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

 S4T5T8_9INFA            Unreviewed;       566 AA.
S4T5T8;
16-OCT-2013, integrated into UniProtKB/TrEMBL.
16-OCT-2013, sequence version 1.
16-JAN-2019, entry version 31.
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:AFU09081.1};
Influenza A virus (A/Paraguay/86HCl/2009(H1N1)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Alphainfluenzavirus.
NCBI_TaxID=1230188 {ECO:0000313|EMBL:AFU09081.1};
[1] {ECO:0000313|EMBL:AFU09081.1}
NUCLEOTIDE SEQUENCE.
STRAIN=A/Paraguay/86HCl/2009 {ECO:0000313|EMBL:AFU09081.1};
PubMed=25328558; DOI=10.2174/1874357901408010009;
Espinola E.E., Amarilla A.A., Martinez M., Aquino V.H., Russomando G.;
"Influenza A H1N1pdm 2009 Virus in Paraguay: Nucleotide Point
Mutations in Hemagglutinin and Neuraminidase Genes are not Associated
with Drug Resistance.";
Open Virol. J. 8:9-13(2014).
-!- 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; JX625231; AFU09081.1; -; Viral_cRNA.
SMR; S4T5T8; -.
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};
Coiled coil {ECO:0000256|SAM:Coils};
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 531 554 Helical. {ECO:0000256|HAMAP-
Rule:MF_04072}.
COILED 382 402 {ECO:0000256|SAM:Coils}.
SITE 344 345 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 72 84 {ECO:0000256|HAMAP-Rule:MF_04072}.
DISULFID 296 320 {ECO:0000256|HAMAP-Rule:MF_04072}.
DISULFID 488 492 {ECO:0000256|HAMAP-Rule:MF_04072}.
SEQUENCE 566 AA; 63236 MW; 9EDEC0A34A96221D CRC64;
MKAILVVLLY TFATANADTL CIGYHANNST DTVDTVLEKN VTVTHSVNLL EDKHNGKLCK
LRGVAPLHLG KCNIAGWILG NPECESLSTA SSWSYIVETS SSDNGTCYPG DFIDYEELRE
QLSSVSSFER FEIFPKTSSW PNHDSNKGVT AACPHAGAKS FYKNLIWLVK KGNSYPKLSK
SYINDKGKEV LVLWGIHHPS TSADQQSLYQ NADAYVFVGT SRYSKKFKPE IAIRPKVRDQ
EGRMNYYWTL VEPGDKITFE ATGNLVVPRY AFAMERNAGS GIIISDTPVH DCNTTCQTPK
GAINTSLPFQ NIHPITIGKC PKYVKSTKLR LATGLRNVPS IQSRGLFGAI AGFIEGGWTG
MVDGWYGYHH QNEQGSGYAA DLKSTQNAID EITNKVNSVI EKMNTQFTAV GKEFNHLEKR
IENLNKKVDD GFLDIWTYNA ELLVLLENER TLDYHDSNVK NLYEKVRSQL KNNAKEIGNG
CFEFYHKCDN TCMESVKNGT YDYPKYSEEA KLNREEIDGV KLESTRIYQI LAIYSTVASS
LVLVVSLGAI SFWMCSNGSL QCRICI


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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 :
[30908021] Remarkable Structural Diversity of N-Glycan Sulfation on Influenza Vaccines.
[30905528] A computationally designed H5 antigen shows immunological breadth of coverage and protects against drifting avian strains.
[30904969] Insights into structural and inhibitory mechanisms of low pH-induced conformational change of influenza HA2 protein: a computational approach.
[30904159] Peptides with the multibasic cleavage site of the hemagglutinin from highly pathogenic influenza viruses act as cell-penetrating via binding to heparan sulfate and neuropilins.
[30903496] Amino Acid Substitutions N123D and N149D in Hemagglutinin Molecule Enhance Immunigenicity of Live Attenuated Influenza H7N9 Vaccine Strain in Experiment.
[30899824] Evolved avian influenza virus (H7N9) isolated from human cases in a middle Yangtze River city in China, from February to April 2017.
[30894620] Epitope mapping of diverse influenza Hemagglutinin drug candidates using HDX-MS.
[30889726] Fabrication of electrochemical biosensor consisted of multi-functional DNA structure/porous au nanoparticle for avian influenza virus (H5N1) in chicken serum.
[30886361] Antigenic drift originating from changes to the lateral surface of the neuraminidase head of influenza A virus.
[30885512] Efficacy of novel recombinant fowlpox vaccine against recent Mexican H7N3 highly pathogenic avian influenza virus.