Reviewed
Aves [TaxID: 8782]; Cetacea (whales) [TaxID: 9721]; Equus Caballus (Horse) [TaxID: 9796]; 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/Equine/Tokyo/1971 H3N2)
Viruses> SsRNA Viruses> SsRNA Negative-strand Viruses> Orthomyxoviridae> Alphainfluenzavirus> Influenza A Virus> Influenza A Virus With Incomplete Names> Influenza A Virus (strain A/Equine/Tokyo/1971 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
MKTTTILILLTHWVHSQIPINDNNTATLCLGHHAVANGTLVKTLTDDQIEVTNATELVQSTSTGKICNNSYRVLDGKNCTLIDAMLGDPHCDVFQYENWD
LFVERSSAFSNCYPYDVPNYALLRSIVASSGTLEFMAEGFTWTGVTQNGGSSSCRRGSADSFFSRLNWLTKSGSSYSTLNVTMPNNDNFDKLYVWGIHHP
STNNEQTKLYVQASGRVTVSTKRSQQTILPNIGLRPWVRGQSGRVSIYWTIVKPGDVLMINSNGNLIAPRGYFKIRAGKSSIMRSDAPIDTCVSECITPN
GSIPNDKPFQNVNKITYGKCPKYVKQSTLKLATGMRNIPGKRLRGIFGAIAGFIENGWEGMIDGWYGFRHQNSEGTGQAGDLKSTQAAIDQINGKLNRVI
EKTNEKFHQIEKEFSEVEGRIQDLEKYVEDTKIDLWSYNAELLVTLENQHTIDLTDAEMNKLFERTRRQLRENAEDIGNGCFKIYHKCDNACIESIRNGT
YDHDIYRDEALNNRFQIKGVELKSGYKDWILWISFAISCFLICVVLLGFIMWACQKGNIRCNICI
LFVERSSAFSNCYPYDVPNYALLRSIVASSGTLEFMAEGFTWTGVTQNGGSSSCRRGSADSFFSRLNWLTKSGSSYSTLNVTMPNNDNFDKLYVWGIHHP
STNNEQTKLYVQASGRVTVSTKRSQQTILPNIGLRPWVRGQSGRVSIYWTIVKPGDVLMINSNGNLIAPRGYFKIRAGKSSIMRSDAPIDTCVSECITPN
GSIPNDKPFQNVNKITYGKCPKYVKQSTLKLATGMRNIPGKRLRGIFGAIAGFIENGWEGMIDGWYGFRHQNSEGTGQAGDLKSTQAAIDQINGKLNRVI
EKTNEKFHQIEKEFSEVEGRIQDLEKYVEDTKIDLWSYNAELLVTLENQHTIDLTDAEMNKLFERTRRQLRENAEDIGNGCFKIYHKCDNACIESIRNGT
YDHDIYRDEALNNRFQIKGVELKSGYKDWILWISFAISCFLICVVLLGFIMWACQKGNIRCNICI
565
Not Available
Not Available
01-02-1991
Inferred from homology
| 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
Predicted/Modelled
Not Available
Not Available
Protein couldn't be modeled using I-Tasser and Raptor X because of length constraints of the software.
Not Available
- Million Molecules
Best 20 Hit molecules
Not Available