ID D1LN57_9INFA Unreviewed; 568 AA. AC D1LN57; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 16-JAN-2019, entry version 55. 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:ACZ48514.1}; OS Influenza A virus (A/Hong Kong/485/1997(H5N1)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Alphainfluenzavirus. OX NCBI_TaxID=680692 {ECO:0000313|EMBL:ACZ48514.1, ECO:0000313|Proteomes:UP000120622}; RN [1] {ECO:0000313|EMBL:ACZ48514.1, ECO:0000313|Proteomes:UP000120622} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 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:SAAS01039073}. 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|RuleBase:RU003324, CC 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|RuleBase:RU003324, CC 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; GU052142; ACZ48514.1; -; Viral_cRNA. DR Proteomes; UP000120622; Genome. 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 Complete proteome {ECO:0000313|Proteomes:UP000120622}; 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|RuleBase:RU003324, 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|RuleBase:RU003324, 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 533 555 Helical. {ECO:0000256|HAMAP-Rule: FT MF_04072}. FT COILED 402 436 {ECO:0000256|SAM:Coils}. FT SITE 346 347 Cleavage; by host. {ECO:0000256|HAMAP- FT Rule:MF_04072}. FT LIPID 557 557 S-palmitoyl cysteine; by host. FT {ECO:0000256|HAMAP-Rule:MF_04072}. FT LIPID 564 564 S-palmitoyl cysteine; by host. FT {ECO:0000256|HAMAP-Rule:MF_04072}. FT LIPID 567 567 S-palmitoyl cysteine; by host. FT {ECO:0000256|HAMAP-Rule:MF_04072}. FT DISULFID 58 290 {ECO:0000256|HAMAP-Rule:MF_04072}. FT DISULFID 71 83 {ECO:0000256|HAMAP-Rule:MF_04072}. FT DISULFID 106 151 {ECO:0000256|HAMAP-Rule:MF_04072}. FT DISULFID 294 318 {ECO:0000256|HAMAP-Rule:MF_04072}. FT DISULFID 490 494 {ECO:0000256|HAMAP-Rule:MF_04072}. 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 //