ID C3W5S1_I09A0 Unreviewed; 566 AA.
AC C3W5S1;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Hemagglutinin {ECO:0000256|HAMAP-Rule:MF_04072};
DE Contains:
DE RecName: Full=Hemagglutinin HA1 chain {ECO:0000256|HAMAP-Rule:MF_04072};
DE Contains:
DE RecName: Full=Hemagglutinin HA2 chain {ECO:0000256|HAMAP-Rule:MF_04072};
DE Flags: Precursor;
GN Name=HA {ECO:0000256|HAMAP-Rule:MF_04072,
GN ECO:0000313|EMBL:ACP41105.1};
OS Influenza A virus (strain swl A/California/04/2009 H1N1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC Alphainfluenzavirus influenzae; Influenza A virus.
OX NCBI_TaxID=641501 {ECO:0000313|EMBL:ACP41105.1, ECO:0000313|Proteomes:UP000132424};
OH NCBI_TaxID=8782; Aves (birds).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1] {ECO:0000313|EMBL:ACP41105.1, ECO:0000313|Proteomes:UP000132424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A/California/04/2009 {ECO:0000313|EMBL:ACP41105.1};
RX PubMed=19423869; DOI=10.1056/NEJMoa0903810;
RG Novel Swine-Origin Influenza A (H1N1) Virus Investigation Team;
RA Dawood F.S., Jain S., Finelli L., Shaw M.W., Lindstrom S., Garten R.J.,
RA Gubareva L.V., Xu X., Bridges C.B., Uyeki T.M.;
RT "Emergence of a novel swine-origin influenza A (H1N1) virus in humans.";
RL N. Engl. J. Med. 360:2605-2615(2009).
RN [2] {ECO:0000313|EMBL:ACP41105.1, ECO:0000313|Proteomes:UP000132424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A/California/04/2009 {ECO:0000313|EMBL:ACP41105.1};
RX PubMed=19465683; DOI=10.1126/science.1176225;
RA Garten R.J., Davis C.T., Russell C.A., Shu B., Lindstrom S., Balish A.,
RA Sessions W.M., Xu X., Skepner E., Deyde V., Okomo-Adhiambo M., Gubareva L.,
RA Barnes J., Smith C.B., Emery S.L., Hillman M.J., Rivailler P., Smagala J.,
RA de Graaf M., Burke D.F., Fouchier R.A., Pappas C., Alpuche-Aranda C.M.,
RA Lopez-Gatell H., Olivera H., Lopez I., Myers C.A., Faix D., Blair P.J.,
RA Yu C., Keene K.M., Dotson P.D.Jr., Boxrud D., Sambol A.R., Abid S.H.,
RA St George K., Bannerman T., Moore A.L., Stringer D.J., Blevins P.,
RA Demmler-Harrison G.J., Ginsberg M., Kriner P., Waterman S., Smole S.,
RA Guevara H.F., Belongia E.A., Clark P.A., Beatrice S.T., Donis R., Katz J.,
RA Finelli L., Bridges C.B., Shaw M., Jernigan D.B., Uyeki T.M., Smith D.J.,
RA Klimov A.I., Cox N.J.;
RT "Antigenic and genetic characteristics of swine-origin 2009 A(H1N1)
RT influenza viruses circulating in humans.";
RL Science 325:197-201(2009).
RN [3] {ECO:0007829|PDB:3AL4}
RP X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 18-344 AND 345-520, DISULFIDE
RP BONDS, AND GLYCOSYLATION AT ASN-40; ASN-104; ASN-293 AND ASN-304.
RX PubMed=21203961; DOI=10.1007/s13238-010-0059-1;
RA Zhang W., Qi J., Shi Y., Li Q., Gao F., Sun Y., Lu X., Lu Q.,
RA Vavricka C.J., Liu D., Yan J., Gao G.F.;
RT "Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus
RT hemagglutinin (HA) reveals similar antigenicity to that of the 1918
RT pandemic virus.";
RL Protein Cell 1:459-467(2010).
RN [4] {ECO:0007829|PDB:3LZG}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 18-344 AND 345-518, DISULFIDE
RP BONDS, AND GLYCOSYLATION AT ASN-104 AND ASN-293.
