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Q289M7 (HEMA_I00A1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 2 chains:

  1. Hemagglutinin HA1 chain
  2. Hemagglutinin HA2 chain
Gene names
Name:HA
OrganismInfluenza A virus (strain A/New Zealand:South Canterbury/35/2000 H1N1)
Taxonomic identifier363066 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length565 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

Subunit structure

Homotrimer of disulfide-linked HA1-HA2 By similarity.

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 By similarity.

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 – 1717 Potential
Chain18 – 342325Hemagglutinin HA1 chain
PRO_0000372867
Chain344 – 565222Hemagglutinin HA2 chain
PRO_0000372868

Regions

Topological domain18 – 528511Extracellular Potential
Transmembrane529 – 54921Helical; Potential
Topological domain550 – 56516Cytoplasmic Potential

Sites

Site343 – 3442Cleavage; by host By similarity

Amino acid modifications

Lipidation5541S-palmitoyl cysteine; by host By similarity
Lipidation5611S-palmitoyl cysteine; by host By similarity
Lipidation5641S-palmitoyl cysteine; by host By similarity
Glycosylation271N-linked (GlcNAc...); by host Potential
Glycosylation281N-linked (GlcNAc...); by host Potential
Glycosylation401N-linked (GlcNAc...); by host Potential
Glycosylation711N-linked (GlcNAc...); by host Potential
Glycosylation1041N-linked (GlcNAc...); by host Potential
Glycosylation1421N-linked (GlcNAc...); by host Potential
Glycosylation1761N-linked (GlcNAc...); by host Potential
Glycosylation3031N-linked (GlcNAc...); by host Potential
Glycosylation4971N-linked (GlcNAc...); by host Potential
Disulfide bond21 ↔ 480Interchain (between HA1 and HA2 chains) By similarity
Disulfide bond59 ↔ 291 By similarity
Disulfide bond72 ↔ 84 By similarity
Disulfide bond107 ↔ 152 By similarity
Disulfide bond295 ↔ 319 By similarity
Disulfide bond487 ↔ 491 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q289M7 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: 4EAF64E3FF5829D6

FASTA56563,239
        10         20         30         40         50         60 
MKVKLLVLLC TFTATYADTI CIGYHANNST DTVDTVLEKN VTVTHSVNLL EDSHNGKLCL 

        70         80         90        100        110        120 
LKGIAPLQLG NCSVAGWILG NPECELLISK ESWSYIVETP NPENGTCYPG YFADYEELRE 

       130        140        150        160        170        180 
QLSSVSSFER FEIFPKESSW PNHTVTGVSA SCSHNGKSSF YRNLLWLTGK NGLYPNLSKS 

       190        200        210        220        230        240 
YANNKEKEVL VLWGVHHPPN IGDQRALYHT ENAYVSVVSS HYSRRFTPEI AKRPKVRNQE 

       250        260        270        280        290        300 
GRINYYWTLL EPGDTIIFEA NGNLIAPRYA FALSRGFGSG IITSNAPMDE CDAKCQTPQG 

       310        320        330        340        350        360 
AINSSLPFQN VHPVTIGECP KYVRSAKLRM VTGLRNIPSI QSRGLFGAIA GFIEGGWTGM 

       370        380        390        400        410        420 
VDGWYGYHHQ NEQGSGYAAD QKSTQNAING ITNKVNSVIE KMNTQFTAVG KEFNKLERRM 

       430        440        450        460        470        480 
ENLNKKVDDG FLDIWTYNAE LLVLLENERT LDFHDSNVKN LYEKVKSQLK NNAKEIGNGC 

       490        500        510        520        530        540 
FEFYHKCNNE CMESVKNGTY DYPKYSEESK LNREKIDGVK LESMGVYQIL AIYSTVASSL 

       550        560 
VLLVSLGAIS FWMCSNGSLQ CRICI 

« Hide

References

[1]"The NIAID influenza genome sequencing project."
Ghedin E., Spiro D., Sengamalay N., Zaborsky J., Feldblyum T., Subbu V., Sparenborg J., Groveman L., Halpin R., Shumway M., Sitz J., Katzel D., Koo H., Salzberg S.L., Jennings L., Smit M., Wells V., Bao Y. expand/collapse author list , Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]The NIAID Influenza Genome Sequencing Consortium
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CY009204 Genomic RNA. Translation: ABD61518.1.

3D structure databases

ProteinModelPortalQ289M7.
ModBaseSearch...
MobiDBSearch...

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 nameHEMA_I00A1
AccessionPrimary (citable) accession number: Q289M7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: April 4, 2006
Last modified: February 19, 2014
This is version 51 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