ID   Q91LS8_9INFA            Unreviewed;       281 AA.
AC   Q91LS8;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   08-NOV-2023, entry version 118.
DE   RecName: Full=Hemagglutinin {ECO:0000256|ARBA:ARBA00022203};
DE   Flags: Fragment;
GN   Name=HA {ECO:0000313|EMBL:AAK82869.1};
OS   Influenza A virus (A/Taiwan/0095/1996(H3N2)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC   Alphainfluenzavirus influenzae; Influenza A virus.
OX   NCBI_TaxID=162497 {ECO:0000313|EMBL:AAK82869.1};
RN   [1] {ECO:0000313|EMBL:AAK82869.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/human/Taiwan/0095/96 {ECO:0000313|EMBL:AAK82869.1};
RA   Shih S.-R., Chen G.-W., Bair C.-H., Bai Y.-L., Yang C.-C., Tsai M.-C.;
RT   "Browser-Based Java Applications for Search and Analysis of Influenza
RT   Sequences in GenBank Format.";
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:2OJE}
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 260-272.
RX   PubMed=17166841; DOI=10.1074/jbc.M608482200;
RA   Li H., Zhao Y., Guo Y., Li Z., Eisele L., Mourad W.;
RT   "Zinc induces dimerization of the class II major histocompatibility complex
RT   molecule that leads to cooperative binding to a superantigen.";
RL   J. Biol. Chem. 282:5991-6000(2007).
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}.
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}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004310}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
CC       {ECO:0000256|ARBA:ARBA00006321, ECO:0000256|RuleBase:RU003324}.
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DR   EMBL; AF362820; AAK82869.1; -; mRNA.
DR   PDB; 2OJE; X-ray; 3.00 A; C/G=260-272.
DR   PDBsum; 2OJE; -.
DR   SMR; Q91LS8; -.
DR   EvolutionaryTrace; Q91LS8; -.
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-KW.
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   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; Viral protein domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:2OJE};
KW   Clathrin- and caveolin-independent endocytosis of virus by host
KW   {ECO:0000256|ARBA:ARBA00023261};
KW   Clathrin-mediated endocytosis of virus by host
KW   {ECO:0000256|ARBA:ARBA00022570};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Fusion of virus membrane with host endosomal membrane
KW   {ECO:0000256|ARBA:ARBA00022510};
KW   Fusion of virus membrane with host membrane
KW   {ECO:0000256|ARBA:ARBA00022506};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hemagglutinin {ECO:0000256|ARBA:ARBA00022546,
KW   ECO:0000256|RuleBase:RU003324};
KW   Host cell membrane {ECO:0000256|ARBA:ARBA00022511};
KW   Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW   Viral envelope protein {ECO:0000256|ARBA:ARBA00022879,
KW   ECO:0000256|RuleBase:RU003324};
KW   Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595};
KW   Virion {ECO:0000256|ARBA:ARBA00022844};
KW   Virus endocytosis by host {ECO:0000256|ARBA:ARBA00022890};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAK82869.1"
FT   NON_TER         281
FT                   /evidence="ECO:0000313|EMBL:AAK82869.1"
SQ   SEQUENCE   281 AA;  31362 MW;  63B306D7AD351E2D CRC64;
     STGRICDSPH RILDGKNCTL IDALLGDPHC DGFQNKEWDL FVERSKAYSN CYPYDVPDYA
     SLRSLVASSG TLEFTNEGFN WTGVAQNGTS YACKRGSVKS FFSRLNWLHK LEYKYPALNV
     TMPNNDKFDK LYIWGVHHPS TDSDQTSLYV QASGRITVST KRSQQTVIPN IGSRPWVRGV
     SSIISIYWTI VKPGDILLIN STGNLIAPRG YFKIRSGKSS IMRSDAPIGN CNSECITPNG
     SIPNDKPFQN VNRITYGACP KYVKQNTLKL ATGMRNVPEK Q
//