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P09345 (HEMA_I59A0) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length564 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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

Signal peptide1 – 1616 Potential
Chain17 – 338322Hemagglutinin HA1 chain
PRO_0000038899
Propeptide339 – 3424Connecting peptide
PRO_0000392211
Chain343 – 564222Hemagglutinin HA2 chain
PRO_0000038900

Regions

Topological domain17 – 527511Extracellular Potential
Transmembrane528 – 54821Helical; Potential
Topological domain549 – 56416Cytoplasmic Potential

Sites

Site342 – 3432Cleavage; by host By similarity

Amino acid modifications

Lipidation5531S-palmitoyl cysteine; by host By similarity
Lipidation5601S-palmitoyl cysteine; by host By similarity
Lipidation5631S-palmitoyl cysteine; by host By similarity
Glycosylation261N-linked (GlcNAc...); by host Potential
Glycosylation391N-linked (GlcNAc...); by host Potential
Glycosylation1811N-linked (GlcNAc...); by host Potential
Glycosylation3021N-linked (GlcNAc...); by host Potential
Glycosylation4961N-linked (GlcNAc...); by host Potential
Disulfide bond20 ↔ 479Interchain (between HA1 and HA2 chains) By similarity
Disulfide bond58 ↔ 290 By similarity
Disulfide bond71 ↔ 83 By similarity
Disulfide bond106 ↔ 151 By similarity
Disulfide bond294 ↔ 318 By similarity
Disulfide bond486 ↔ 490 By similarity

Experimental info

Sequence conflict891V → L in CAA30719. Ref.1
Sequence conflict891V → L in CAA30680. Ref.1
Sequence conflict931S → L in CAA30719. Ref.1
Sequence conflict931S → L in CAA30680. Ref.1
Sequence conflict1191H → Y in CAA30719. Ref.1
Sequence conflict1191H → Y in CAA30680. Ref.1
Sequence conflict1311Q → R in CAA30719. Ref.1
Sequence conflict1311Q → R in CAA30680. Ref.1
Sequence conflict1601F → L in CAA30719. Ref.1
Sequence conflict1601F → L in CAA30680. Ref.1
Sequence conflict170 – 1723DNA → NNT in CAA30719. Ref.1
Sequence conflict170 – 1723DNA → NNT in CAA30680. Ref.1
Sequence conflict2671E → R in CAA30719. Ref.1
Sequence conflict2671E → R in CAA30680. Ref.1
Sequence conflict3001A → E in CAA30719. Ref.1
Sequence conflict3001A → E in CAA30680. Ref.1
Sequence conflict404 – 4063QFK → RFE in CAA30719. Ref.1
Sequence conflict404 – 4063QFK → RFE in CAA30680. Ref.1
Sequence conflict4581K → N in CAA30719. Ref.1
Sequence conflict4581K → N in CAA30680. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P09345 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: 5C57790D6B76255F

FASTA56463,671
        10         20         30         40         50         60 
MERIVLLLAI VSLVKSDQIC IGYHANKSTK QVDTIMEKNV TVTHAQDILE RTHNGKLCSL 

        70         80         90        100        110        120 
NGVKPLILRD CSVAGWLLGN PMCDEFLNVP EWSYIVEKDN PINSLCYPGD FNDYEELKHL 

       130        140        150        160        170        180 
LSSTNHFEKI QIIPRSSWSN HDASSGVSSA CPYIGRSSFF RNVVWLIKKD NAYPTIKRSY 

       190        200        210        220        230        240 
NNTNQEDLLI LWGIHHPNDA AEQTKLYQNP TTYVSVGTST LNQRSIPEIA TRPKVNGQSG 

       250        260        270        280        290        300 
RMEFFWTILK PNDAINFESN GNFIAPEYAY KIVKKGDSAI MKSGLAYGNC DTKCQTPVGA 

       310        320        330        340        350        360 
INSSMPFHNI HPHTIGECPK YVKSDRLVLA TGLRNVPQRK KRGLFGAIAG FIEGGWQGMV 

       370        380        390        400        410        420 
DGWYGYHHSN EQGSGYAADK ESTQKAIDGI TNKVNSIIDK MNTQFKAVGK EFNNLERRVE 

       430        440        450        460        470        480 
NLNKKMEDGF LDVWTYNVEL LVLMENERTL DFHDSNVKNL YDKVRLQLKD NARELGNGCF 

       490        500        510        520        530        540 
EFYHKCDNEC MESVRNGTYD YPQYSEEARL NREEISGVKL ESMGVYQILS IYSTVASSLA 

       550        560 
LAIMIAGLSF WMCSNGSLQC RICI

« Hide

References

[1]"Complete sequence of a cDNA clone of the hemagglutinin gene of influenza A/Chicken/Scotland/59 (H5N1) virus: comparison with contemporary North American and European strains."
De B.K., Brownlee G.G., Kendal A.P., Shaw M.W.
Nucleic Acids Res. 16:4181-4182(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Large-scale sequence analysis of avian influenza isolates."
Obenauer J.C., Denson J., Mehta P.K., Su X., Mukatira S., Finkelstein D.B., Xu X., Wang J., Ma J., Fan Y., Rakestraw K.M., Webster R.G., Hoffmann E., Krauss S., Zheng J., Zhang Z., Naeve C.W.
Science 311:1576-1580(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X07826 Genomic RNA. Translation: CAA30680.1.
X07869 mRNA. Translation: CAA30719.1.
CY015081 Genomic RNA. Translation: ABI85106.1.

3D structure databases

ProteinModelPortalP09345.
SMRP09345. Positions 17-337, 343-516.
ModBaseSearch...

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. Capsid_hemag. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHEMA_I59A0
AccessionPrimary (citable) accession number: P09345
Secondary accession number(s): Q0A2H6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 13, 2007
Last modified: May 1, 2013
This is version 100 of the entry and version 2 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

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