RX PubMed=20339031; DOI=10.1126/science.1186430;
RA Xu R., Ekiert D.C., Krause J.C., Hai R., Crowe J.E., Wilson I.A.;
RT "Structural basis of preexisting immunity to the 2009 H1N1 pandemic
RT influenza virus.";
RL Science 328:357-360(2010).
RN [5] {ECO:0007829|PDB:3UYW, ECO:0007829|PDB:3UYX}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 65-278, AND DISULFIDE BONDS.
RX PubMed=22231357; DOI=10.1007/s13238-011-1134-y;
RA Xuan C., Shi Y., Qi J., Zhang W., Xiao H., Gao G.F.;
RT "Structural vaccinology: structure-based design of influenza A virus
RT hemagglutinin subtype-specific subunit vaccines.";
RL Protein Cell 2:997-1005(2011).
RN [6] {ECO:0007829|PDB:3ZTN}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 18-344 AND 345-520, DISULFIDE
RP BONDS, AND GLYCOSYLATION AT ASN-40 AND ASN-293.
RX PubMed=21798894; DOI=10.1126/science.1205669;
RA Corti D., Voss J., Gamblin S.J., Codoni G., Macagno A., Jarrossay D.,
RA Vachieri S.G., Pinna D., Minola A., Vanzetta F., Silacci C.,
RA Fernandez-Rodriguez B.M., Agatic G., Bianchi S., Giacchetto-Sasselli I.,
RA Calder L., Sallusto F., Collins P., Haire L.F., Temperton N.,
RA Langedijk J.P., Skehel J.J., Lanzavecchia A.;
RT "A neutralizing antibody selected from plasma cells that binds to group 1
RT and group 2 influenza A hemagglutinins.";
RL Science 333:850-856(2011).
RN [7] {ECO:0007829|PDB:3UBE, ECO:0007829|PDB:3UBJ}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 18-344 AND 345-518 IN COMPLEX
RP WITH GALACTOSE, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-28; ASN-40;
RP ASN-104; ASN-293; ASN-304 AND ASN-498.
RX PubMed=22072785; DOI=10.1128/JVI.06322-11;
RA Xu R., McBride R., Nycholat C.M., Paulson J.C., Wilson I.A.;
RT "Structural characterization of the hemagglutinin receptor specificity from
RT the 2009 H1N1 influenza pandemic.";
RL J. Virol. 86:982-990(2012).
RN [8] {ECO:0007829|PDB:4JTV, ECO:0007829|PDB:4JTX}
RP X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 18-339 AND 345-508 IN COMPLEX
RP WITH GALACTOSE, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-28; ASN-40;
RP ASN-104 AND ASN-293.
RX PubMed=23514882; DOI=10.1128/JVI.00545-13;
RA Zhang W., Shi Y., Qi J., Gao F., Li Q., Fan Z., Yan J., Gao G.F.;
RT "Molecular basis of the receptor binding specificity switch of the
RT hemagglutinins from both the 1918 and 2009 pandemic influenza A viruses by
RT a D225G substitution.";
RL J. Virol. 87:5949-5958(2013).
RN [9] {ECO:0007829|PDB:4M4Y}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 18-344 AND 345-518, DISULFIDE
RP BONDS, AND GLYCOSYLATION AT ASN-28; ASN-40; ASN-104 AND ASN-293.
RX PubMed=24027321; DOI=10.1128/JVI.01388-13;
RA Hong M., Lee P.S., Hoffman R.M., Zhu X., Krause J.C., Laursen N.S.,
RA Yoon S.I., Song L., Tussey L., Crowe J.E., Ward A.B., Wilson I.A.;
RT "Antibody recognition of the pandemic H1N1 Influenza virus hemagglutinin
RT receptor binding site.";
RL J. Virol. 87:12471-12480(2013).
RN [10] {ECO:0000313|Proteomes:UP000132424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26404790; DOI=10.1186/s13567-015-0236-6;
RA Qiu Y., De Hert K., Van Reeth K.;
RT "Cross-protection against European swine influenza viruses in the context
RT of infection immunity against the 2009 pandemic H1N1 virus: studies in the
RT pig model of influenza.";
RL Vet. Res. 46:105-105(2015).
RN [11] {ECO:0007829|PDB:5K9O}
RP X-RAY CRYSTALLOGRAPHY (3.39 ANGSTROMS) OF 18-520, AND DISULFIDE BONDS.
