ID A0A023IVI1_9INFA Unreviewed; 565 AA. AC A0A023IVI1; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 12-AUG-2020, entry version 38. 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:AHA98414.1}; OS Influenza A virus (A/ruddy turnstone/Ilha de Canelas/A08/2008(H11N9)). OC Viruses; Riboviria; Negarnaviricota; Polyploviricotina; Insthoviricetes; OC Articulavirales; Orthomyxoviridae; Alphainfluenzavirus. OX NCBI_TaxID=1419066 {ECO:0000313|EMBL:AHA98414.1, ECO:0000313|Proteomes:UP000145460}; RN [1] {ECO:0000313|EMBL:AHA98414.1, ECO:0000313|Proteomes:UP000145460} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A/ruddy turnstone/Ilha de Canelas/A08/2008 RC {ECO:0000313|EMBL:AHA98414.1}; RX PubMed=25329399; RA de Araujo J., de Azevedo Junior S.M., Gaidet N., Hurtado R.F., Walker D., RA Thomazelli L.M., Ometto T., Seixas M.M., Rodrigues R., Galindo D.B., RA da Silva A.C., Rodrigues A.M., Bomfim L.L., Mota M.A., Larrazabal M.E., RA Branco J.O., Serafini P., Neto I.S., Franks J., Webby R.J., Webster R.G., RA Durigon E.L.; RT "Avian Influenza Virus (H11N9) in Migratory Shorebirds Wintering in the RT Amazon Region, Brazil."; RL PLoS ONE 9:E110141-E110141(2014). RN [2] {ECO:0000313|Proteomes:UP000145460} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=26689791; RA Hurtado R., Fabrizio T., Vanstreels R.E., Krauss S., Webby R.J., RA Webster R.G., Durigon E.L.; RT "Molecular Characterization of Subtype H11N9 Avian Influenza Virus Isolated RT from Shorebirds in Brazil."; RL PLoS ONE 10:E0145627-E0145627(2015). 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; KF824501; AHA98414.1; -; Viral_cRNA. DR Proteomes; UP000145460; Genome. 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 Coiled coil {ECO:0000256|SAM:Coils}; 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, ECO:0000256|RuleBase:RU003324}; 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, ECO:0000256|RuleBase:RU003324}; 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 17..342 FT /note="Hemagglutinin HA1 chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT /id="PRO_5023452587" FT TRANSMEM 530..553 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT COILED 398..425 FT /evidence="ECO:0000256|SAM:Coils" FT SITE 342..343 FT /note="Cleavage; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT LIPID 554 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT LIPID 561 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT LIPID 564 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT DISULFID 20..479 FT /note="Interchain (between HA1 and HA2 chains)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT DISULFID 58..290 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT DISULFID 71..83 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT DISULFID 106..151 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT DISULFID 294..318 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT DISULFID 486..490 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" SQ SEQUENCE 565 AA; 62895 MW; 2401B714AD6B0717 CRC64; MKKIMLLAAI IICIQADEIC IGYLSNNSTE KVDTIIESNV TVTSSVELVE NEHTGSFCSI NGKAPISLGD CSFAGWILGN PRCDDLIGKT SWSYIVEKPN PTNGICYPGT LENEEELRLK FSGVLEFSKF EAFTSNGWGA VNSGAGVTAA CKYGSSSSFF RHMVWLIHQS GTYPVIQRTF NNTKGRDVLM VWGVHHPASL KEHQDLYKKD SSYVAVGSES YNRRFTPEIS TRPRVNGQAG RMTFYWTIVK PGEAITFESN GAFLAPRYAF ELVSLGNGKL FRSDLSIGSC STKCQSEIGG INTNRSFHNV HRNTIGDCPK YVNVKSLKLA TGLRNVPTIA TRGLFGAIAG FIEGGWPGLI NGWYGFQHRN EEGTGIAADK ESTQKAIDQI TSKVNNIVDR MNTNFESVQH EFSEIEERIN QLSQHVDDSI IDIWSYNAQL LVLLENEKTL DLHDSNVRNL HEKVRRMLQD NAKDEGNGCF TFYHKCDNEC IEKVRNGTYD HKEFEEESKL NRQEIEGVKL DSNGNVYKIL SIYSCIASSL VLAAIIMGFI LWACSNGSCR CTICI //