Reviewed
Aves [TaxID: 8782]; Cetacea (whales) [TaxID: 9721]; Homo Sapiens (Human) [TaxID: 9606]; Phocidae (true Seals) [TaxID: 9709]; Sus Scrofa (Pig) [TaxID: 9823]
HA
♦Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain
♦ Hemagglutinin HA2 chain]
♦ Hemagglutinin HA2 chain]
Influenza A Virus (strain A/X-31 H3N2)
Viruses> SsRNA Viruses> SsRNA Negative-strand Viruses> Orthomyxoviridae> Alphainfluenzavirus> Influenza A Virus> H3N2 Subtype> Influenza A Virus (strain A/X-31 H3N2)
NC_007373.1 ; CY002066.1 ; NC_007372.1 ; CY002065.1 ; NC_007371.1 ; CY002067.1 ; NC_007366.1 ;
CY002070.1 ; NC_007369.1 ; CY002064.1 ; NC_007368.1 ; CY002066.1 ; NC_007367.1 ; CY002064.1 ;
NC_007370.1 ; CY002066.1
CY002070.1 ; NC_007369.1 ; CY002064.1 ; NC_007368.1 ; CY002066.1 ; NC_007367.1 ; CY002064.1 ;
NC_007370.1 ; CY002066.1
Various pathway(s) in which protein is involved
Not Available
Not Available
MKTIIALSYIFCLALGQDLPGNDNSTATLCLGHHAVPNGTLVKTITDDQIEVTNATELVQSSSTGKICNNPHRILDGIDCTLIDALLGDPHCDVFQKETW
DLFVERSKAFSNCYPYDVPDYASLRSLVASSGTLEFITEGFTWTGVTQNGGSIACKRGPDSGFFSRLNWLTKSESTYPVLNVTMPNNDNFDKLYIWGIHH
PSTNQEQTSLYVQASGRVTVSTRRSQQTIIPNIGSRPWVRGLSSRISIYWTIVKPGDVLVINSNGNLIAPRGYFKMRTGKSSIMRSDAPIDTCISECITP
NGSIPNDKPFQNVNKITYGACPKYVKQNTLKLATGMRNVPEKQTRGLFGAIAGFIENGWEGMIDGWYGFRHQNSEGTGQAADLKSTQAAIDQINGKLNRV
IEKTNEKFHQIEKEFSEVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNKLFEKTRRQLRENAEDMGNGCFKIYHKCDNACIESIRNG
TYDHDVYRDEALNNRFQIKGVELKSGYKDWILWISFAISCFLLCVVLLGFIMWTCQRGNIRCNICI
DLFVERSKAFSNCYPYDVPDYASLRSLVASSGTLEFITEGFTWTGVTQNGGSIACKRGPDSGFFSRLNWLTKSESTYPVLNVTMPNNDNFDKLYIWGIHH
PSTNQEQTSLYVQASGRVTVSTRRSQQTIIPNIGSRPWVRGLSSRISIYWTIVKPGDVLVINSNGNLIAPRGYFKMRTGKSSIMRSDAPIDTCISECITP
NGSIPNDKPFQNVNKITYGACPKYVKQNTLKLATGMRNVPEKQTRGLFGAIAGFIENGWEGMIDGWYGFRHQNSEGTGQAADLKSTQAAIDQINGKLNRV
IEKTNEKFHQIEKEFSEVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNKLFEKTRRQLRENAEDMGNGCFKIYHKCDNACIESIRNG
TYDHDVYRDEALNNRFQIKGVELKSGYKDWILWISFAISCFLLCVVLLGFIMWTCQRGNIRCNICI
566
Not Available
Not Available
06-03-2007
Evidence at protein level
| Amino Acid | Count | % Frequency | Amino Acid | Count | % Frequency |
|---|---|---|---|---|---|
| Alanine (A) | Leucine (L) | ||||
| Arginine (R) | Lysine (K) | ||||
| Asparagine (N) | Methionine (M) | ||||
| Aspartic Acid (D) | Phenylalanine (F) | ||||
| Cysteine (C) | Proline (P) | ||||
| Glutamine (Q) | Serine (S) | ||||
| Glutamic Acid (E) | Threonine (T) | ||||
| Glycine (G) | Tryptophan (W) | ||||
| Histidine (H) | Tyrosine (Y) | ||||
| Isoleucine (I) | Valine (V) |
| % Number of Residues in Helices | % Number of Residues in Strands | % Number of Residues in Coils |
|---|---|---|
♦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.
♦ 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 either through clathrin-dependent endocytosis or through 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.
♦ 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 either through clathrin-dependent endocytosis or through 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.
Not Available
GO:0016021 ; GO:0019031 ; GO:0019062 ; GO:0019064 ; GO:0020002 ;
GO:0039654 ; GO:0046789 ; GO:0055036 ; GO:0075512
GO:0039654 ; GO:0046789 ; GO:0055036 ; GO:0075512
♦ Virion membrane
♦ Single-pass type I membrane protein . 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. .
♦ Single-pass type I membrane protein . 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. .
Not Available
Not Available
X-ray crystallography (9)
Not Available
Protein couldn't be modeled using I-Tasser and Raptor X because of length constraints of the software.