RX PubMed=27453470; DOI=10.1016/j.cell.2016.06.043;
RG NISC Comparative Sequencing Program;
RA Joyce M.G., Wheatley A.K., Thomas P.V., Chuang G.Y., Soto C., Bailer R.T.,
RA Druz A., Georgiev I.S., Gillespie R.A., Kanekiyo M., Kong W.P., Leung K.,
RA Narpala S.N., Prabhakaran M.S., Yang E.S., Zhang B., Zhang Y., Asokan M.,
RA Boyington J.C., Bylund T., Darko S., Lees C.R., Ransier A., Shen C.H.,
RA Wang L., Whittle J.R., Wu X., Yassine H.M., Santos C., Matsuoka Y.,
RA Tsybovsky Y., Baxa U., Mullikin J.C., Subbarao K., Douek D.C., Graham B.S.,
RA Koup R.A., Ledgerwood J.E., Roederer M., Shapiro L., Kwong P.D.,
RA Mascola J.R., McDermott A.B.;
RT "Vaccine-Induced Antibodies that Neutralize Group 1 and Group 2 Influenza A
RT Viruses.";
RL Cell 166:609-623(2016).
RN [12] {ECO:0007829|PDB:5GJS}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 18-344 AND 345-520, AND DISULFIDE
RP BONDS.
RX PubMed=27910950; DOI=10.1038/ncomms13577;
RA Wang W., Sun X., Li Y., Su J., Ling Z., Zhang T., Wang F., Zhang H.,
RA Chen H., Ding J., Sun B.;
RT "Human antibody 3E1 targets the HA stem region of H1N1 and H5N6 influenza A
RT viruses.";
RL Nat. Commun. 7:13577-13577(2016).
RN [13] {ECO:0007829|PDB:5WKO}
RP X-RAY CRYSTALLOGRAPHY (3.49 ANGSTROMS) OF 18-344, AND DISULFIDE BONDS.
RX PubMed=28930686; DOI=10.1016/j.celrep.2017.08.084;
RA Lang S., Xie J., Zhu X., Wu N.C., Lerner R.A., Wilson I.A.;
RT "Antibody 27F3 Broadly Targets Influenza A Group 1 and 2 Hemagglutinins
RT through a Further Variation in VH1-69 Antibody Orientation on
RT the HA Stem.";
RL Cell Rep. 20:2935-2943(2017).
RN [14] {ECO:0007829|PDB:6WJ1}
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 18-344 AND 345-519, AND DISULFIDE
RP BONDS.
RX PubMed=32619441; DOI=10.1016/j.chom.2020.06.003;
RA Wu N.C., Andrews S.F., Raab J.E., O'Connell S., Schramm C.A., Ding X.,
RA Chambers M.J., Leung K., Wang L., Zhang Y., Mascola J.R., Douek D.C.,
RA Ledgerwood J.E., McDermott A.B., Wilson I.A.;
RT "Convergent Evolution in Breadth of Two VH6-1-Encoded Influenza
RT Antibody Clonotypes from a Single Donor.";
RL Cell Host Microbe 28:434-444.e4(2020).
RN [15] {ECO:0007829|PDB:6URM}
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 18-520, AND DISULFIDE BONDS.
RX PubMed=32877670; DOI=10.1016/j.celrep.2020.108088;
RA Cheung C.S., Fruehwirth A., Paparoditis P.C.G., Shen C.H., Foglierini M.,
RA Joyce M.G., Leung K., Piccoli L., Rawi R., Silacci-Fregni C., Tsybovsky Y.,
RA Verardi R., Wang L., Wang S., Yang E.S., Zhang B., Zhang Y., Chuang G.Y.,
RA Corti D., Mascola J.R., Shapiro L., Kwong P.D., Lanzavecchia A., Zhou T.;
RT "Identification and Structure of a Multidonor Class of Head-Directed
RT Influenza-Neutralizing Antibodies Reveal the Mechanism for Its Recurrent
RT Elicitation.";
RL Cell Rep. 32:108088-108088(2020).
RN [16] {ECO:0007829|PDB:7MEM}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF 345-518 AND 18-344,
RP AND DISULFIDE BONDS.
