ID A0FFQ6_9INFA Unreviewed; 556 AA. AC A0FFQ6; DT 28-NOV-2006, integrated into UniProtKB/TrEMBL. DT 28-NOV-2006, sequence version 1. DT 09-DEC-2015, entry version 62. DE RecName: Full=Hemagglutinin {ECO:0000256|SAAS:SAAS00363365}; DE Flags: Fragment; GN Name=HA {ECO:0000313|EMBL:ABJ96698.1}; OS Influenza A virus (A/goose/Guiyang/337/2006(H5N1)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=407713 {ECO:0000313|EMBL:ABJ96698.1}; RN [1] {ECO:0000213|PDB:4JUM} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 17-339 AND 347-522, RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-181 AND ASN-302. RA DuBois R.M., Zaraket H., Reddivari M., Coop T., Heath R.J., RA White S.W., Russell C.J.; RT "To be published."; RL Submitted (MAR-2013) to the PDB data bank. 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 -!- 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 {ECO:0000256|SAAS:SAAS00363200}. CC -!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2. CC {ECO:0000256|RuleBase:RU003324, ECO:0000256|SAAS:SAAS00363128}. CC -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family. CC {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; DQ992765; ABJ96698.1; -; Viral_cRNA. DR PDB; 4JUM; X-ray; 2.00 A; A=17-339, B=347-522. DR PDBsum; 4JUM; -. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW. DR GO; GO:0075512; P:clathrin-mediated 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; 2.10.77.10; -; 1. 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. 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 Pfam; PF00509; Hemagglutinin; 1. DR PRINTS; PR00330; HEMAGGLUTN1. DR PRINTS; PR00329; HEMAGGLUTN12. DR SUPFAM; SSF49818; SSF49818; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4JUM}; KW Clathrin- and caveolin-independent endocytosis of virus by host KW {ECO:0000256|SAAS:SAAS00046919}; KW Clathrin-mediated endocytosis of virus by host KW {ECO:0000256|SAAS:SAAS00046886}; Coiled coil {ECO:0000256|SAM:Coils}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00228526}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|SAAS:SAAS00070798}; KW Fusion of virus membrane with host membrane KW {ECO:0000256|SAAS:SAAS00070828}; KW Hemagglutinin {ECO:0000256|RuleBase:RU003324, KW ECO:0000256|SAAS:SAAS00228908}; KW Host cell membrane {ECO:0000256|SAAS:SAAS00228620}; KW Host membrane {ECO:0000256|SAAS:SAAS00228760}; KW Host-virus interaction {ECO:0000256|SAAS:SAAS00070855}; KW Membrane {ECO:0000256|SAAS:SAAS00228566, ECO:0000256|SAM:Phobius}; KW Transmembrane {ECO:0000256|SAAS:SAAS00228433, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00228386, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|SAAS:SAAS00070808}; KW Viral envelope protein {ECO:0000256|RuleBase:RU003324, KW ECO:0000256|SAAS:SAAS00228641}; KW Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS00070831}; KW Virion {ECO:0000256|SAAS:SAAS00070858}; KW Virus endocytosis by host {ECO:0000256|SAAS:SAAS00046951}; KW Virus entry into host cell {ECO:0000256|SAAS:SAAS00070771}. FT TRANSMEM 533 555 Helical. {ECO:0000256|SAM:Phobius}. FT COILED 402 429 {ECO:0000256|SAM:Coils}. FT CARBOHYD 181 181 N-linked (GlcNAc...). {ECO:0000213|PDB: FT 4JUM}. FT /FTId=CAR_5005389383. FT CARBOHYD 302 302 N-linked (GlcNAc...). {ECO:0000213|PDB: FT 4JUM}. FT /FTId=CAR_5005389384. FT DISULFID 20 483 Interchain (with C-483 in A0FFQ6). FT {ECO:0000213|PDB:4JUM}. FT DISULFID 58 290 {ECO:0000213|PDB:4JUM}. FT DISULFID 71 83 {ECO:0000213|PDB:4JUM}. FT DISULFID 106 151 {ECO:0000213|PDB:4JUM}. FT DISULFID 294 318 {ECO:0000213|PDB:4JUM}. FT DISULFID 490 494 {ECO:0000213|PDB:4JUM}. FT NON_TER 556 556 {ECO:0000313|EMBL:ABJ96698.1}. SQ SEQUENCE 556 AA; 62980 MW; 0974A8F404E126E4 CRC64; MEKIVLLLAI ISLVKSDQIC IGYHANNSTV QVDTIMEKNV TVTHAQDILE KTHNGKLCSL DGVKPLILRD CSVAGWLLGN PMCDEFINVP EWSYIVEKAS PANDLCYPGD FNDYEELKHL LSRINHFEKI QIIPKSSWPN HEASLGVSSA CPYLGESSFF RNVVWLIKKN SSYPTIKRSY NNTNQEDLLV LWGIHHPNDA AEQIKLYQNP NTYISVGTST LNQRLVPTIA TRSKVNGQSG RMEFFWTILK PNDAINFESN GNFIAPEYAY KIVKKGDSAI MKSELEYGNC NTKCQTPMGA INSSMPFHNI HPLTIGECPK YVKSNRLVLA TGLRNTLQRE RRRKKRGLFG AIAGFIEGGW QGMVDGWYGY HHSNEQGSGY AADKESTQKA IDGITNKVNS IINKMNTQFE AVGREFSNLE RRIENLNKKM EDGFLDVWTY NAELLVLMEN ERTLDFHDSN VKNLYDKVRL QLRDNAKELG NGCFEFYHKC DDECMESVKN GTYDYPQYSE EARLNREEIN GVKLESMGTY QILSIYSTVA SSLALAIMVA GLSLWM //