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P11133 (HEMA_I78A9) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 96. 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 2 chains:

  1. Hemagglutinin HA1 chain
  2. Hemagglutinin HA2 chain
Gene names
Name:HA
OrganismInfluenza A virus (strain A/Swine/Hong Kong/81/1978 H3N2)
Taxonomic identifier384484 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostAves [TaxID: 8782]
Cetacea (whales) [TaxID: 9721]
Homo sapiens (Human) [TaxID: 9606]
Phocidae (true seals) [TaxID: 9709]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length550 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_0000039075
Chain330 – 550221Hemagglutinin HA2 chain
PRO_0000039076

Regions

Topological domain1 – 514514Extracellular Potential
Transmembrane515 – 53521Helical; Potential
Topological domain536 – 55015Cytoplasmic Potential

Sites

Site329 – 3302Cleavage; by host By similarity

Amino acid modifications

Lipidation5391S-palmitoyl cysteine; by host By similarity
Lipidation5461S-palmitoyl cysteine; by host By similarity
Lipidation5491S-palmitoyl cysteine; by host By similarity
Glycosylation81N-linked (GlcNAc...); by host Potential
Glycosylation221N-linked (GlcNAc...); by host Potential
Glycosylation381N-linked (GlcNAc...); by host Potential
Glycosylation1651N-linked (GlcNAc...); by host Potential
Glycosylation2851N-linked (GlcNAc...); by host Potential
Glycosylation4831N-linked (GlcNAc...); by host Potential
Disulfide bond14 ↔ 466Interchain (between HA1 and HA2 chains) By similarity
Disulfide bond52 ↔ 277 By similarity
Disulfide bond64 ↔ 76 By similarity
Disulfide bond97 ↔ 139 By similarity
Disulfide bond281 ↔ 305 By similarity
Disulfide bond473 ↔ 477 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P11133 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 1F2A7E758C531CE8

FASTA55061,437
        10         20         30         40         50         60 
QDLPGTDNST ATLCLGHHAV PNGTIVKTIT DDQIEVTNAT ELVQSSSTGK ICNNPHKILD 

        70         80         90        100        110        120 
GIDCTLIDAL LGDPHCDVFQ DETWDLFVER SNAFSNCYPY DVPDYASLRS LVASSGTLEF 

       130        140        150        160        170        180 
ITEGFTWTGV TQNGGSNACK RGPANGFFSR LNWLTKSGST YPVLNVTMPN NDNSDKLYIW 

       190        200        210        220        230        240 
GVHHPSTNQE QTNLYVQASG RVTVSTKRSQ QTMIPNAGSR PWVRGLSSRI SIYWTIVKPG 

       250        260        270        280        290        300 
DILVINSNGN LIAPRGYFKM RTGKSSIMRS DAPIGTCSSE CITPNGSIPN DKPFQNVNKI 

       310        320        330        340        350        360 
TYGACPKYVK QNTLKLATGM RNVPEKQTRG LFGAIAGFIE NGWEGMIDGW YGFRHQNSEG 

       370        380        390        400        410        420 
TGQAADLKST QAAIDLINGK VNRVIEKTNE KFHQIEKEFS EVEGRIQDLE KYVEDTKIDL 

       430        440        450        460        470        480 
WSYNADVLVA LENQHTIDLT DSEMNKLFEK TRRQLRENAE DMGNGCFKIY HKCDNACIES 

       490        500        510        520        530        540 
IRNGTYDHDI YRDEALNNRF QIKGVELKSG YKDWILWISF AISCFLLCVV LLGFIMWACQ 

       550 
RGNIRCNICI 

« Hide

References

[1]"Origin of the hemagglutinin gene of H3N2 influenza viruses from pigs in China."
Kida H., Shortridge K.F., Webster R.G.
Virology 162:160-166(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19057 Genomic RNA. Translation: AAA43212.1.
PIRHMIVS3. B29971.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R5IX-ray2.60C/G306-318[»]
ProteinModelPortalP11133.
SMRP11133. Positions 9-502.
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...

Other

EvolutionaryTraceP11133.

Entry information

Entry nameHEMA_I78A9
AccessionPrimary (citable) accession number: P11133
Secondary accession number(s): Q84019, Q84020
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 15, 1998
Last modified: February 19, 2014
This is version 96 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references