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UniProtKB/Swiss-Prot entry Q03909


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

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Entry information
Entry name HEMA_I89A7
Primary accession number Q03909
Secondary accession numbers None
Integrated into Swiss-Prot on March 6, 2007
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 55)
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/Equine/Jillin/1/1989 H3N8) [TaxID: 385585] 
Taxonomy Viruses; ssRNA negative-strand viruses; Orthomyxoviridae; Influenzavirus A.
Virus hosts Aves [TaxID: 8782]
Equus caballus (Horse) [TaxID: 9796]
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Guo Y., Wang M.G., Kawaoka Y., Gorman O.T., Ito T., Webster R.G.;
"Emergence of a new influenza A virus in horses from avian sources.";
Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
  • SUBUNIT: 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).
  • 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
M65018; AAA43151.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P03437; 1QU1. [HSSP ENTRY / PDB]
SMR Q03909; 22-348, 30-523.
ModBase Q03909.
Ontologies
GO
GO:0020002; Cellular component: host cell plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0019031; Cellular component: viral envelope (inferred from electronic annotation from UniProtKB-KW).
GO:0055036; Cellular component: virion membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0046789; Molecular function: host cell surface receptor binding (inferred from electronic annotation from InterPro).
GO:0019064; Biological process: viral envelope fusion with host membrane (inferred from electronic annotation from InterPro).
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; 2.
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]
Other
ProtoNet Q03909.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Disulfide bond; 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    21  21     Potential. 
CHAIN   22   349  328     Hemagglutinin HA1 chain. PRO_0000280189
CHAIN   351   571  221     Hemagglutinin HA2 chain. PRO_0000280190
TOPO_DOM   24   535  512     Extracellular (Potential). 
TRANSMEM   536   556  21     Potential. 
TOPO_DOM   557   571  15     Cytoplasmic (Potential). 
SITE   350   351  2     Cleavage; by host (By similarity). 
LIPID   560   560        S-palmitoyl cysteine; by host (By similarity). 
LIPID   567   567        S-palmitoyl cysteine; by host (By similarity). 
LIPID   570   570        S-palmitoyl cysteine; by host (By similarity). 
CARBOHYD   29    29        N-linked (GlcNAc...); by host (Potential). 
CARBOHYD   43    43        N-linked (GlcNAc...); by host (Potential). 
CARBOHYD   59    59        N-linked (GlcNAc...); by host (Potential). 
CARBOHYD   84    84        N-linked (GlcNAc...); by host (Potential). 
CARBOHYD   186   186        N-linked (GlcNAc...); by host (Potential). 
CARBOHYD   306   306        N-linked (GlcNAc...); by host (Potential). 
CARBOHYD   504   504        N-linked (GlcNAc...); by host (Potential). 
DISULFID   35   487        Interchain (between HA1 and HA2 chains) (By similarity). 
DISULFID   73   298        By similarity. 
DISULFID   85    97        By similarity. 
DISULFID   118   160        By similarity. 
DISULFID   302   326        By similarity. 
DISULFID   494   498        By similarity. 
Sequence information
Length: 571 AA [This is the length of the unprocessed precursor] Molecular weight: 64105 Da [This is the MW of the unprocessed precursor] CRC64: 718DAA0F291CE349 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLSLIMRTVI ALSYIFCLAF GQGLPWNDNN TATLCLGHHA VPNGTIVKTI TDDQIEVTNA 

        70         80         90        100        110        120 
TELVQSSSTG KICNNPHRIL DGGNCTLIDA LLGDPHCNVF QYETWDLFVE RTNAFSNCYP 

       130        140        150        160        170        180 
YDVPDYASLR SIVASSGTLE FFAESFTWTG VTQNGGSSAC KRGTASSFFS RLNWLTKSGN 

       190        200        210        220        230        240 
AYPLLNVTMP NNDNFDKLYI WGVHHPSTNQ EQTELYVQAS GRVTVSTRKS QQTVIPNIGS 

       250        260        270        280        290        300 
RPWVRGQSGR VSIYWTIVKP GDVLVINSNG NLIAPRGYFK VRTGKSSIMR SDAPIDTCIS 

       310        320        330        340        350        360 
ECITPNGSIP NDKPFQNVNK ITYGACPKYV KQNTLKLATG MRNVPEKQIR GIFGAIAGFI 

       370        380        390        400        410        420 
ENGWEGMIDG WYGFRHQNSE GTGQAADLKS TQAALDQING KLNRVIEKTN EKFHQIEKEF 

       430        440        450        460        470        480 
SEVEGRIQDL EKYVEDTKID LWSYNAELLV ALENQHTIDL TDSEMNKLFE KTRRQLRENA 

       490        500        510        520        530        540 
EDMGNGCFKI YHNCDNACIE SIRNGTYDHN IYRDEALNNR FQIKGVELKS GYKDWILWIS 

       550        560        570 
FAISCFLLCV VLLGFIMWAC QKGNIRCNIC F 

Q03909 in FASTA format

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