ID Q1WDL8_9INFA Unreviewed; 567 AA. AC Q1WDL8; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 07-APR-2021, entry version 88. 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:ABD28182.1}; OS Influenza A virus (A/Guangxi/1/2005(H5N1)). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus. OX NCBI_TaxID=370812 {ECO:0000313|EMBL:ABD28182.1, ECO:0000313|Proteomes:UP000105802}; RN [1] {ECO:0000313|Proteomes:UP000105802} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20834097; DOI=10.3851/IMP1656; RA Lan Y., Zhang Y., Dong L., Wang D., Huang W., Xin L., Yang L., Zhao X., RA Li Z., Wang W., Li X., Xu C., Yang L., Guo J., Wang M., Peng Y., Gao Y., RA Guo Y., Wen L., Jiang T., Shu Y.; RT "A comprehensive surveillance of adamantane resistance among human RT influenza A virus isolated from mainland China between 1956 and 2009."; RL Antivir. Ther. 15:853-859(2010). RN [2] {ECO:0000313|Proteomes:UP000105802} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21976646; DOI=10.1128/JVI.05266-11; RA Wan X.F., Dong L., Lan Y., Long L.P., Xu C., Zou S., Li Z., Wen L., Cai Z., RA Wang W., Li X., Yuan F., Sui H., Zhang Y., Dong J., Sun S., Gao Y., RA Wang M., Bai T., Yang L., Li D., Yang W., Yu H., Wang S., Feng Z., Wang Y., RA Guo Y., Webby R.J., Shu Y.; RT "Indications that Live Poultry Markets Are a Major Source of Human H5N1 RT Influenza Virus Infection in China."; RL J. Virol. 85:13432-13438(2011). 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; DQ371930; ABD28182.1; -; Genomic_RNA. DR Proteomes; UP000105802; Genome. 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 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}; 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 346..567 FT /note="Hemagglutinin HA2 chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT /id="PRO_5023248827" FT TRANSMEM 532..554 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT COILED 401..435 FT /evidence="ECO:0000256|SAM:Coils" FT SITE 345..346 FT /note="Cleavage; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT LIPID 556 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT LIPID 563 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT LIPID 566 FT /note="S-palmitoyl cysteine; by host" 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 489..493 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" SQ SEQUENCE 567 AA; 64058 MW; DF9D13166F723572 CRC64; MEKIVLLLAI VSLVKSDQIC IGYHANNSTE QVDTIMEKNV TVTHAQDILE KTHNGKLCDL DGVKPLILRD CSVAGWLLGN PMCDEFINVP EWSYIVEKAN PANDLCYPGN FNDYEELKHL LSRINHFEKI QIIPKSSWSD HEASSGGSSA CPYQGTPSFF RNVVWLIKKN NTYPTIKRSY NNTNQEDLLI LWGIHHSNDA AEQTKLYQNP TTYISVGTST LNQRLVPKIA TRSKVNGQSG RMDFFWTILK PNDAINFESN GNFIAPEYAY KIVKKGDSAI MKSEVEYGNC NTKCQTPIGA INSSMPFHNI HPLTIGECPK YVKSNKLVLA TGLRNSPLRE RRRKRGLFGA IAGFIEGGWQ GMVDGWYGYH HSNEQGSGYA ADKESTQKAI DGVTNKVNSI IDKMNTQFEA VGREFNNLER RIENLNKKME DGFLDVWTYN AELLVLMENE RTLDFHDSNV KNLYDKVRLQ LRDNAKELGN GCFEFYHKCD NECMESVRNG TYDYPQYSEE ARLKREEISG VKLESIGTYQ ILSIYSTVAS SLALAIMVAG LSLWMCSNGS LQCRICI //