ID F2NZC6_9INFA Unreviewed; 566 AA. AC F2NZC6; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 28-FEB-2018, entry version 43. DE RecName: Full=Hemagglutinin {ECO:0000256|HAMAP-Rule:MF_04072}; DE Contains: DE RecName: Full=Hemagglutinin HA2 chain {ECO:0000256|HAMAP-Rule:MF_04072}; DE Contains: DE RecName: Full=Hemagglutinin HA1 chain {ECO:0000256|HAMAP-Rule:MF_04072}; GN Name=HA {ECO:0000256|HAMAP-Rule:MF_04072, GN ECO:0000313|EMBL:ADZ53133.1}; OS Influenza A virus (A/Hong Kong/419305/2009(H1N1)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=997486 {ECO:0000313|EMBL:ADZ53133.1}; RN [1] {ECO:0000313|EMBL:ADZ53133.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Hong Kong/419305/2009 {ECO:0000313|EMBL:ADZ53133.1}; 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 either CC through clathrin-dependent endocytosis or through clathrin- and CC caveolin-independent pathway. Plays a major role in the CC determination of host range restriction and virulence. Class I CC viral fusion protein. Responsible for penetration of the virus CC into the cell cytoplasm by mediating the fusion of the membrane of CC the endocytosed virus particle with the endosomal membrane. Low pH CC in 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. {ECO:0000256|HAMAP- CC Rule:MF_04072, ECO:0000256|SAAS:SAAS00842802}. 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 -!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2. CC {ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|SAAS:SAAS00070616}. CC -!- SUBCELLULAR LOCATION: Host apical cell membrane CC {ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|SAAS:SAAS00554492}; CC Single-pass type I membrane protein {ECO:0000256|HAMAP- CC Rule:MF_04072, ECO:0000256|SAAS:SAAS00554492}. Virion membrane CC {ECO:0000256|HAMAP-Rule:MF_04072}; Single-pass type I membrane CC protein {ECO:0000256|HAMAP-Rule:MF_04072}. Note=Targeted to the CC apical plasma membrane in epithelial polarized cells through a CC signal present in the transmembrane domain. Associated with CC glycosphingolipid- and cholesterol-enriched detergent-resistant CC lipid rafts. {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 CC identified protease that may be involved in this process is CC secreted in lungs by Clara cells. {ECO:0000256|HAMAP- CC Rule:MF_04072}. CC -!- PTM: Palmitoylated. {ECO:0000256|HAMAP-Rule:MF_04072}. CC -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family. CC {ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|SAAS:SAAS00963381}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of 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; CY087296; ADZ53133.1; -; Viral_cRNA. DR SMR; F2NZC6; -. 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|HAMAP-Rule:MF_04072, ECO:0000256|SAAS:SAAS00452788}; KW Clathrin-mediated endocytosis of virus by host {ECO:0000256|HAMAP- KW Rule:MF_04072, ECO:0000256|SAAS:SAAS00453157}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS00963411}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|SAAS:SAAS00963419}; KW Fusion of virus membrane with host membrane {ECO:0000256|HAMAP- KW Rule:MF_04072, ECO:0000256|SAAS:SAAS00963379}; KW Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04072}; KW Hemagglutinin {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS00963391}; KW Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS00963415}; KW Host membrane {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS00963389}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS00963361}; KW Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04072}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS00963418}; KW Palmitate {ECO:0000256|HAMAP-Rule:MF_04072}; KW Signal {ECO:0000256|HAMAP-Rule:MF_04072}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS00963395}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS00963387}; KW Viral attachment to host cell {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS00963390}; KW Viral envelope protein {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS00963382}; KW Viral penetration into host cytoplasm {ECO:0000256|HAMAP- KW Rule:MF_04072, ECO:0000256|SAAS:SAAS00963370}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS00070858}; KW Virus endocytosis by host {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS00963339}; KW Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS00963443}. FT TRANSMEM 531 554 Helical. {ECO:0000256|HAMAP-Rule: FT MF_04072}. FT COILED 382 402 {ECO:0000256|SAM:Coils}. FT SITE 344 345 Cleavage; by host. {ECO:0000256|HAMAP- FT Rule:MF_04072}. FT LIPID 555 555 S-palmitoyl cysteine; by host. FT {ECO:0000256|HAMAP-Rule:MF_04072}. FT LIPID 562 562 S-palmitoyl cysteine; by host. FT {ECO:0000256|HAMAP-Rule:MF_04072}. FT LIPID 565 565 S-palmitoyl cysteine; by host. FT {ECO:0000256|HAMAP-Rule:MF_04072}. FT DISULFID 72 84 {ECO:0000256|HAMAP-Rule:MF_04072}. FT DISULFID 296 320 {ECO:0000256|HAMAP-Rule:MF_04072}. FT DISULFID 488 492 {ECO:0000256|HAMAP-Rule:MF_04072}. 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 //