ID A8CDU0_9INFA Unreviewed; 104 AA. AC A8CDU0; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 2. DT 08-NOV-2023, entry version 89. DE RecName: Full=Hemagglutinin {ECO:0000256|ARBA:ARBA00022203}; DE Flags: Fragment; OS Influenza A virus (A/mallard/Sweden/S90391/2005(H3N8)). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus; OC Alphainfluenzavirus influenzae; Influenza A virus. OX NCBI_TaxID=527221 {ECO:0000313|EMBL:ABV58843.2}; RN [1] {ECO:0007829|PDB:2IPK} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 59-71. RX PubMed=17351628; DOI=10.1038/nchembio868; RA Venkatraman P., Nguyen T.T., Sainlos M., Bilsel O., Chitta S., RA Imperiali B., Stern L.J.; RT "Fluorogenic probes for monitoring peptide binding to class II MHC proteins RT in living cells."; RL Nat. Chem. Biol. 3:222-228(2007). RN [2] {ECO:0000313|EMBL:ABV58843.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/mallard/Sweden/S90391/05 {ECO:0000313|EMBL:ABV58843.2}; RX PubMed=19026689; DOI=10.1016/j.jviromet.2008.10.019; RA Yacoub A., Kiss I., Zohari S., Hakhverdyan M., Czifra G., Mohamed N., RA Gyarmati P., Blomberg J., Belak S.; RT "The rapid molecular subtyping and pathotyping of avian influenza RT viruses."; RL J. Virol. Methods 156:157-161(2009). 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. CC {ECO:0000256|RuleBase:RU003324}. CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000256|ARBA:ARBA00004247}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004247}. Cell membrane CC {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004251}. Host apical cell membrane CC {ECO:0000256|ARBA:ARBA00004310}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004310}. Membrane CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479}. CC -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family. CC {ECO:0000256|ARBA:ARBA00006321, 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; EU057721; ABV58843.2; -; Viral_cRNA. DR PDB; 2IPK; X-ray; 2.30 A; C=59-71. DR PDBsum; 2IPK; -. DR SMR; A8CDU0; -. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW. DR GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro. DR GO; GO:0075512; P:clathrin-dependent 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; 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_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; SSF58064; Influenza hemagglutinin (stalk); 1. DR SUPFAM; SSF49818; Viral protein domain; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:2IPK}; KW Clathrin- and caveolin-independent endocytosis of virus by host KW {ECO:0000256|ARBA:ARBA00023261}; KW Clathrin-mediated endocytosis of virus by host KW {ECO:0000256|ARBA:ARBA00022570}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|ARBA:ARBA00022510}; KW Fusion of virus membrane with host membrane KW {ECO:0000256|ARBA:ARBA00022506}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Hemagglutinin {ECO:0000256|ARBA:ARBA00022546, KW ECO:0000256|RuleBase:RU003324}; KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Palmitate {ECO:0000256|ARBA:ARBA00023139}; KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804}; KW Viral envelope protein {ECO:0000256|ARBA:ARBA00022879, KW ECO:0000256|RuleBase:RU003324}; KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595}; KW Virion {ECO:0000256|ARBA:ARBA00022844}; KW Virus endocytosis by host {ECO:0000256|ARBA:ARBA00022890}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}. FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ABV58843.2" FT NON_TER 104 FT /evidence="ECO:0000313|EMBL:ABV58843.2" SQ SEQUENCE 104 AA; 11510 MW; D45DF6D778AB1219 CRC64; NGNFIAPRGY FKMRTGKSSI MRSDAPIDTC ISECITPNGS IPNDKPFQNV NKITYGACPK YVKQNTLKLA TGMRNVPEKQ TRGLFGAIAG FIENGWEGMI DGWY //