RX PubMed=34078743; DOI=10.1126/scitranslmed.abg4535;
RA Guthmiller J.J., Han J., Li L., Freyn A.W., Liu S.T.H., Stovicek O.,
RA Stamper C.T., Dugan H.L., Tepora M.E., Utset H.A., Bitar D.J., Hamel N.J.,
RA Changrob S., Zheng N.Y., Huang M., Krammer F., Nachbagauer R., Palese P.,
RA Ward A.B., Wilson P.C.;
RT "First exposure to the pandemic H1N1 virus induced broadly neutralizing
RT antibodies targeting hemagglutinin head epitopes.";
RL Sci. Transl. Med. 13:eabg4535-eabg4535(2021).
RN [17] {ECO:0007829|PDB:7FAH}
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 18-518, AND DISULFIDE BONDS.
RX PubMed=36056024; DOI=10.1038/s41467-022-32926-5;
RA Li T., Chen J., Zheng Q., Xue W., Zhang L., Rong R., Zhang S., Wang Q.,
RA Hong M., Zhang Y., Cui L., He M., Lu Z., Zhang Z., Chi X., Li J., Huang Y.,
RA Wang H., Tang J., Ying D., Zhou L., Wang Y., Yu H., Zhang J., Gu Y.,
RA Chen Y., Li S., Xia N.;
RT "Identification of a cross-neutralizing antibody that targets the receptor
RT binding site of H1N1 and H5N1 influenza viruses.";
RL Nat. Commun. 13:5182-5182(2022).
RN [18] {ECO:0007829|PDB:7T3D}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF 18-344 AND 345-518,
RP AND DISULFIDE BONDS.
RX PubMed=34942633; DOI=10.1038/s41586-021-04356-8;
RA Guthmiller J.J., Han J., Utset H.A., Li L., Lan L.Y., Henry C.,
RA Stamper C.T., McMahon M., O'Dell G., Fernandez-Quintero M.L., Freyn A.W.,
RA Amanat F., Stovicek O., Gentles L., Richey S.T., de la Pena A.T.,
RA Rosado V., Dugan H.L., Zheng N.Y., Tepora M.E., Bitar D.J., Changrob S.,
RA Strohmeier S., Huang M., Garcia-Sastre A., Liedl K.R., Bloom J.D.,
RA Nachbagauer R., Palese P., Krammer F., Coughlan L., Ward A.B., Wilson P.C.;
RT "Broadly neutralizing antibodies target a haemagglutinin anchor epitope.";
RL Nature 602:314-320(2022).
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|HAMAP-Rule:MF_04072}.
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. {ECO:0000256|HAMAP-
CC Rule:MF_04072, 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, ECO:0000256|HAMAP-Rule:MF_04072};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004310,
CC ECO:0000256|HAMAP-Rule:MF_04072}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Virion membrane {ECO:0000256|HAMAP-
CC Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_04072}. Note=Targeted to the apical plasma membrane in
CC epithelial polarized cells through a signal present in the
CC transmembrane domain. Associated with glycosphingolipid- and
CC cholesterol-enriched detergent-resistant lipid rafts.
CC {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 identified
CC protease that may be involved in this process is secreted in lungs by
CC club cells. {ECO:0000256|HAMAP-Rule:MF_04072}.
CC -!- PTM: Palmitoylated. {ECO:0000256|HAMAP-Rule:MF_04072}.
CC -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
CC {ECO:0000256|ARBA:ARBA00006321, ECO:0000256|HAMAP-Rule:MF_04072,
CC ECO:0000256|RuleBase:RU003324}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04072}.
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DR EMBL; FJ966082; ACP41105.1; -; Viral_cRNA.
DR EMBL; GQ117044; ACQ76318.1; -; Viral_cRNA.
DR PDB; 3AL4; X-ray; 2.87 A; A/C/E/G/I/K=18-344, B/D/F/H/J/L=345-520.
DR PDB; 3LZG; X-ray; 2.60 A; A/C/E/G/I/K=18-344, B/D/F/H/J/L=345-518.
DR PDB; 3UBE; X-ray; 2.15 A; A/C/E/G/I/K=18-344, B/D/F/H/J/L=345-518.
DR PDB; 3UBJ; X-ray; 2.25 A; A/C/E/G/I/K=18-344, B/D/F/H/J/L=345-518.
