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Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]

 B5ALP7_9INFA            Unreviewed;       566 AA.
B5ALP7;
23-SEP-2008, integrated into UniProtKB/TrEMBL.
23-SEP-2008, sequence version 1.
10-APR-2019, entry version 66.
RecName: Full=Hemagglutinin {ECO:0000256|HAMAP-Rule:MF_04072};
Contains:
RecName: Full=Hemagglutinin HA2 chain {ECO:0000256|HAMAP-Rule:MF_04072};
Contains:
RecName: Full=Hemagglutinin HA1 chain {ECO:0000256|HAMAP-Rule:MF_04072};
Name=HA {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000313|EMBL:ACF36453.1};
Influenza A virus (A/Hong Kong/CUHK7546/2005(H3N2)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Negarnaviricota; Polyploviricotina; Insthoviricetes; Articulavirales;
Orthomyxoviridae; Alphainfluenzavirus.
NCBI_TaxID=499510 {ECO:0000313|EMBL:ACF36453.1};
[1] {ECO:0000313|EMBL:ACF36453.1}
NUCLEOTIDE SEQUENCE.
STRAIN=A/Hong Kong/CUHK7546/2005 {ECO:0000313|EMBL:ACF36453.1};
PubMed=18648550; DOI=10.1371/journal.pone.0002768;
Tang J.W., Ngai K.L., Lam W.Y., Chan P.K.;
"Seasonality of influenza A(H3N2) virus: a Hong Kong perspective
(1997-2006).";
PLoS ONE 3:e2768-e2768(2008).
-!- FUNCTION: 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. {ECO:0000256|HAMAP-
Rule:MF_04072, ECO:0000256|SAAS:SAAS01039073}.
-!- FUNCTION: 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.
{ECO:0000256|RuleBase:RU003324}.
-!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2.
{ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|RuleBase:RU003324,
ECO:0000256|SAAS:SAAS00070616}.
-!- SUBCELLULAR LOCATION: Host apical cell membrane
{ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|SAAS:SAAS00554492};
Single-pass type I membrane protein {ECO:0000256|HAMAP-
Rule:MF_04072, ECO:0000256|SAAS:SAAS00554492}. Virion membrane
{ECO:0000256|HAMAP-Rule:MF_04072}; Single-pass type I membrane
protein {ECO:0000256|HAMAP-Rule:MF_04072}. 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. {ECO:0000256|HAMAP-Rule:MF_04072}.
-!- 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. {ECO:0000256|HAMAP-
Rule:MF_04072}.
-!- PTM: Palmitoylated. {ECO:0000256|HAMAP-Rule:MF_04072}.
-!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
{ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|RuleBase:RU003324,
ECO:0000256|SAAS:SAAS00963381}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04072}.
-----------------------------------------------------------------------
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EMBL; EU857088; ACF36453.1; -; Viral_cRNA.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0046789; F:host cell surface receptor binding; IEA:UniProtKB-UniRule.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-UniRule.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
GO; GO:0046761; P:viral budding from plasma membrane; IEA:UniProtKB-UniRule.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
Gene3D; 3.90.209.20; -; 1.
HAMAP; MF_04072; INFV_HEMA; 1.
InterPro; IPR008980; Capsid_hemagglutn.
InterPro; IPR013828; Hemagglutn_HA1_a/b_dom_sf.
InterPro; IPR000149; Hemagglutn_influenz_A.
InterPro; IPR001364; Hemagglutn_influenz_A/B.
Pfam; PF00509; Hemagglutinin; 1.
PRINTS; PR00330; HEMAGGLUTN1.
PRINTS; PR00329; HEMAGGLUTN12.
SUPFAM; SSF49818; SSF49818; 1.
3: Inferred from homology;
Clathrin- and caveolin-independent endocytosis of virus by host
{ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|SAAS:SAAS01039036};
Clathrin-mediated endocytosis of virus by host {ECO:0000256|HAMAP-
Rule:MF_04072, ECO:0000256|SAAS:SAAS01038958};
Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963411};
Fusion of virus membrane with host endosomal membrane
{ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|SAAS:SAAS00963419};
Fusion of virus membrane with host membrane {ECO:0000256|HAMAP-
Rule:MF_04072, ECO:0000256|SAAS:SAAS00963419};
Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04072};
Hemagglutinin {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|RuleBase:RU003324, ECO:0000256|SAAS:SAAS00963391};
Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963415};
Host membrane {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963415};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963390};
Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04072};
Membrane {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963387, ECO:0000256|SAAS:SAAS00963415};
Palmitate {ECO:0000256|HAMAP-Rule:MF_04072};
Signal {ECO:0000256|HAMAP-Rule:MF_04072};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963387};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963387};
Viral attachment to host cell {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963390};
Viral envelope protein {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|RuleBase:RU003324, ECO:0000256|SAAS:SAAS00963382};
Viral penetration into host cytoplasm {ECO:0000256|HAMAP-
Rule:MF_04072, ECO:0000256|SAAS:SAAS00963419,
ECO:0000256|SAAS:SAAS01038958, ECO:0000256|SAAS:SAAS01039036};
Virion {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|RuleBase:RU003324, ECO:0000256|SAAS:SAAS00963382,
ECO:0000256|SAAS:SAAS00963390};
Virus endocytosis by host {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS01038958, ECO:0000256|SAAS:SAAS01039036};
Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963390, ECO:0000256|SAAS:SAAS00963419,
ECO:0000256|SAAS:SAAS01038958, ECO:0000256|SAAS:SAAS01039036}.
TRANSMEM 530 554 Helical. {ECO:0000256|HAMAP-
Rule:MF_04072}.
SITE 345 346 Cleavage; by host. {ECO:0000256|HAMAP-
Rule:MF_04072}.
LIPID 555 555 S-palmitoyl cysteine; by host.
{ECO:0000256|HAMAP-Rule:MF_04072}.
LIPID 562 562 S-palmitoyl cysteine; by host.
{ECO:0000256|HAMAP-Rule:MF_04072}.
LIPID 565 565 S-palmitoyl cysteine; by host.
{ECO:0000256|HAMAP-Rule:MF_04072}.
DISULFID 80 92 {ECO:0000256|HAMAP-Rule:MF_04072}.
DISULFID 297 321 {ECO:0000256|HAMAP-Rule:MF_04072}.
DISULFID 489 493 {ECO:0000256|HAMAP-Rule:MF_04072}.
SEQUENCE 566 AA; 63544 MW; AE2EB2FBE7CE2BE8 CRC64;
MKTIIALSYI LCLVFAQKLP GNDNSTATLC LGHHAVPNGT IVKTITNDQI EVTNATELVQ
SSSTGGICDS PHQILDGKNC TLIDALLGDP QCDGFQNKKW DLFVERSKAY SNCYPYDVPD
YASLRSLVAS SGTLEFNNES FNWTGVTQNG TSSACKRRSN NSFFSRLNWL THLKFKYPAL
NVTMPNNEKF DKLYIWGVHH PGTDNDQISL YAQASGRITV STKRSQQTVI PNIGSRPRVR
DISSRISIYW TIVKPGDILL INSTGNLIAP RGYFKIRSGK SSIMRSDAPI GKCNSECITP
NGSIPNDKPF QNVNRITYGA CPRYVKQNTL KLATGMRNVP ETQTRGIFGA IAGFIENGWE
GMVDGWYGFR HQNSEGTGQA ADLKSTQAAI NQINGKLNRL IGKTNEKFHQ IEKEFSEVEG
RIQDLEKYVE DTKIDLWSYN AELLVALENQ HTIDLTDSEM NKLFERTKKQ LRENAEDMGN
GCFKIYHKCD NACIGSIRNE TYDHDVYRDE ALNNRFQIKG VELKSGYKDW ILWISFAISC
FLLCVALLGF IMWACQKGNI RCNICI


