Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P04664 (HEMA_I69A0) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hemagglutinin

Cleaved into the following chain:

  1. Hemagglutinin HA1 chain
Gene names
Name:HA
OrganismInfluenza A virus (strain A/England/878/1969 H3N2)
Taxonomic identifier387147 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Mysticeti (baleen whales) [TaxID: 9761]
Phocidae (true seals) [TaxID: 9709]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length328 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Subunit structure

Homotrimer of disulfide-linked HA1-HA2.

Subcellular location

Virion membrane; Single-pass type I membrane protein Potential. Host apical cell membrane; Single-pass type I membrane protein. Note: Targeted to the apical plasma membrane in epithelial polarized cells through a signal present in the transmembrane domain. Associated with glycosphingolipid- and cholesterol-enriched detergent-resistant lipid rafts.

Post-translational modification

In natural infection, inactive HA is matured into HA1 and HA2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in this process is secreted in lungs by Clara cells By similarity.

Palmitoylated By similarity.

Miscellaneous

Major glycoprotein, comprises over 80% of the envelope proteins present in virus particle.

The extent of infection into host organism is determined by HA. Influenza viruses bud from the apical surface of polarized epithelial cells (e.g. bronchial epithelial cells) into lumen of lungs and are therefore usually pneumotropic. The reason is that HA is cleaved by tryptase clara which is restricted to lungs. However, HAs of H5 and H7 pantropic avian viruses subtypes can be cleaved by furin and subtilisin-type enzymes, allowing the virus to grow in other organs than lungs.

The influenza A genome consist of 8 RNA segments. Genetic variation of hemagglutinin and/or neuraminidase genes results in the emergence of new influenza strains. The mechanism of variation can be the result of point mutations or the result of genetic reassortment between segments of two different strains.

Sequence similarities

Belongs to the influenza viruses hemagglutinin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 328328Hemagglutinin HA1 chain
PRO_0000038948

Amino acid modifications

Glycosylation81N-linked (GlcNAc...); by host Potential
Glycosylation221N-linked (GlcNAc...); by host Potential
Glycosylation381N-linked (GlcNAc...); by host Potential
Glycosylation631N-linked (GlcNAc...); by host Potential
Glycosylation1651N-linked (GlcNAc...); by host Potential
Glycosylation2851N-linked (GlcNAc...); by host Potential
Disulfide bond52 ↔ 277 By similarity
Disulfide bond64 ↔ 76 By similarity
Disulfide bond97 ↔ 139 By similarity
Disulfide bond281 ↔ 305 By similarity

Experimental info

Non-terminal residue11
Non-terminal residue3281

Sequences

Sequence LengthMass (Da)Tools
P04664 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 9C3A86B3A8D856FE

FASTA32836,073
        10         20         30         40         50         60 
QDLPGNDNST ATLCLGHHAV PNGTLVKTIT NDQIEVTNAT ELVQSSSTGK ICNNPHRILD 

        70         80         90        100        110        120 
GINCTLIDAL LGDPHCDVFQ DETWDLFVER SKAFSNCYPY DVPDYASLRS LVASSGTLEF 

       130        140        150        160        170        180 
ITEGFTWTGV TQNGGSNACK RGPDSGFFSR LNWLTKSGST YPVLNVTMPN NDNFDKLYIW 

       190        200        210        220        230        240 
GVHHPSTNQE QTSLYVQASG RVTVSTRRSQ QTIIPNIGSR PWVRGLSSRI SIYWTIVKPG 

       250        260        270        280        290        300 
DVLVINSNGN LIAPRGYFKM RTGKSSIMRS DAPIDTCISE CITPNGSIPN DKPFQNVNKI 

       310        320 
TYGACPKYVK QNTLKLATGM RNVPEKQT 

« Hide

References

[1]"Antigenic drift in the hemagglutinin of the Hong Kong influenza subtype: correlation of amino acid changes with alterations in viral antigenicity."
Sleigh M.J., Both G.W., Underwood P.A., Bender V.J.
J. Virol. 37:845-853(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide."
Stern L.J., Brown J.H., Jardetzky T.J., Gorga J.C., Urban R.G., Strominger J.L., Wiley D.C.
Nature 368:215-221(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 306-318.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K03335 Genomic RNA. Translation: AAA43184.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DLHX-ray2.80C/F306-318[»]
2G9HX-ray2.00C306-318[»]
ProteinModelPortalP04664.
SMRP04664. Positions 1-328.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.10.77.10. 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.
[Graphical view]
PfamPF00509. Hemagglutinin. 1 hit.
[Graphical view]
PRINTSPR00330. HEMAGGLUTN1.
PR00329. HEMAGGLUTN12.
SUPFAMSSF49818. SSF49818. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP04664.

Entry information

Entry nameHEMA_I69A0
AccessionPrimary (citable) accession number: P04664
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: February 19, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references