DR PDB; 3UBN; X-ray; 2.51 A; A/C/E/G/I/K=18-344, B/D/F/H/J/L=345-518.
DR PDB; 3UBQ; X-ray; 2.00 A; A/C/E/G/I/K=18-344, B/D/F/H/J/L=345-518.
DR PDB; 3UYW; X-ray; 1.90 A; A/B/C/D=65-278.
DR PDB; 3UYX; X-ray; 1.80 A; A/B=65-278.
DR PDB; 3ZTN; X-ray; 3.00 A; A=18-344, B=345-520.
DR PDB; 4JTV; X-ray; 3.00 A; A/C/E/G/I/K=18-338, B/D/F/H/J/L=345-506.
DR PDB; 4JTX; X-ray; 3.00 A; A/C/E/G/I/K=18-339, B/D/F/H/J/L=345-510.
DR PDB; 4JU0; X-ray; 2.91 A; A/C/E/G/I/K=18-339, B/D/F/H/J/L=345-508.
DR PDB; 4M4Y; X-ray; 2.20 A; A/C/E=18-344, B/D/F=345-518.
DR PDB; 5GJS; X-ray; 2.90 A; A=18-344, B=345-520.
DR PDB; 5K9O; X-ray; 3.39 A; F/I=18-520.
DR PDB; 5WKO; X-ray; 3.49 A; M/N/O/S/T/U=18-344.
DR PDB; 6URM; X-ray; 2.65 A; C/F=18-520.
DR PDB; 6WJ1; X-ray; 3.50 A; A/C/E=18-344, B/D/F=345-519.
DR PDB; 7FAH; X-ray; 3.15 A; A/B=18-518.
DR PDB; 7MEM; EM; 3.20 A; A/B/D=345-518, C/E/F=18-344.
DR PDB; 7T3D; EM; 3.38 A; A/E/F=18-344, B/G/I=345-518.
DR PDBsum; 3AL4; -.
DR PDBsum; 3LZG; -.
DR PDBsum; 3UBE; -.
DR PDBsum; 3UBJ; -.
DR PDBsum; 3UBN; -.
DR PDBsum; 3UBQ; -.
DR PDBsum; 3UYW; -.
DR PDBsum; 3UYX; -.
DR PDBsum; 3ZTN; -.
DR PDBsum; 4JTV; -.
DR PDBsum; 4JTX; -.
DR PDBsum; 4JU0; -.
DR PDBsum; 4M4Y; -.
DR PDBsum; 5GJS; -.
DR PDBsum; 5K9O; -.
DR PDBsum; 5WKO; -.
DR EMDB; EMD-23792; -.
DR EMDB; EMD-25655; -.
DR Proteomes; UP000132424; Genome.
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-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; 3.90.20.10; -; 1.
DR Gene3D; 3.90.209.20; -; 1.
DR Gene3D; 2.10.77.10; Hemagglutinin Chain A, Domain 2; 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; SSF58064; Influenza hemagglutinin (stalk); 1.
DR SUPFAM; SSF49818; Viral protein domain; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3AL4, ECO:0007829|PDB:3LZG};
KW Clathrin- and caveolin-independent endocytosis of virus by host
KW {ECO:0000256|ARBA:ARBA00023261, ECO:0000256|HAMAP-Rule:MF_04072};
KW Clathrin-mediated endocytosis of virus by host
KW {ECO:0000256|ARBA:ARBA00022570, ECO:0000256|HAMAP-Rule:MF_04072};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW Rule:MF_04072};
KW Fusion of virus membrane with host endosomal membrane
KW {ECO:0000256|ARBA:ARBA00022510, ECO:0000256|HAMAP-Rule:MF_04072};
KW Fusion of virus membrane with host membrane {ECO:0000256|ARBA:ARBA00022506,
KW ECO:0000256|HAMAP-Rule:MF_04072};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|HAMAP-
KW Rule:MF_04072};
KW Hemagglutinin {ECO:0000256|ARBA:ARBA00022546, ECO:0000256|HAMAP-
KW Rule:MF_04072};
KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511, ECO:0000256|HAMAP-
KW Rule:MF_04072};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870, ECO:0000256|HAMAP-
KW Rule:MF_04072};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, ECO:0000256|HAMAP-
KW Rule:MF_04072};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW Rule:MF_04072};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_04072};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_04072};
KW Signal {ECO:0000256|HAMAP-Rule:MF_04072};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_04072};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04072};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804,
KW ECO:0000256|HAMAP-Rule:MF_04072};
KW Viral envelope protein {ECO:0000256|ARBA:ARBA00022879, ECO:0000256|HAMAP-
KW Rule:MF_04072};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595,
KW ECO:0000256|HAMAP-Rule:MF_04072};
KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04072};
KW Virus endocytosis by host {ECO:0000256|ARBA:ARBA00022890,
KW ECO:0000256|HAMAP-Rule:MF_04072};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296,
KW ECO:0000256|HAMAP-Rule:MF_04072}.
