ID   C0IZT5_9INFA            Unreviewed;       566 AA.
AC   C0IZT5;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   08-JUN-2016, entry version 46.
DE   RecName: Full=Hemagglutinin {ECO:0000256|SAAS:SAAS00046876};
GN   Name=HA {ECO:0000313|EMBL:ACF09402.1};
OS   Influenza A virus (A/Guangdong/03/2005(H3N2)).
OC   Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC   Orthomyxoviridae; Influenzavirus A.
OX   NCBI_TaxID=543833 {ECO:0000313|EMBL:ACF09402.1};
RN   [1] {ECO:0000313|EMBL:ACF09402.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/Guangdong/03/2005 {ECO:0000313|EMBL:ACF09402.1};
RX   PubMed=19083267; DOI=10.1016/j.jcv.2008.10.011;
RA   Sun L., Zhang G., Shu Y., Chen X., Zhu Y., Yang L., Ma G.,
RA   Kitamura Y., Liu W.;
RT   "Genetic correlation between H3N2 human and swine influenza viruses.";
RL   J. Clin. Virol. 44:141-144(2009).
CC   -!- FUNCTION: Binds to sialic acid-containing receptors on the cell
CC       surface, bringing about the attachment of the virus particle to
CC       the cell. This attachment induces virion internalization of about
CC       two third of the virus particles through clathrin-dependent
CC       endocytosis and about one third through a clathrin- and caveolin-
CC       independent pathway. Plays a major role in the determination of
CC       host range restriction and virulence. Class I viral fusion
CC       protein. Responsible for penetration of the virus into the cell
CC       cytoplasm by mediating the fusion of the membrane of the
CC       endocytosed virus particle with the endosomal membrane. Low pH in
CC       endosomes induces an irreversible conformational change in HA2,
CC       releasing the fusion hydrophobic peptide. Several trimers are
CC       required to form a competent fusion pore.
CC       {ECO:0000256|RuleBase:RU003324, ECO:0000256|SAAS:SAAS00363335}.
CC   -!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2.
CC       {ECO:0000256|RuleBase:RU003324, ECO:0000256|SAAS:SAAS00046877}.
CC   -!- SUBCELLULAR LOCATION: Host apical cell membrane
CC       {ECO:0000256|SAAS:SAAS00554387}; Single-pass type I membrane
CC       protein {ECO:0000256|SAAS:SAAS00554387}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|SAAS:SAAS00562712}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane
CC       {ECO:0000256|SAAS:SAAS00562983}; Single-pass type I membrane
CC       protein {ECO:0000256|SAAS:SAAS00562983}.
CC   -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
CC       {ECO:0000256|RuleBase:RU003324, ECO:0000256|SAAS:SAAS00554249}.
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DR   EMBL; EU604298; ACF09402.1; -; Viral_cRNA.
DR   ProteinModelPortal; C0IZT5; -.
DR   SMR; C0IZT5; 25-518.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW.
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:0075512; P:clathrin-mediated 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; 2.10.77.10; -; 1.
DR   Gene3D; 3.90.20.10; -; 1.
DR   Gene3D; 3.90.209.20; -; 1.
DR   InterPro; IPR008980; Capsid_hemagglutn.
DR   InterPro; IPR013828; Hemagglutn_HA1_a/b_dom.
DR   InterPro; IPR013827; Hemagglutn_HA1_b-rbn_dom.
DR   InterPro; IPR000149; Hemagglutn_influenz_A.
DR   InterPro; IPR001364; Hemagglutn_influenz_A/B.
DR   InterPro; IPR013829; Hemagglutn_stalk.
DR   Pfam; PF00509; Hemagglutinin; 1.
DR   PRINTS; PR00330; HEMAGGLUTN1.
DR   PRINTS; PR00329; HEMAGGLUTN12.
DR   SUPFAM; SSF49818; SSF49818; 1.
PE   3: Inferred from homology;
KW   Clathrin- and caveolin-independent endocytosis of virus by host
KW   {ECO:0000256|SAAS:SAAS00440672};
KW   Clathrin-mediated endocytosis of virus by host
KW   {ECO:0000256|SAAS:SAAS00440950};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00452091};
KW   Fusion of virus membrane with host endosomal membrane
KW   {ECO:0000256|SAAS:SAAS00441030};
KW   Fusion of virus membrane with host membrane
KW   {ECO:0000256|SAAS:SAAS00440737};
KW   Hemagglutinin {ECO:0000256|RuleBase:RU003324,
KW   ECO:0000256|SAAS:SAAS00453741};
KW   Host cell membrane {ECO:0000256|SAAS:SAAS00452920};
KW   Host membrane {ECO:0000256|SAAS:SAAS00452739};
KW   Host-virus interaction {ECO:0000256|SAAS:SAAS00440928};
KW   Membrane {ECO:0000256|SAAS:SAAS00453010, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00452243,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00453372,
KW   ECO:0000256|SAM:Phobius};
KW   Viral attachment to host cell {ECO:0000256|SAAS:SAAS00441773};
KW   Viral envelope protein {ECO:0000256|RuleBase:RU003324,
KW   ECO:0000256|SAAS:SAAS00454107};
KW   Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS00441679};
KW   Virion {ECO:0000256|SAAS:SAAS00453281};
KW   Virus endocytosis by host {ECO:0000256|SAAS:SAAS00440901};
KW   Virus entry into host cell {ECO:0000256|SAAS:SAAS00440964}.
FT   TRANSMEM    530    554       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   566 AA;  63581 MW;  C9715FC626A3AA28 CRC64;
     MKTIIALSYI LCLVFAQKLP GNDNSTATLC LGHHAVPNGT IVKTITNDQI EVTNATELVQ
     SSSTGGICDS PHQILDGENC TLIDALLGDP QCDGFQNKKW DLFVERSKAY SNCYPYDVPD
     YASLRSLVAS SGTLEFNNES FNWTGVTQNG TSSACKRRSN NSFFSRLNWL THLKFKYPAL
     NVTMPNNEKF DKLYIWGVHH PGTDNDQIFL YAQASGRITV STKRSQQTVI PNIGSRPRVR
     NIPSRISIYW TIVKPGDILL INSTGNLIAP RGYFKIRSGK SSIMRSDAPI GKCNSECITP
     NGSIPNDKPF QNVNRITYGA CPRYVKQNTL KLATGMRNVP EKQTRGIFGA IAGFIENGWE
     GMVDGWYGFR HQNSEGIGQA ADLKSTQAAI NQINGKLNRL IGKTNEKFHQ IEKEFSEVEG
     RIQDLEKYVE DTKIDLWSYN AELLVALENQ HTIDLTDSEM NKLFERTKKQ LRENAEDMGN
     GCFKIYHKCD NACIGSIRNG TYDHDVYRDE ALNNRFQIKG VELKSGYKDW ILWISFAISC
     FLLCVALLGF IMWACQKGNI RCNICI
//