SAAS SAAS000149
Host membrane
Membrane
Viral envelope protein RuleBase RU003324 SAAS SAAS000149
Virion
   DomainTransmembrane
Transmembrane helix SAAS SAAS000149
   Molecular functionHemagglutinin RuleBase RU003324 SAAS SAAS000149
   PTMDisulfide bond SAAS SAAS000149
   Technical term3D-structure PDB 4BGY PDB 4BGW PDB 4BGX PDB 3ZNK PDB 3ZNL PDB 3ZNM PDB 3ZP0 PDB 3ZP1 PDB 3ZP2 PDB 3ZP3 PDB 3ZP6 PDB 3ZPA PDB 3ZPB
Gene Ontology (GO)
   Biological_processclathrin-mediated endocytosis of virus by host cell

Inferred from electronic annotation. Source: UniProtKB-KW

fusion of virus membrane with host endosome membrane

Inferred from electronic annotation. Source: UniProtKB-KW

fusion of virus membrane with host plasma membrane

Inferred from electronic annotation. Source: InterPro

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral envelope

Inferred from electronic annotation. Source: UniProtKB-KW

virion membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region237 – 2382Galactose binding PDB 4BGY PDB 4BGX PDB 3ZP0 PDB 3ZPB

Sites

Binding site2341Fucose

Amino acid modifications

Glycosylation271N-linked (GlcNAc...) PDB 3ZP3
Glycosylation391N-linked (GlcNAc...) PDB 4BGY PDB 4BGW PDB 4BGX PDB 3ZNK PDB 3ZNL PDB 3ZNM PDB 3ZP2 PDB 3ZP6
Glycosylation1811N-linked (GlcNAc...) PDB 4BGY PDB 4BGW PDB 4BGX PDB 3ZNK PDB 3ZNL PDB 3ZNM PDB 3ZP2 PDB 3ZP6 PDB 3ZPA PDB 3ZPB
Glycosylation5001N-linked (GlcNAc...)

Experimental info

Non-terminal residue5651 EMBL AAT73273.1

Sequences

Sequence LengthMass (Da)Tools
Q6DQ34 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: F2ACE6D25A5A2B34

FASTA56564,105
        10         20         30         40         50         60 
MEKIVLLFAI VSLVKSDQIC IGYHANNSTE QVDTIMEKNV TVTHAQDILE KTHNGKLCDL 

        70         80         90        100        110        120 
DGVKPLILRD CSVAGWLLGN PMCDEFINVP EWSYIVEKAN PVNDLCYPGD FNDYEELKHL 

       130        140        150        160        170        180 
LSRINHFEKI QIIPKSSWSS HEASLGVSSA CPYQGKSSFF RNVVWLIKKN STYPTIKRSY 

       190        200        210        220        230        240 
NNTNQEDLLV LWGIHHPNDA AEQTKLYQNP TTYISVGTST LNQRLVPRIA TRSKVNGQSG 

       250        260        270        280        290        300 
RMEFFWTILK PNDAINFESN GNFIAPEYAY KIVKKGDSTI MKSELEYGNC NTKCQTPMGA 

       310        320        330        340        350        360 
INSSMPFHNI HPLTIGECPK YVKSNRLVLA TGLRNSPQRE RRRKKRGLFG AIAGFIEGGW 

       370        380        390        400        410        420 
QGMVDGWYGY HHSNEQGSGY AADKESTQKA IDGVTNKVNS IIDKMNTQFE AVGREFNNLE 

       430        440        450        460        470        480 
RRIENLNKKM EDGFLDVWTY NAELLVLMEN ERTLDFHDSN VKNLYDKVRL QLRDNAKELG 

       490        500        510        520        530        540 
NGCFEFYHKC DNECMESVRN GTYDYPQYSE EARLKREEIS GVKLESIGIY QILSIYSTVA 

