ID   Q9YS52_9INFA            Unreviewed;       329 AA.
AC   Q9YS52;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   08-NOV-2023, entry version 115.
DE   RecName: Full=Hemagglutinin {ECO:0000256|ARBA:ARBA00022203};
DE   Flags: Fragment;
GN   Name=HA {ECO:0000313|EMBL:AAC78090.1};
OS   Influenza A virus (A/Swine/Netherlands/L2/93(H3N2)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus;
OC   Alphainfluenzavirus influenzae; Influenza A virus.
OX   NCBI_TaxID=83928 {ECO:0000313|EMBL:AAC78090.1};
RN   [1] {ECO:0000313|EMBL:AAC78090.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/Swine/Netherlands/L2/93 {ECO:0000313|EMBL:AAC78090.1};
RA   De Jong J.C., Van Nieuwstadt A.P., Kimman T.G., Loeffen W.L.A.,
RA   Bestebroer T.M., Bijlsma K., Verweij C., Osterhaus A.D.M.E., Claas E.C.J.;
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAC78090.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/Swine/Netherlands/L2/93 {ECO:0000313|EMBL:AAC78090.1};
RX   PubMed=10195767; DOI=10.1016/S0264-410X(98)00392-2;
RA   de Jong J.C., van Nieuwstadt A.P., Kimman T.G., Loeffen W.L.A.,
RA   Bestebroer T.M., Bijlsma K., Verweij C., Osterhaus A.M.E., Class E.C.J.;
RT   "Antigenic drift in swine influenza H3 haemagglutinins with implications
RT   for vaccination policy.";
RL   Vaccine 17:1321-1328(1999).
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; AF092056; AAC78090.1; -; Genomic_RNA.
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   Gene3D; 2.10.77.10; Hemagglutinin Chain A, Domain 2; 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   3: Inferred from homology;
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:AAC78090.1"
FT   NON_TER         329
FT                   /evidence="ECO:0000313|EMBL:AAC78090.1"
SQ   SEQUENCE   329 AA;  36457 MW;  935A469B7C517952 CRC64;
     QDLPGNGNNT ATLCLGHHAV PNGTLVRTIT DDQIEVTNAT ELVQNFSMGK ICNNPHRILD
     GANCTLIDAL LGDPHCDGFQ NEKWDLFIER SKAFSNCYPY DVPEYTSLRS LIASSGTLEF
     INEGFNWTGV TQNGGSNACK RGPNSSFFSR LNWLYKSGNT YPMLNVTMPN SDSFDKLYIW
     GVHHPSTDRE QINLYVQASG KITVSTKRSQ QTIIPNVGSR PWVRGLSSRI SIYWTIVKPG
     DILIINSNGN LIAPRGYFKV HTGKSSIMRS DAPIDTCSSE CITPNGSIPN DKPFQNVNKI
     TYGACPKYVK QNTLKLATGM RNIPEKQTR
//