ID D1LN57_9INFA Unreviewed; 568 AA. AC D1LN57; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 14-OCT-2015, entry version 34. DE RecName: Full=Hemagglutinin {ECO:0000256|SAAS:SAAS00046876}; GN Name=HA {ECO:0000313|EMBL:ACZ48514.1}; OS Influenza A virus (A/Hong Kong/485/1997(H5N1)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=680692 {ECO:0000313|EMBL:ACZ48514.1}; RN [1] {ECO:0000313|EMBL:ACZ48514.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Hong Kong/485/1997 {ECO:0000313|EMBL:ACZ48514.1}; RA Kim L.M., Scott M.A., Suarez D.L., Spackman E., Swayne D.E., RA Afonso C.L.; RT "USDA Agriculture Research Service Avian Influenza Virus Sequencing RT Project."; RL Submitted (OCT-2009) 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; GU052142; ACZ48514.1; -; Viral_cRNA. 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 533 555 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 402 436 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 568 AA; 64333 MW; 18DA3277E61EA162 CRC64; MEKIVLLLAT VSLVKSDQIC IGYHANNSTE QVDTIMEKNV TVTHAQDILE RTHNGKLCDL NGVKPLILRD CSVAGWLLGN PMCDEFINVP EWSYIVEKAS PANDLCYPGN FNDYEELKHL LSRINHFEKI QIIPKSSWSN HDASSGVSSA CPYLGRSSFF RNVVWLIKKN SSYPTIKRSY NNTNQEDLLV LWGIHHPNDA AEQTRLYQNP TTYISVGTST LNQRLVPEIA TRPKVNGQSG RMEFFWTILK PNDAINFESN GNFIAPEYAY KIVKKGDSTI MKSELEYGNC NTKCQTPMGA INSSMPFHNI HPLTIGECPK YVKSNRLVLA TGLRNTPQRE RRRKKRGLFG AIAGFIEGGW QGMVDGWYGY HHSNEQGSGY AADQESTQKA IDGVTNKVNS IINKMNTQFE AVGREFNNLE RRIENLNKKM EDGFLDVWTY NAELLVLMEN ERTLDFHDSN VKNLYDKVRL QLRDNAKELG NGCFEFYHKC DNECMESVKN GTYDYPQYSE EARLNREEIS GVKLESMGTY QILSIYSTVA SSLALAIMVA GLSLWMCSNG SLQCRICI //