ID F2NZC6_9INFA Unreviewed; 566 AA. AC F2NZC6; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 21-SEP-2011, entry version 4. DE SubName: Full=Hemagglutinin; DE Flags: Precursor; GN Name=HA; OS Influenza A virus (A/Hong Kong/419305/2009(H1N1)). OC Viruses; ssRNA negative-strand viruses; Orthomyxoviridae; OC Influenzavirus A. OX NCBI_TaxID=997486; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Hong Kong/419305/2009; RA Wu W.L., Lau S.Y., Wang G., Chen Y., Song W., Wang P., Mok B.W.Y., RA Tai H., 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 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 -!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2 (By similarity). CC -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family. 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 GO; GO:0019031; C:viral envelope; IEA:InterPro. DR GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro. DR GO; GO:0019064; P:viral envelope fusion with host membrane; IEA:InterPro. 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 Gene3D; G3DSA:3.90.209.20; Haemagglutn_HA1_a/b; 1. DR Gene3D; G3DSA:2.10.77.10; Haemagglutn_HA1_b-ribbon; 1. DR Gene3D; G3DSA:3.90.20.10; Haemagglutn_stalk; 1. DR Pfam; PF00509; Hemagglutinin; 1. DR PRINTS; PR00330; HEMAGGLUTN1. DR PRINTS; PR00329; HEMAGGLUTN12. DR SUPFAM; SSF49818; Capsid_hemag; 1. PE 3: Inferred from homology; KW Clathrin- and caveolin-independent endocytosis of virus by host; KW Hemagglutinin; Host cell membrane; Host membrane; KW Host-virus interaction; Membrane; Signal; Transmembrane; KW Transmembrane helix; Viral envelope protein; Virion; KW Virus endocytosis by host. FT SIGNAL 1 17 Potential. FT CHAIN 18 566 Potential. FT /FTId=PRO_5000731538. FT CHAIN 18 344 HA1. FT /FTId=PRO_5000731539. FT CHAIN 345 566 HA2. FT /FTId=PRO_5000731540. 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 //