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A8CDU0 (A8CDU0_9INFA) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 49. 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 length104 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 SAAS008980
Fusion of virus membrane with host membrane
Host-virus interaction
Viral attachment to host cell SAAS SAAS008980
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 2IPK
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

Amino acid modifications

Modified residue591N-actyl X PDB 2IPK

Experimental info

Non-terminal residue11 EMBL ABV58843.2
Non-terminal residue1041 EMBL ABV58843.2

Sequences

Sequence LengthMass (Da)Tools
A8CDU0 [UniParc].

Last modified February 10, 2009. Version 2.
Checksum: D45DF6D778AB1219

FASTA10411,510
        10         20         30         40         50         60 
NGNFIAPRGY FKMRTGKSSI MRSDAPIDTC ISECITPNGS IPNDKPFQNV NKITYGACPK 

        70         80         90        100 
YVKQNTLKLA TGMRNVPEKQ TRGLFGAIAG FIENGWEGMI DGWY 

« Hide

References

[1]"Fluorogenic probes for monitoring peptide binding to class II MHC proteins in living cells."
Venkatraman P., Nguyen T.T., Sainlos M., Bilsel O., Chitta S., Imperiali B., Stern L.J.
Nat. Chem. Biol. 3:222-228(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 59-71, N-ACTYL X AT PRO-59.
[2]"The rapid molecular subtyping and pathotyping of avian influenza viruses."
Yacoub A., Kiss I., Zohari S., Hakhverdyan M., Czifra G., Mohamed N., Gyarmati P., Blomberg J., Belak S.
J. Virol. Methods 156:157-161(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A/mallard/Sweden/S90391/05 EMBL ABV58843.2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EU057721 Viral cRNA. Translation: ABV58843.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IPKX-ray2.30C59-71[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.90.20.10. 1 hit.
InterProIPR008980. Capsid_hemagglutn.
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 nameA8CDU0_9INFA
AccessionPrimary (citable) accession number: A8CDU0
Entry history
Integrated into UniProtKB/TrEMBL: November 13, 2007
Last sequence update: February 10, 2009
Last modified: June 11, 2014
This is version 49 of the entry and version 2 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)