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P03453 (HEMA_I77AB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 98. 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/USSR/90/1977 H1N1) [Complete proteome]
Taxonomic identifier381516 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length566 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.

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 – 1717 Potential
Chain18 – 343326Hemagglutinin HA1 chain
PRO_0000039063
Chain345 – 566222Hemagglutinin HA2 chain
PRO_0000039064

Regions

Topological domain18 – 529512Extracellular Potential
Transmembrane530 – 55021Helical; Potential
Topological domain551 – 56616Cytoplasmic Potential

Sites

Site344 – 3452Cleavage; by host By similarity

Amino acid modifications

Lipidation5551S-palmitoyl cysteine; by host By similarity
Lipidation5621S-palmitoyl cysteine; by host By similarity
Lipidation5651S-palmitoyl cysteine; by host By similarity
Glycosylation271N-linked (GlcNAc...); by host Potential
Glycosylation281N-linked (GlcNAc...); by host Potential
Glycosylation401N-linked (GlcNAc...); by host Potential
Glycosylation1041N-linked (GlcNAc...); by host Potential
Glycosylation1441N-linked (GlcNAc...); by host Potential
Glycosylation1721N-linked (GlcNAc...); by host Potential
Glycosylation1771N-linked (GlcNAc...); by host Potential
Glycosylation2861N-linked (GlcNAc...); by host Potential
Glycosylation3041N-linked (GlcNAc...); by host Potential
Glycosylation4981N-linked (GlcNAc...); by host Potential
Disulfide bond21 ↔ 481Interchain (between HA1 and HA2 chains) By similarity
Disulfide bond59 ↔ 292 By similarity
Disulfide bond72 ↔ 84 By similarity
Disulfide bond296 ↔ 320 By similarity
Disulfide bond488 ↔ 492 By similarity

Experimental info

Sequence conflict131S → A in AAA43206. Ref.1
Sequence conflict1801K → S in AAA43206. Ref.1
Sequence conflict2961Missing in AAA43240. Ref.4
Sequence conflict4581N → S in AAA43206. Ref.1
Sequence conflict4621L → A in AAA43206. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P03453 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: D23D848AB2A6793B

FASTA56663,587
        10         20         30         40         50         60 
MKAKLLVLLC ALSATDADTI CIGYHANNST DTVDTVLEKN VTVTHSVNLL EDSHNGKLCR 

        70         80         90        100        110        120 
LKGIAPLQLG KCNIAGWILG NPECESLFSK KSWSYIAETP NSENGTCYPG YFADYEELRE 

       130        140        150        160        170        180 
QLSSVSSFER FEIFPKERSW PKHNVTRGVT ASCSHKGKSS FYRNLLWLTE KNGSYPNLSK 

       190        200        210        220        230        240 
SYVNNKEKEV LVLWGVHHPS NIEDQKTIYR KENAYVSVVS SNYNRRFTPE IAERPKVRGQ 

       250        260        270        280        290        300 
AGRINYYWTL LEPGDTIIFE ANGNLIAPWH AFALNRGFGS GIITSNASMD ECDTKCQTPQ 

       310        320        330        340        350        360 
GAINSSLPFQ NIHPVTIGEC PKYVRSTKLR MVTGLRNIPS IQSRGLFGAI AGFIEGGWTG 

       370        380        390        400        410        420 
MIDGWYGYHH QNEQGSGYAA DQKSTQNAIN GITNKVNSVI EKMNTQFTAV GKEFNKLEKR 

       430        440        450        460        470        480 
MENLNKKVDD GFLDIWTYNA ELLVLLENER TLDFHDSNVK NLYEKVKSQL KNNAKEIGNG 

       490        500        510        520        530        540 
CFEFYHKCNN ECMESVKNGT YDYPKYSEES KLNREKIDGV KLESMGVYQI LAIYSTVASS 

       550        560 
LVLLVSLGAI SFWMCSNGSL QCRICI 

« Hide

References

[1]"Nucleotide sequence of the influenza virus A/USSR/90/77 hemagglutinin gene."
Concannon P., Cummings I.W., Salser W.A.
J. Virol. 49:276-278(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"The NIAID influenza genome sequencing project."
Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V., Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H., Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., 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].
[3]"Complete genome sequencing and analysis of selected influenza virus vaccine strains spanning six decades (1933-1999)."
Mbawuike I.N., Zhang Y., Yamada R.E., Nino D., Bui H.-H., Sette A., Couch R.B.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[4]"Identification of the binding sites to monoclonal antibodies on A/USSR/90/77 (H1N1) hemagglutinin and their involvement in antigenic drift in H1N1 influenza viruses."
Nakajima S., Nakajima K., Kendal A.P.
Virology 131:116-127(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-343.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K01330 Genomic RNA. Translation: AAA43206.1.
CY010372 Genomic RNA. Translation: ABD95350.1.
DQ508897 Genomic RNA. Translation: ABF21277.1.
K01331 Genomic RNA. Translation: AAA43240.1.
PIRHMIVUR. A04064.

3D structure databases

ProteinModelPortalP03453.
SMRP03453. Positions 18-340, 345-519.
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_I77AB
AccessionPrimary (citable) accession number: P03453
Secondary accession number(s): Q1WP09
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 17, 2007
Last modified: February 19, 2014
This is version 98 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