ID A0FFQ6_9INFA Unreviewed; 556 AA. AC A0FFQ6; DT 28-NOV-2006, integrated into UniProtKB/TrEMBL. DT 28-NOV-2006, sequence version 1. DT 11-DEC-2019, entry version 89. DE RecName: Full=Hemagglutinin {ECO:0000256|SAAS:SAAS00046903}; DE Flags: Fragment; GN Name=HA {ECO:0000313|EMBL:ABJ96698.1}; OS Influenza A virus (A/goose/Guiyang/337/2006(H5N1)). OC Viruses; Riboviria; Negarnaviricota; Polyploviricotina; Insthoviricetes; OC Articulavirales; Orthomyxoviridae; Alphainfluenzavirus. OX NCBI_TaxID=407713 {ECO:0000313|EMBL:ABJ96698.1}; RN [1] {ECO:0000313|EMBL:ABJ96698.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/goose/Guiyang/337/2006 {ECO:0000313|EMBL:ABJ96698.1}; RX PubMed=17075062; DOI=10.1073/pnas.0608157103; RA Smith G.J., Fan X.H., Wang J., Li K.S., Qin K., Zhang J.X., RA Vijaykrishna D., Cheung C.L., Huang K., Rayner J.M., Peiris J.S., Chen H., RA Webster R.G., Guan Y.; RT "Emergence and predominance of an H5N1 influenza variant in China."; RL Proc. Natl. Acad. Sci. U.S.A. 103:16936-16941(2006). RN [2] {ECO:0000313|EMBL:ABJ96698.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/goose/Guiyang/337/2006 {ECO:0000313|EMBL:ABJ96698.1}; RG The Broad Institute Genome Sequencing Platform; RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L., RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., RA Mauceli E., Brockman W., Rounsley S., Young S., LaButti K., Pushparaj V., RA DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P., RA Pearson M., Howarth C., Zeng Q., Kodira C., Yandava C., O'Leary S., RA Alvarado L., Murray M., Kreiswirth B.; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000213|PDB:4JUM} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 17-339 AND 347-522, DISULFIDE RP BONDS, AND GLYCOSYLATION AT ASN-181 AND ASN-302. RA DuBois R.M., Zaraket H., Reddivari M., Coop T., Heath R.J., White S.W., RA 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 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|SAAS:SAAS01039674}. 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, ECO:0000256|SAAS:SAAS00047800}. CC -!- SUBCELLULAR LOCATION: Host apical cell membrane CC {ECO:0000256|SAAS:SAAS00554492}; Single-pass type I membrane protein CC {ECO:0000256|SAAS:SAAS00554492}. Virion membrane CC {ECO:0000256|SAAS:SAAS00967511}; Single-pass type I membrane protein CC {ECO:0000256|SAAS:SAAS00967511}. CC -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family. CC {ECO:0000256|RuleBase:RU003324, ECO:0000256|SAAS:SAAS00963381}. 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 SMR; A0FFQ6; -. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. 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:0055036; C:virion membrane; IEA:UniProtKB-SubCell. 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; 3.90.209.20; -; 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 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:SAAS01039667}; KW Clathrin-mediated endocytosis of virus by host KW {ECO:0000256|SAAS:SAAS01039644}; Coiled coil {ECO:0000256|SAM:Coils}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00967496}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|SAAS:SAAS00963419}; KW Fusion of virus membrane with host membrane KW {ECO:0000256|SAAS:SAAS00963379}; KW Hemagglutinin {ECO:0000256|RuleBase:RU003324, KW ECO:0000256|SAAS:SAAS00967480}; KW Host cell membrane {ECO:0000256|SAAS:SAAS00967506}; KW Host membrane {ECO:0000256|SAAS:SAAS00967527}; KW Host-virus interaction {ECO:0000256|SAAS:SAAS00963361}; KW Membrane {ECO:0000256|SAAS:SAAS00967516, ECO:0000256|SAM:Phobius}; KW Transmembrane {ECO:0000256|SAAS:SAAS00967476, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00967518, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|SAAS:SAAS00963390}; KW Viral envelope protein {ECO:0000256|RuleBase:RU003324, KW ECO:0000256|SAAS:SAAS00967473}; KW Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS00963370}; KW Virion {ECO:0000256|SAAS:SAAS01198246}; KW Virus endocytosis by host {ECO:0000256|SAAS:SAAS00963339}; KW Virus entry into host cell {ECO:0000256|SAAS:SAAS00963443}. FT TRANSMEM 533..555 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT COILED 402..429 FT /evidence="ECO:0000256|SAM:Coils" FT CARBOHYD 181 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000213|PDB:4JUM" FT CARBOHYD 302 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000213|PDB:4JUM" FT DISULFID 20 FT /note="Interchain (with C-483)" FT /evidence="ECO:0000213|PDB:4JUM" FT DISULFID 58..290 FT /evidence="ECO:0000213|PDB:4JUM" FT DISULFID 71..83 FT /evidence="ECO:0000213|PDB:4JUM" FT DISULFID 106..151 FT /evidence="ECO:0000213|PDB:4JUM" FT DISULFID 294..318 FT /evidence="ECO:0000213|PDB:4JUM" FT DISULFID 483 FT /note="Interchain (with C-20)" FT /evidence="ECO:0000213|PDB:4JUM" FT DISULFID 490..494 FT /evidence="ECO:0000213|PDB:4JUM" FT NON_TER 556 FT /evidence="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 //