viHumans
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]
Influenza A Virus (strain A/Aichi/2/1968 H3N2)
Viruses> SsRNA Viruses> SsRNA Negative-strand Viruses> Orthomyxoviridae> Alphainfluenzavirus> Influenza A Virus> H3N2 Subtype> Influenza A Virus (strain A/Aichi/2/1968 H3N2)
Not Available
Various pathway(s) in which protein is involved
Not Available
Not Available
MKTIIALSYIFCLALGQDLPGNDNSTATLCLGHHAVPNGTLVKTITDDQIEVTNATELVQSSSTGKICNNPHRILDGIDCTLIDALLGDPHCDVFQNETW
DLFVERSKAFSNCYPYDVPDYASLRSLVASSGTLEFITEGFTWTGVTQNGGSNACKRGPGSGFFSRLNWLTKSGSTYPVLNVTMPNNDNFDKLYIWGIHH
PSTNQEQTSLYVQASGRVTVSTRRSQQTIIPNIGSRPWVRGLSSRISIYWTIVKPGDVLVINSNGNLIAPRGYFKMRTGKSSIMRSDAPIDTCISECITP
NGSIPNDKPFQNVNKITYGACPKYVKQNTLKLATGMRNVPEKQTRGLFGAIAGFIENGWEGMIDGWYGFRHQNSEGTGQAADLKSTQAAIDQINGKLNRV
IEKTNEKFHQIEKEFSEVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNKLFEKTRRQLRENAEEMGNGCFKIYHKCDNACIESIRNG
TYDHDVYRDEALNNRFQIKGVELKSGYKDWILWISFAISCFLLCVVLLGFIMWACQRGNIRCNICI
566
Not Available
Not Available
21-07-1986
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.
Not Available
GO:0016021  ;   GO:0019031  ;   GO:0019062  ;   GO:0019064  ;   GO:0020002  ;  
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. .
Not Available
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X-ray crystallography (25)
1EO8  1FYT  1HA0  1HGG  1HTM  1J8H  1KEN  1KG0  1PYW  1QFU  1QU1  2HMG  2VIR  2VIS  2VIT  
2VIU  2YPG  3EYM  3HMG  3S4S  3S5L  3VUN  4C56  4HMG  5HMG  
Not Available
Protein couldn't be modeled using I-Tasser and Raptor X because of length constraints of the software.
CHEMBL1932897            
Not Applicable