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Pathways :
WP1002: Electron Transport Chain
WP111: Electron Transport Chain
WP1119: Electron Transport Chain
WP1339: Electron Transport Chain
WP1502: Mitochondrial biogenesis
WP1614: 1- and 2-Methylnaphthalene degradation
WP1626: Benzoate degradation via CoA ligation
WP1633: Bisphenol A degradation
WP1647: Fatty acid biosynthesis
WP1654: gamma-Hexachlorocyclohexane degradation
WP1665: Limonene and pinene degradation
WP1673: Naphthalene and anthracene degradation
WP1708: Terpenoid backbone biosynthesis
WP1996: Linoleate Biosynthesis
WP2347: vitamin B5 (pantothenate) and CoA biosynthesis Pathway
WP2434: very-long-chain-fatty-acid-biosynthesis
WP295: Electron Transport Chain
WP542: Electron Transport Chain
WP59: Electron Transport Chain
WP772: Electron Transport Chain
WP884: Electron Transport Chain

Related Genes :
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]

Bibliography :
[31017567] Epistatic interactions can moderate the antigenic effect of substitutions in haemagglutinin of influenza H3N2 virus.
[31016481] Identification of a Novel Universal Potential Epitope on the Cytoplasmic Tail of H7N9 Virus Hemagglutinin.
[31014196] Continuing evolution of highly pathogenic H5N1 viruses in Bangladeshi live poultry markets.
[31014029] Influenza Hemagglutinin and Neuraminidase: Yin⁻Yang Proteins Coevolving to Thwart Immunity.
[31008587] Hydrogen-deuterium exchange supports independent membrane-interfacial fusion peptide and transmembrane domains in subunit 2 of influenza virus hemagglutinin protein, a structured and aqueous-protected connection between the fusion peptide and soluble ectodomain, and the importance of membrane apposition by the trimer-of-hairpins structure.
[31007873] Structural Insights for Anti-Influenza Vaccine Design.
[31005703] Hydrophobic-interaction chromatography for purification of influenza A and B virus.
[31005427] Efficient influenza A virus production in high cell density using the novel porcine suspension cell line PBG.PK2.1.
[31004012] Prolonged evolution of the memory B cell response induced by a replicating adenovirus-influenza H5 vaccine.
[31001638] Risk assessment of the tropism & pathogenesis of the highly pathogenic avian influenza A/H7N9 virus using ex vivo & in vitro cultures of human respiratory tract.