FT CHAIN 345..566
FT /note="Hemagglutinin HA2 chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT /id="PRO_5041491885"
FT TRANSMEM 531..554
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT SITE 344..345
FT /note="Cleavage; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT LIPID 555
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT LIPID 562
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT LIPID 565
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT CARBOHYD 28
FT /note="N-acetyl-D-glucosamine 1"
FT /evidence="ECO:0007829|PDB:3AL4, ECO:0007829|PDB:4JTV"
FT CARBOHYD 28
FT /note="N-acetyl-D-glucosamine 2"
FT /evidence="ECO:0007829|PDB:3UBQ"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:3AL4, ECO:0007829|PDB:3UBQ"
FT CARBOHYD 34
FT /note="N-acetyl-D-glucosamine 3"
FT /evidence="ECO:0007829|PDB:4JTV"
FT CARBOHYD 39
FT /note="N-acetyl-D-glucosamine 3"
FT /evidence="ECO:0007829|PDB:4JTV"
FT CARBOHYD 40
FT /note="N-acetyl-D-glucosamine 3"
FT /evidence="ECO:0007829|PDB:4JTV"
FT CARBOHYD 40
FT /note="N-acetyl-D-glucosamine 4"
FT /evidence="ECO:0007829|PDB:3UBQ, ECO:0007829|PDB:4JTX"
FT CARBOHYD 40
FT /note="N-acetyl-D-glucosamine 5"
FT /evidence="ECO:0007829|PDB:4JU0"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:3UBQ, ECO:0007829|PDB:4JTV"
FT CARBOHYD 62
FT /note="N-acetyl-D-glucosamine 5"
FT /evidence="ECO:0007829|PDB:4JU0"
FT CARBOHYD 81
FT /note="N-acetyl-D-glucosamine 7"
FT /evidence="ECO:0007829|PDB:3LZG, ECO:0007829|PDB:3UBQ"
FT CARBOHYD 81
FT /note="N-acetyl-D-glucosamine 8"
FT /evidence="ECO:0007829|PDB:6URM"
FT CARBOHYD 103
FT /note="N-acetyl-D-glucosamine 7"
FT /evidence="ECO:0007829|PDB:3LZG, ECO:0007829|PDB:3UBQ"
FT CARBOHYD 104
FT /note="N-acetyl-D-glucosamine 6"
FT /evidence="ECO:0007829|PDB:4JU0"
FT CARBOHYD 104
FT /note="N-acetyl-D-glucosamine 7"
FT /evidence="ECO:0007829|PDB:3LZG, ECO:0007829|PDB:3UBQ"
FT CARBOHYD 104
FT /note="N-acetyl-D-glucosamine 8"
FT /evidence="ECO:0007829|PDB:6URM"
FT CARBOHYD 104
FT /note="N-acetyl-D-glucosamine 9"
FT /evidence="ECO:0007829|PDB:7FAH"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:3LZG, ECO:0007829|PDB:3UBQ"
FT CARBOHYD 154
FT /note="N-acetyl-D-glucosamine 6"
FT /evidence="ECO:0007829|PDB:4JU0"
FT CARBOHYD 238
FT /note="N-acetyl-D-glucosamine 7"
FT /evidence="ECO:0007829|PDB:3LZG, ECO:0007829|PDB:3UBQ"
FT CARBOHYD 291
FT /note="N-acetyl-D-glucosamine 10"
FT /evidence="ECO:0007829|PDB:4M4Y"
FT CARBOHYD 293
FT /note="N-acetyl-D-glucosamine 10"
FT /evidence="ECO:0007829|PDB:4M4Y"
FT CARBOHYD 293
FT /note="N-acetyl-D-glucosamine 11"
