ID Q1WDL8_9INFA Unreviewed; 567 AA. AC Q1WDL8; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 14-OCT-2015, entry version 61. DE RecName: Full=Hemagglutinin {ECO:0000256|SAAS:SAAS00046876}; GN Name=HA {ECO:0000313|EMBL:ABD28182.1}; OS Influenza A virus (A/Guangxi/1/2005(H5N1)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=370812 {ECO:0000313|EMBL:ABD28182.1}; RN [1] {ECO:0000313|EMBL:ABD28182.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Guangxi/1/2005 {ECO:0000313|EMBL:ABD28182.1}; RA Shu Y., Yu H., Li D.; RT "Lethal Avian Influenza (H5N1) Infection in a Pregnant Woman, Anhui RT Province, China."; RL Submitted (JAN-2006) 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 CC the cell. This attachment induces virion internalization of about CC two third of the virus particles through clathrin-dependent CC endocytosis and about one third through a clathrin- and caveolin- CC independent pathway. Plays a major role in the determination of CC host range restriction and virulence. Class I viral fusion CC protein. Responsible for penetration of the virus into the cell CC cytoplasm by mediating the fusion of the membrane of the CC endocytosed virus particle with the endosomal membrane. Low pH in CC endosomes induces an irreversible conformational change in HA2, CC releasing the fusion hydrophobic peptide. Several trimers are CC required to form a competent fusion pore. CC {ECO:0000256|RuleBase:RU003324}. CC -!- FUNCTION: Binds to sialic acid-containing receptors on the cell CC surface, bringing about the attachment of the virus particle to CC the cell. This attachment induces virion internalization of about CC two third of the virus particles through clathrin-dependent CC endocytosis and about one third through a clathrin- and caveolin- CC independent pathway. Plays a major role in the determination of CC host range restriction and virulence. Class I viral fusion CC protein. Responsible for penetration of the virus into the cell CC cytoplasm by mediating the fusion of the membrane of the CC endocytosed virus particle with the endosomal membrane. Low pH in CC endosomes induces an irreversible conformational change in HA2, CC releasing the fusion hydrophobic peptide. Several trimers are CC required to form a competent fusion pore (By similarity). CC {ECO:0000256|SAAS:SAAS00204388}. CC -!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2. CC {ECO:0000256|RuleBase:RU003324, ECO:0000256|SAAS:SAAS00046877}. CC -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family. CC {ECO:0000256|RuleBase:RU003324}. 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 GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW. DR GO; GO:0075512; P:clathrin-mediated endocytosis of virus by host cell; IEA:UniProtKB-KW. DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW. DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR Gene3D; 2.10.77.10; -; 1. DR Gene3D; 3.90.20.10; -; 1. DR Gene3D; 3.90.209.20; -; 1. DR InterPro; IPR008980; Capsid_hemagglutn. DR InterPro; IPR013828; Hemagglutn_HA1_a/b_dom. DR InterPro; IPR013827; Hemagglutn_HA1_b-rbn_dom. DR InterPro; IPR000149; Hemagglutn_influenz_A. DR InterPro; IPR001364; Hemagglutn_influenz_A/B. DR InterPro; IPR013829; Hemagglutn_stalk. 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|SAAS:SAAS00046919}; KW Clathrin-mediated endocytosis of virus by host KW {ECO:0000256|SAAS:SAAS00046886}; Coiled coil {ECO:0000256|SAM:Coils}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00276375}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|SAAS:SAAS00070798}; KW Fusion of virus membrane with host membrane KW {ECO:0000256|SAAS:SAAS00070828}; KW Hemagglutinin {ECO:0000256|RuleBase:RU003324, KW ECO:0000256|SAAS:SAAS00276224}; KW Host cell membrane {ECO:0000256|SAAS:SAAS00276325}; KW Host membrane {ECO:0000256|SAAS:SAAS00276242}; KW Host-virus interaction {ECO:0000256|SAAS:SAAS00070855}; KW Membrane {ECO:0000256|SAAS:SAAS00276163, ECO:0000256|SAM:Phobius}; KW Transmembrane {ECO:0000256|SAAS:SAAS00276177, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00276322, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|SAAS:SAAS00070808}; KW Viral envelope protein {ECO:0000256|RuleBase:RU003324, KW ECO:0000256|SAAS:SAAS00276363}; KW Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS00070831}; KW Virion {ECO:0000256|SAAS:SAAS00070858}; KW Virus endocytosis by host {ECO:0000256|SAAS:SAAS00046951}; KW Virus entry into host cell {ECO:0000256|SAAS:SAAS00070771}. FT TRANSMEM 532 554 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 401 435 {ECO:0000256|SAM:Coils}. 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 //