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Q207Z6 (Q207Z6_9INFA) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 55. 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 length568 AA.
Sequence statusComplete.
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. SAAS SAAS000149 RuleBase RU003324

Subunit structure

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

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 SAAS SAAS000149 RuleBase RU003324
Virion
   DomainTransmembrane
Transmembrane helix SAAS SAAS000149
   Molecular functionHemagglutinin SAAS SAAS000149 RuleBase RU003324
   PTMDisulfide bond SAAS SAAS000149
   Technical term3D-structure PDB 4BH0 PDB 4BH1 PDB 4BGZ
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

Region137 – 1415Phosphate 3 binding PDB 4BH0 PDB 4BH1 PDB 4BGZ
Region137 – 1415Phosphate 4 binding PDB 4BH0
Region148 – 1492Phosphate 5 binding PDB 4BGZ
Region237 – 2382Galactose binding PDB 4BH0 PDB 4BH1
Region413 – 4153Phosphate 7 binding PDB 4BH0

Sites

Binding site1041Phosphate 1 PDB 4BH1
Binding site1181Phosphate 2; via carbonyl oxygen PDB 4BH0
Binding site1781Phosphate 3 PDB 4BH0 PDB 4BH1
Binding site2261Phosphate 6; via carbonyl oxygen PDB 4BH0
Binding site2381Phosphate 5 PDB 4BGZ
Binding site2431Phosphate 6 PDB 4BH0
Binding site4751Phosphate 8 PDB 4BGZ

Amino acid modifications

Glycosylation391N-linked (GlcNAc...) PDB 4BGZ
Glycosylation1811N-linked (GlcNAc...) PDB 4BH0 PDB 4BH1 PDB 4BGZ

Sequences

Sequence LengthMass (Da)Tools
Q207Z6 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 4763F22A2A73A57B

FASTA56864,248
        10         20         30         40         50         60 
MEKIVLLLAI VSLVKSDQIC IGYHANNSTE QVDTIMEKNV TVTHAQDILE KTHNGKLCDL 

        70         80         90        100        110        120 
DGVKPLILRD CSVAGWLLGN PMCDEFLNVP EWSYIVEKIN PANDLCYPGN FNDYEELKHL 

       130        140        150        160        170        180 
LSRINHFEKI QIIPKSSWSD HEASAGVSSA CPYQGRSSFF RNVVWLIKKD NAYPTIKRSY 

       190        200        210        220        230        240 
NNTNQEDLLV LWGIHHPNDA AEQTRLYQNP TTYISVGTST LNQRLVPKIA TRSKVNGQSG 

       250        260        270        280        290        300 
RMEFFWTILK PNDAINFESN GNFIAPENAY KIVKKGDSTI MKSELEYGNC NTKCQTPIGA 

       310        320        330        340        350        360 
INSSMPFHNI HPLTIGECPK YVKSSRLVLA TGLRNSPQGE 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 
NGCFEFYHRC DNECMESVRN GTYDYPQYSE EARLKREEIS GVKLESIGTY QILSIYSTVA 

       550        560 
SSLALAIMVA GLSLWMCSNG SLQCRICI 

« Hide

References

[1]"First incursion of H5N1 highly pathogenic avian influenza viruses of the 'Asian' lineage into Europe."
Londt B.Z., Brown I.H.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A/turkey/Turkey/1/2005 EMBL ABD73284.1.
[2]Lin Y.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A/turkey/Turkey/1/2005 EMBL ABQ58921.1.
[3]"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 (2.15 ANGSTROMS) OF 17-338 AND 347-512 IN COMPLEX WITH GALACTOSE AND PHOSPHATE, GLYCOSYLATION AT ASN-39 AND ASN-181.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ407519 Genomic RNA. Translation: ABD73284.1.
EF619980 Viral cRNA. Translation: ABQ58921.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BGZX-ray2.68A/C/E17-338[»]
B/D/F347-512[»]
4BH0X-ray2.36A/C/E17-338[»]
B/D/F347-512[»]
4BH1X-ray2.15A/C/E17-338[»]
B/D/F347-512[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60225N.

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...

Entry information

Entry nameQ207Z6_9INFA
AccessionPrimary (citable) accession number: Q207Z6
Entry history
Integrated into UniProtKB/TrEMBL: April 18, 2006
Last sequence update: April 18, 2006
Last modified: February 19, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)