       550        560 
SSLALAIMVA GLSLWMCSNG SLQCR 

« Hide

References

[1]"Genesis of a highly pathogenic and potentially pandemic H5N1 influenza virus in eastern Asia."
Li K.S., Guan Y., Wang J., Smith G.J.D., Xu K.M., Duan L., Rahardjo A.P., Puthavathana P., Buranathai C., Nguyen T.D., Estoepangestie A.T.S., Chaisingh A., Auewarakul P., Long H.T., Hanh N.T.H., Webby R.J., Poon L.L.M., Chen H. expand/collapse author list , Shortridge K.F., Yuen K.Y., Webster R.G., Peiris J.S.M.
Nature 430:209-213(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A/Viet Nam/1194/2004 EMBL AAT73273.1.
[2]"Receptor binding by a ferret-transmissible H5 avian influenza virus."
Xiong X., Coombs P.J., Martin S.R., Liu J., Xiao H., McCauley J.W., Locher K., Walker P.A., Collins P.J., Kawaoka Y., Skehel J.J., Gamblin S.J.
Nature 497:392-396(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 17-340 AND 347-512 IN COMPLEX WITH GALACTOSE, GLYCOSYLATION AT ASN-39; ASN-181 AND ASN-500.
[3]"Changes in the hemagglutinin of H5N1 viruses during human infection--influence on receptor binding."
Crusat M., Liu J., Palma A.S., Childs R.A., Liu Y., Wharton S.A., Lin Y.P., Coombs P.J., Martin S.R., Matrosovich M., Chen Z., Stevens D.J., Hien V.M., Thanh T.T., Nhu l.e. .N.T., Nguyet L.A., Ha d.o. .Q., van Doorn H.R. expand/collapse author list , Hien T.T., Conradt H.S., Kiso M., Gamblin S.J., Chai W., Skehel J.J., Hay A.J., Farrar J., de Jong M.D., Feizi T.
Virology 447:326-337(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-340 AND 347-506 IN COMPLEX WITH GALACTOSE, GLYCOSYLATION AT ASN-27; ASN-39 AND ASN-181.
[4]"Recognition of sulphated and fucosylated receptor sialosides by A/Vietnam/1194/2004 (H5N1) influenza virus."
Xiong X., Tuzikov A., Coombs P.J., Martin S.R., Walker P.A., Gamblin S.J., Bovin N., Skehel J.J.
Virus Res. 178:12-14(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 17-340 AND 347-512 IN COMPLEX WITH FUCOSE, GLYCOSYLATION AT ASN-39; ASN-181 AND ASN-500.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY651333 Viral cRNA. Translation: AAT73273.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZNKX-ray2.71A/C/E17-340[»]
3ZNLX-ray2.50A/C/E17-340[»]
B/D/F347-512[»]
3ZNMX-ray2.40A/C/E17-340[»]
B/D/F347-512[»]
3ZP0X-ray2.51E1-340[»]
F347-506[»]
3ZP1X-ray2.60E17-342[»]
F347-512[»]
3ZP2X-ray2.50E17-342[»]
F347-512[»]
3ZP3X-ray2.65E1-340[»]
F347-506[»]
3ZP6X-ray2.60E1-340[»]
F347-506[»]
3ZPAX-ray2.50E1-340[»]
F347-506[»]
3ZPBX-ray2.60E1-340[»]
F347-506[»]
4BGWX-ray2.48A17-340[»]
B347-512[»]
4BGXX-ray2.48A17-340[»]
B347-512[»]
4BGYX-ray2.68A17-340[»]
B347-512[»]
ProteinModelPortalQ6DQ34.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60226N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.10.77.10. 1 hit.
3.90.20.10. 1 hit.
3.90.209.20. 1 hit.
InterProIPR008980. Capsid_hemagglutn.
IPR013828. Hemagglutn_HA1_a/b_dom.
IPR013827. Hemagglutn_HA1_b-rbn_dom.
IPR000149. Hemagglutn_influenz_A.
IPR001364. Hemagglutn_influenz_A/B.
IPR013829. Hemagglutn_stalk.
[Graphical view]
PfamPF00509. Hemagglutinin. 1 hit.
[Graphical view]
PRINTSPR00330. HEMAGGLUTN1.
PR00329. HEMAGGLUTN12.
SUPFAMSSF49818. SSF49818. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ6DQ34.

Entry information

Entry nameQ6DQ34_9INFA
AccessionPrimary (citable) accession number: Q6DQ34
Entry history
Integrated into UniProtKB/TrEMBL: August 16, 2004
Last sequence update: August 16, 2004
Last modified: March 19, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)