ID   Q1AQW8_9INFA            Unreviewed;       565 AA.
AC   Q1AQW8;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   08-NOV-2023, entry version 98.
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};
GN   Name=HA {ECO:0000256|HAMAP-Rule:MF_04072,
GN   ECO:0000313|EMBL:ABF82819.1};
OS   Influenza A virus (A/Wellington/1/2001(H1N1)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC   Alphainfluenzavirus influenzae; Influenza A virus.
OX   NCBI_TaxID=383132 {ECO:0000313|EMBL:ABF82819.1, ECO:0000313|Proteomes:UP000169419};
RN   [1] {ECO:0000313|EMBL:ABF82819.1, ECO:0000313|Proteomes:UP000169419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A/Wellington/1/2001 {ECO:0000313|EMBL:ABF82819.1};
RA   Ghedin E., Spiro D., Sengamalay N., Zaborsky J., Feldblyum T., Subbu V.,
RA   Sparenborg J., Groveman L., Halpin R., Shumway M., Sitz J., Katzel D.,
RA   Koo H., Salzberg S.L., Jennings L., Smit M., Wells V., Bao Y., Bolotov P.,
RA   Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
RT   "The NIAID Influenza Genome Sequencing Project.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABF82819.1, ECO:0000313|Proteomes:UP000169419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A/Wellington/1/2001 {ECO:0000313|EMBL:ABF82819.1};
RG   The NIAID Influenza Genome Sequencing Consortium;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000169419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bedford T., Riley S., Barr I.G., Broor S., Chadha M., Cox N.J.,
RA   Daniels R.S., Gunasekaran C.P., Hurt A.C., Kelso A., Klimov A., Lewis N.S.,
RA   Li X., McCauley J.W., Odagiri T., Potdar V., Rambaut A., Shu Y.,
RA   Skepner E., Smith D.J., Suchard M.A., Tashiro M., Wang D., Xu X., Lemey P.,
RA   Russell C.A.;
RT   "Global circulation patterns of seasonal influenza viruses vary with rates
RT   of antigenic drift.";
RL   Submitted (JAN-2015) 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 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}.
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DR   EMBL; CY011152; ABF82819.1; -; Genomic_RNA.
DR   SMR; Q1AQW8; -.
DR   Proteomes; UP000169419; 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   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   3: Inferred from homology;
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           18..343
FT                   /note="Hemagglutinin HA1 chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT                   /id="PRO_5023238643"
FT   CHAIN           344..565
FT                   /note="Hemagglutinin HA2 chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT                   /id="PRO_5023238644"
FT   TRANSMEM        530..553
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT   SITE            343..344
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT   LIPID           554
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT   LIPID           561
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT   LIPID           564
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT   DISULFID        21..480
FT                   /note="Interchain (between HA1 and HA2 chains)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT   DISULFID        59..291
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT   DISULFID        72..84
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT   DISULFID        107..152
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT   DISULFID        295..319
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT   DISULFID        487..491
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
SQ   SEQUENCE   565 AA;  63241 MW;  99C0ACE695F7EE17 CRC64;
     MKVKLLVLLC TFTATYADTI CIGYHANNST DTVDTVLEKN VTVTHSVNLL EDSHNGKLCL
     LKGIAPLQLG NCSVAGWILG NPECELLISK ESWSYIVETP NPENGTCYPG YFADYEELRE
     QLSSVSSFER FEIFPKESSW PNHTVTGVSA SCSHNGKSSF YRNLLWLTGK NGLYPNLSKS
     YANNKEKEVL VLWGVHHPPN IGDQRALYHT ENAYVSVVSS HYSRRFTPEI AKRPKVRDQE
     GRINYYWTLL EPGDTIIFEA NGNLIAPRYA FALSRGFGSG IITSNAPMDE CDAKCQTPQG
     AINSSLPFQN VHPVTIGECP KYVRSAKLRM VTGLRNIPSI QSRGLFGAIA GFIEGGWTGM
     VDGWYGYHHQ NEQGSGYAAD QKSTQNAING ITNKVNSVIE KMNTQFTAVG KEFNKLERRM
     ENLNKKVDDG FLDIWTYNAE LLVLLENERT LDFHDSNVKN LYEKVKSQLK NNAKEIGNGC
     FEFYHKCNDE CMESVKNGTY DYPKYSEESK LNREKIDGVK LESMGVYQIL AIYSTVASSL
     VLLVSLGAIS FWMCSNGSLQ CRICI
//