ID C0JRM0_9INFA Unreviewed; 560 AA. AC C0JRM0; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 11-DEC-2019, entry version 64. 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:ACJ35235.1}; OS Influenza A virus (A/chicken/Anhui/AH16/2008(H9N2)). OC Viruses; Riboviria; Negarnaviricota; Polyploviricotina; Insthoviricetes; OC Articulavirales; Orthomyxoviridae; Alphainfluenzavirus. OX NCBI_TaxID=572976 {ECO:0000313|EMBL:ACJ35235.1}; RN [1] {ECO:0000313|EMBL:ACJ35235.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/chicken/Anhui/AH16/2008 {ECO:0000313|EMBL:ACJ35235.1}; RX PubMed=19781574; DOI=10.1016/j.jviromet.2009.09.013; RA Ji K., Jiang W.M., Liu S., Chen J.M., Chen J., Hou G.Y., Li J.P., RA Huang B.X.; RT "Characterization of the hemagglutinin gene of subtype H9 avian influenza RT viruses isolated in 2007-2009 in China."; RL J. Virol. Methods 163:186-189(2010). 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 ECO:0000256|SAAS:SAAS01039073}. 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 ECO:0000256|SAAS:SAAS00047800}. CC -!- SUBCELLULAR LOCATION: Host apical cell membrane {ECO:0000256|HAMAP- CC Rule:MF_04072, ECO:0000256|SAAS:SAAS00554492}; Single-pass type I CC membrane protein {ECO:0000256|HAMAP-Rule:MF_04072, CC ECO:0000256|SAAS:SAAS00554492}. 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|HAMAP-Rule:MF_04072, ECO:0000256|RuleBase:RU003324, CC ECO:0000256|SAAS:SAAS00963381}. 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; FJ434579; ACJ35235.1; -; Viral_cRNA. 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:SAAS01039036}; KW Clathrin-mediated endocytosis of virus by host {ECO:0000256|HAMAP- KW Rule:MF_04072, ECO:0000256|SAAS:SAAS01038958}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS01198254}; KW Fusion of virus membrane with host endosomal membrane {ECO:0000256|HAMAP- KW 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|RuleBase:RU003324, ECO:0000256|SAAS:SAAS01198242}; KW Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS01198249}; KW Host membrane {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS01198252}; 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, ECO:0000256|SAAS:SAAS01198250}; 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:SAAS01198248}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS01198253}; 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|RuleBase:RU003324, ECO:0000256|SAAS:SAAS01198245}; KW Viral penetration into host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04072, KW ECO:0000256|SAAS:SAAS00963370}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|SAAS:SAAS01198246}; 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 CHAIN 339..560 FT /note="Hemagglutinin HA2 chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT /id="PRO_5023578166" FT TRANSMEM 525..549 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT COILED 394..428 FT /evidence="ECO:0000256|SAM:Coils" FT SITE 338..339 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 559 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT DISULFID 73..85 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT DISULFID 290..314 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" FT DISULFID 482..486 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072" SQ SEQUENCE 560 AA; 62675 MW; 76B576BF9412B81B CRC64; METVSLITML LVVTVINADK ICIGYQSTNS TETVDTLTEN NVPVTHAKEL LHTEHNGMLC ATNLGHPLIL DTCTIEGLIY GNPSCDLLLG GGEWSYIVER PSAVNGLCYP GNVENLEELR SLFSSASSYQ RIQIFPDTIW NVSYSGTSKA CSDSFYRSMR WLTQKNNAYP IQDAQYTNNR EKNILFMWGI NQPPTETAQT NLYTRTDTTT SVATEEINRT FKPLIGPRPL VNGLQGRIDY YWSVLKPGQT LRIRSNGNLI APWYGHILSG ESHGRILKTD LKRGSCTVQC QTEKGGLNTT LPFQNVSKYA FGNCSKYVGI KSLKLAVGLR NVPSRSSRGL FGAIAGFIEG GWSGLVAGWY GFQHSNDQGV GMAADRDSTQ KAIDKITSKV NNIVDKMNKQ YEIIDHEFSE VENRLNMINN KIDDQIQDIW AYNAELLVLL ENQKTLDEHD ANVNNLYNKV KRALGSNAVE DGKGCFELYH KCDDQCMETI RNGTYNRRKY QEESKLKRQR IEGVKLESEG TYKILTIYST VASSLVIAMG FAAFLFWAMS NGSCRCNICI //