ID A0FFQ6_9INFA Unreviewed; 556 AA. AC A0FFQ6; DT 28-NOV-2006, integrated into UniProtKB/TrEMBL. DT 28-NOV-2006, sequence version 1. DT 14-OCT-2008, entry version 15. DE SubName: Full=Hemagglutinin; DE Flags: Fragment; GN Name=HA; OS Influenza A virus (A/goose/Guiyang/337/2006(H5N1)). OC Viruses; ssRNA negative-strand viruses; Orthomyxoviridae; OC Influenzavirus A. OX NCBI_TaxID=407713; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/goose/Guiyang/337/2006; RA Smith G.J.D., Guan Y.; RL Submitted (SEP-2006) 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. Plays a major role in the determination of host range CC restriction and virulence. Class I viral fusion protein. CC Responsible for penetration of the virus into the cell cytoplasm CC by mediating the fusion of the membrane of the endocytosed virus CC particle with the endosomal membrane. Low pH in endosomes induce CC an irreversible conformational change in HA2, releasing the fusion CC hydrophobic peptide. Several trimers are required to form a CC competent fusion pore. 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. Plays a major role in the determination of host range CC restriction and virulence. Class I viral fusion protein. CC Responsible for penetration of the virus into the cell cytoplasm CC by mediating the fusion of the membrane of the endocytosed virus CC particle with the endosomal membrane. Low pH in endosomes induce CC an irreversible conformational change in HA2, releasing the fusion CC hydrophobic peptide. Several trimers are required to form a CC competent fusion pore (By similarity). CC -!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2. CC -!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2 (By similarity). CC -!- SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane CC protein (Potential). Apical cell membrane; Single-pass type I CC membrane protein. CC -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family. 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; -; Other_RNA. DR SMR; A0FFQ6; 17-336. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0019031; C:viral envelope; IEA:InterPro. DR GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro. DR GO; GO:0019064; P:viral envelope fusion with host membrane; IEA:InterPro. DR InterPro; IPR000149; Hemagglutn_influenz_HA1. DR InterPro; IPR001364; Hemagglutn_influenz_HA1/HA2. DR Pfam; PF00509; Hemagglutinin; 1. DR PRINTS; PR00330; HEMAGGLUTN1. DR PRINTS; PR00329; HEMAGGLUTN12. DR ProDom; PD000225; Hemagglutn; 1. PE 3: Inferred from homology; KW Cell membrane; Envelope protein; Fusion protein; Hemagglutinin; KW Membrane; Transmembrane; Virion. FT NON_TER 556 556 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 //