ID F2NZC6_9INFA Unreviewed; 566 AA. AC F2NZC6; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 03-AUG-2022, entry version 56. DE RecName: Full=Hemagglutinin {ECO:0000256|HAMAP-Rule:MF_04072}; DE Contains: DE RecName: Full=Hemagglutinin HA1 chain {ECO:0000256|HAMAP-Rule:MF_04072}; DE Contains: DE RecName: Full=Hemagglutinin HA2 chain {ECO:0000256|HAMAP-Rule:MF_04072}; GN Name=HA {ECO:0000256|HAMAP-Rule:MF_04072, GN ECO:0000313|EMBL:ADZ53133.1}; OS Influenza A virus (A/Hong Kong/419305/2009(H1N1)). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus. OX NCBI_TaxID=997486 {ECO:0000313|EMBL:ADZ53133.1}; RN [1] {ECO:0000313|EMBL:ADZ53133.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Hong Kong/419305/2009 {ECO:0000313|EMBL:ADZ53133.1}; RA Wu W.L., Lau S.Y., Wang G., Chen Y., Song W., Wang P., Mok B.W.Y., Tai H., RA Wen X., Guan Y., Lin T., Yuen K.Y., Chen H.; RT "Mechanism for the emergence and prevalence of H1N1 influenza virus RT carrying H275Y oseltamivir resistance mutation."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Binds to sialic acid-containing receptors on the cell CC surface, bringing about the attachment of the virus particle to the CC cell. This attachment induces virion internalization either through CC clathrin-dependent endocytosis or through clathrin- and caveolin- CC independent pathway. Plays a major role in the determination of host CC range restriction and virulence. Class I viral fusion protein. CC Responsible for penetration of the virus into the cell cytoplasm by CC mediating the fusion of the membrane of the endocytosed virus particle CC with the endosomal membrane. Low pH in endosomes induces an CC irreversible conformational change in HA2, releasing the fusion CC hydrophobic peptide. Several trimers are required to form a competent CC fusion pore. {ECO:0000256|HAMAP-Rule:MF_04072}. CC -!- FUNCTION: Binds to sialic acid-containing receptors on the cell CC surface, bringing about the attachment of the virus particle to the CC cell. This attachment induces virion internalization of about two third CC of the virus particles through clathrin-dependent endocytosis and about CC one third through a clathrin- and caveolin-independent pathway. Plays a CC major role in the determination of host range restriction and CC virulence. Class I viral fusion protein. Responsible for penetration of CC the virus into the cell cytoplasm by mediating the fusion of the CC membrane of the endocytosed virus particle with the endosomal membrane. CC Low pH in endosomes induces an irreversible conformational change in CC HA2, releasing the fusion hydrophobic peptide. Several trimers are CC required to form a competent fusion pore. CC {ECO:0000256|RuleBase:RU003324}. CC -!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2. {ECO:0000256|HAMAP- CC Rule:MF_04072, ECO:0000256|RuleBase:RU003324}. CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000256|ARBA:ARBA00004247}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004247}. Cell membrane CC {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004251}. Host apical cell membrane CC {ECO:0000256|ARBA:ARBA00004310, ECO:0000256|HAMAP-Rule:MF_04072}; CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004310, CC ECO:0000256|HAMAP-Rule:MF_04072}. Membrane CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479}. Virion membrane {ECO:0000256|HAMAP- CC Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000256|HAMAP- CC Rule:MF_04072}. Note=Targeted to the apical plasma membrane in CC epithelial polarized cells through a signal present in the CC transmembrane domain. Associated with glycosphingolipid- and CC cholesterol-enriched detergent-resistant lipid rafts. CC {ECO:0000256|HAMAP-Rule:MF_04072}. CC -!- PTM: In natural infection, inactive HA is matured into HA1 and HA2 CC outside the cell by one or more trypsin-like, arginine-specific CC endoprotease secreted by the bronchial epithelial cells. One identified CC protease that may be involved in this process is secreted in lungs by CC Clara cells. {ECO:0000256|HAMAP-Rule:MF_04072}. CC -!- PTM: Palmitoylated. {ECO:0000256|HAMAP-Rule:MF_04072}. CC -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family. CC {ECO:0000256|ARBA:ARBA00006321, ECO:0000256|HAMAP-Rule:MF_04072, CC ECO:0000256|RuleBase:RU003324}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04072}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CY087296; ADZ53133.1; -; Viral_cRNA. DR SMR; F2NZC6; -. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046789; F:host cell surface receptor binding; IEA:UniProtKB-UniRule. DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-UniRule. DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule. DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro. DR GO; GO:0046761; P:viral budding from plasma membrane; IEA:UniProtKB-UniRule. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR Gene3D; 3.90.209.20; -; 1. DR HAMAP; MF_04072; INFV_HEMA; 1. DR InterPro; IPR008980; Capsid_hemagglutn. DR InterPro; IPR013828; Hemagglutn_HA1_a/b_dom_sf. DR InterPro; IPR000149; Hemagglutn_influenz_A. DR InterPro; IPR001364; Hemagglutn_influenz_A/B. DR Pfam; PF00509; Hemagglutinin; 1. DR PRINTS; PR00330; HEMAGGLUTN1. DR PRINTS; PR00329; HEMAGGLUTN12. DR SUPFAM; SSF49818; SSF49818; 1. PE 3: Inferred from homology; KW Clathrin- and caveolin-independent endocytosis of virus by host KW {ECO:0000256|ARBA:ARBA00023261, ECO:0000256|HAMAP-Rule:MF_04072}; KW Clathrin-mediated endocytosis of virus by host KW {ECO:0000256|ARBA:ARBA00022570, ECO:0000256|HAMAP-Rule:MF_04072}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP- KW Rule:MF_04072}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|ARBA:ARBA00022510, ECO:0000256|HAMAP-Rule:MF_04072}; KW Fusion of virus membrane with host membrane {ECO:0000256|ARBA:ARBA00022506, KW ECO:0000256|HAMAP-Rule:MF_04072}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|HAMAP- KW Rule:MF_04072}; KW Hemagglutinin {ECO:0000256|ARBA:ARBA00022546, ECO:0000256|HAMAP- KW Rule:MF_04072}; KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511, ECO:0000256|HAMAP- KW Rule:MF_04072}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870, ECO:0000256|HAMAP- KW Rule:MF_04072}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, ECO:0000256|HAMAP- KW Rule:MF_04072}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP- KW Rule:MF_04072}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_04072}; KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_04072}; KW Signal {ECO:0000256|HAMAP-Rule:MF_04072}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_04072}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04072}; KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804, KW ECO:0000256|HAMAP-Rule:MF_04072}; KW Viral envelope protein {ECO:0000256|ARBA:ARBA00022879, ECO:0000256|HAMAP- KW Rule:MF_04072}; KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595, KW ECO:0000256|HAMAP-Rule:MF_04072}; KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04072}; KW Virus endocytosis by host {ECO:0000256|ARBA:ARBA00022890, KW ECO:0000256|HAMAP-Rule:MF_04072}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296, KW ECO:0000256|HAMAP-Rule:MF_04072}. FT CHAIN 345..566 FT /note="Hemagglutinin HA2 chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT /id="PRO_5023283338" FT TRANSMEM 531..554 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT SITE 344..345 FT /note="Cleavage; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT LIPID 555 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT LIPID 562 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT LIPID 565 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT DISULFID 72..84 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT DISULFID 296..320 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT DISULFID 488..492 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" SQ 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 //