FT /evidence="ECO:0007829|PDB:3AL4, ECO:0007829|PDB:3UBE"
FT CARBOHYD 293
FT /note="N-acetyl-D-glucosamine 12"
FT /evidence="ECO:0007829|PDB:3UBJ, ECO:0007829|PDB:3UBQ"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:3AL4, ECO:0007829|PDB:3UBE"
FT CARBOHYD 293
FT /note="O-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:3AL4"
FT CARBOHYD 304
FT /note="N-acetyl-D-glucosamine 12"
FT /evidence="ECO:0007829|PDB:3UBJ, ECO:0007829|PDB:3UBQ"
FT CARBOHYD 304
FT /note="N-acetyl-D-glucosamine 13"
FT /evidence="ECO:0007829|PDB:4JU0, ECO:0007829|PDB:6WJ1"
FT CARBOHYD 304
FT /note="N-acetyl-D-glucosamine 2"
FT /evidence="ECO:0007829|PDB:3UBQ"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:3UBJ, ECO:0007829|PDB:3UBQ"
FT CARBOHYD 498
FT /note="N-acetyl-D-glucosamine 14"
FT /evidence="ECO:0007829|PDB:3UBE, ECO:0007829|PDB:3UBJ"
FT CARBOHYD 498
FT /note="N-acetyl-D-glucosamine 15"
FT /evidence="ECO:0007829|PDB:3UBN"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:3UBE, ECO:0007829|PDB:3UBJ"
FT CARBOHYD 500
FT /note="N-acetyl-D-glucosamine 15"
FT /evidence="ECO:0007829|PDB:3UBN"
FT DISULFID 21..481
FT /evidence="ECO:0007829|PDB:5K9O"
FT DISULFID 21
FT /note="Interchain (with C-481 in C5MVT7)"
FT /evidence="ECO:0007829|PDB:5WKO"
FT DISULFID 21
FT /note="Interchain (with C-481)"
FT /evidence="ECO:0007829|PDB:3AL4, ECO:0007829|PDB:3LZG"
FT DISULFID 59..292
FT /evidence="ECO:0007829|PDB:3AL4, ECO:0007829|PDB:3LZG"
FT DISULFID 72..84
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072,
FT ECO:0007829|PDB:3AL4"
FT DISULFID 107..153
FT /evidence="ECO:0007829|PDB:3AL4, ECO:0007829|PDB:3LZG"
FT DISULFID 296..320
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072,
FT ECO:0007829|PDB:3AL4"
FT DISULFID 481
FT /note="Interchain (with C-21)"
FT /evidence="ECO:0007829|PDB:3AL4, ECO:0007829|PDB:3LZG"
FT DISULFID 488..492
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04072,
FT ECO:0007829|PDB:3AL4"
SQ SEQUENCE 566 AA; 63276 MW; FBCE01FBF1FCA445 CRC64;
MKAILVVLLY TFATANADTL CIGYHANNST DTVDTVLEKN VTVTHSVNLL EDKHNGKLCK
LRGVAPLHLG KCNIAGWILG NPECESLSTA SSWSYIVETP SSDNGTCYPG DFIDYEELRE
QLSSVSSFER FEIFPKTSSW PNHDSNKGVT AACPHAGAKS FYKNLIWLVK KGNSYPKLSK
SYINDKGKEV LVLWGIHHPS TSADQQSLYQ NADTYVFVGS SRYSKKFKPE IAIRPKVRDQ
EGRMNYYWTL VEPGDKITFE ATGNLVVPRY AFAMERNAGS GIIISDTPVH DCNTTCQTPK
GAINTSLPFQ NIHPITIGKC PKYVKSTKLR LATGLRNIPS IQSRGLFGAI AGFIEGGWTG
MVDGWYGYHH QNEQGSGYAA DLKSTQNAID EITNKVNSVI EKMNTQFTAV GKEFNHLEKR
IENLNKKVDD GFLDIWTYNA ELLVLLENER TLDYHDSNVK NLYEKVRSQL KNNAKEIGNG
CFEFYHKCDN TCMESVKNGT YDYPKYSEEA KLNREEIDGV KLESTRIYQI LAIYSTVASS
LVLVVSLGAI SFWMCSNGSL QCRICI
//