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UniProtKB/Swiss-Prot entry P09345


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HEMA_I59A0
Primary accession number P09345
Secondary accession number Q0A2H6
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on November 13, 2007 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 69)
Name and origin of the protein
Protein name Hemagglutinin [Precursor]
Synonyms None
Contains Hemagglutinin HA1 chain
Hemagglutinin HA2 chain
Gene name
Name: HA
From
Influenza A virus (strain A/Chicken/Scotland/1959 H5N1) [TaxID: 173721] 
Taxonomy Viruses; ssRNA negative-strand viruses; Orthomyxoviridae; Influenzavirus A.
Virus hosts Aves [TaxID: 8782]
Felis silvestris catus (Cat) [TaxID: 9685]
Homo sapiens (Human) [TaxID: 9606]
Panthera pardus (Leopard) [TaxID: 9691]
Panthera tigris (Tiger) [TaxID: 9694]
Sus scrofa (Pig) [TaxID: 9823]
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
DOI=10.1093/nar/16.9.4181; PubMed=3375087 [NCBI, ExPASy, EBI, Israel, Japan]
De B.K., Brownlee G.G., Kendal A.P., Shaw M.W.;
"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.";
Nucleic Acids Res. 16:4181-4182(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
DOI=10.1126/science.1121586; PubMed=16439620 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Large-scale sequence analysis of avian influenza isolates.";
Science 311:1576-1580(2006).
Comments
  • FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. 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 induce an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.
  • SUBUNIT: Homotrimer of disulfide-linked HA1-HA2.
  • SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein (Potential). 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.
  • PTM: 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).
  • PTM: Palmitoylated (By similarity).
  • MISCELLANEOUS: Major glycoprotein, comprises over 80% of the envelope proteins present in virus particle.
  • MISCELLANEOUS: 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.
  • MISCELLANEOUS: 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.
  • SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X07826; CAA30680.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07869; CAA30719.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CY015081; ABI85106.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP Q9DLP3; 1JSM. [HSSP ENTRY / PDB]
SMR P09345; 17-337.
ModBase P09345.
Ontologies
GO
GO:0016324; Cellular component: apical plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0055036; Cellular component: virion membrane (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
InterPro IPR000149; Hemagglutn_influenz_HA1.
IPR001364; Hemagglutn_influenz_HA1/HA2.
IPR013829; Hemagglutn_stalk.
Graphical view of domain structure.
Gene3D G3DSA:3.90.20.10; Haemagglutn_stalk; 1.
Pfam PF00509; Hemagglutinin; 1.
Pfam graphical view of domain structure.
PRINTS PR00330; HEMAGGLUTN1.
PR00329; HEMAGGLUTN12.
ProDom PD000225; Hemagglutn; 1.
[Domain structure / List of seq. sharing at least 1 domain]
BLOCKS P09345.
Other
ProtoNet P09345.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Cleavage on pair of basic residues; Complete proteome; Envelope protein; Fusion protein; Glycoprotein; Hemagglutinin; Lipoprotein; Membrane; Palmitate; Signal; Transmembrane; Virion.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    16  16      
CHAIN   17   341  325     Hemagglutinin HA1 chain. PRO_0000038899
CHAIN   343   564  222     Hemagglutinin HA2 chain. PRO_0000038900
TOPO_DOM   17   527  511     Extracellular (Potential). 
TRANSMEM   528   548  21     Potential. 
TOPO_DOM   549   564  16     Cytoplasmic (Potential). 
SITE   342   343  2     Cleavage; by host (By similarity). 
LIPID   553   553        S-palmitoyl cysteine; by host (By similarity). 
LIPID   560   560        S-palmitoyl cysteine; by host (By similarity). 
LIPID   563   563        S-palmitoyl cysteine; by host (By similarity). 
CARBOHYD   26    26        N-linked (GlcNAc...) (Potential). 
CARBOHYD   39    39        N-linked (GlcNAc...) (Potential). 
CARBOHYD   181   181        N-linked (GlcNAc...) (Potential). 
CARBOHYD   302   302        N-linked (GlcNAc...) (Potential). 
CARBOHYD   496   496        N-linked (GlcNAc...) (Potential). 
DISULFID   20   479        Interchain (between HA1 and HA2 chains) (By similarity). 
DISULFID   58   290        By similarity. 
DISULFID   71    83        By similarity. 
DISULFID   106   151        By similarity. 
DISULFID   294   318        By similarity. 
DISULFID   486   490        By similarity. 
CONFLICT   89    89        V -> L (in Ref. 1; CAA30719/CAA30680). 
CONFLICT   93    93        S -> L (in Ref. 1; CAA30719/CAA30680). 
CONFLICT   119   119        H -> Y (in Ref. 1; CAA30719/CAA30680). 
CONFLICT   131   131        Q -> R (in Ref. 1; CAA30719/CAA30680). 
CONFLICT   160   160        F -> L (in Ref. 1; CAA30719/CAA30680). 
CONFLICT   170   172        DNA -> NNT (in Ref. 1; CAA30719/CAA30680). 
CONFLICT   267   267        E -> R (in Ref. 1; CAA30719/CAA30680). 
CONFLICT   300   300        A -> E (in Ref. 1; CAA30719/CAA30680). 
CONFLICT   404   406        QFK -> RFE (in Ref. 1; CAA30719/CAA30680). 
CONFLICT   458   458        K -> N (in Ref. 1; CAA30719/CAA30680). 
Sequence information
Length: 564 AA [This is the length of the unprocessed precursor] Molecular weight: 63671 Da [This is the MW of the unprocessed precursor] CRC64: 5C57790D6B76255F [This is a checksum on the sequence]
        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 

P09345 in FASTA format

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