ID   C1FXN8_9INFA            Unreviewed;       566 AA.
AC   C1FXN8;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-FEB-2011, entry version 14.
DE   SubName: Full=Hemagglutinin;
DE   Flags: Precursor;
GN   Name=HA;
OS   Influenza A virus (A/Hong Kong/HKU70/2005(H3N2)).
OC   Viruses; ssRNA negative-strand viruses; Orthomyxoviridae;
OC   Influenzavirus A.
OX   NCBI_TaxID=586208;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/Hong Kong/HKU70/2005;
RA   Spiro D., Halpin R., Bera J., Ghedin E., Hostetler J., Fedorova N.,
RA   Hine E., Overton L., Djuric K., Sarmiento M., Sitz J., Katzel D.,
RA   Chan K.H., Guan Y., Peiris J.S., Smith G.J., Bao Y., Sanders R.,
RA   Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
RT   "The NIAID Influenza Genome Sequencing Project.";
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/Hong Kong/HKU70/2005;
RG   The NIAID Influenza Genome Sequencing Consortium;
RL   Submitted (MAR-2009) 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
CC       the cell. Plays a major role in the determination of host range
CC       restriction and virulence. Class I viral fusion protein.
CC       Responsible for penetration of the virus into the cell cytoplasm
CC       by mediating the fusion of the membrane of the endocytosed virus
CC       particle with the endosomal membrane. Low pH in endosomes induce
CC       an irreversible conformational change in HA2, releasing the fusion
CC       hydrophobic peptide. Several trimers are required to form a
CC       competent fusion pore (By similarity).
CC   -!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2 (By similarity).
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DR   EMBL; CY038735; ACO36661.1; -; Viral_cRNA.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:InterPro.
DR   GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro.
DR   GO; GO:0019064; P:viral envelope fusion with host membrane; IEA:InterPro.
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   Gene3D; G3DSA:3.90.209.20; Haemagglutn_HA1_a/b; 1.
DR   Gene3D; G3DSA:2.10.77.10; Haemagglutn_HA1_b-ribbon; 1.
DR   Gene3D; G3DSA:3.90.20.10; Haemagglutn_stalk; 1.
DR   Pfam; PF00509; Hemagglutinin; 1.
DR   PRINTS; PR00330; HEMAGGLUTN1.
DR   PRINTS; PR00329; HEMAGGLUTN12.
DR   SUPFAM; SSF49818; Capsid_hemag; 1.
PE   3: Inferred from homology;
KW   Hemagglutinin; Host cell membrane; Host membrane; Membrane; Signal;
KW   Transmembrane; Transmembrane helix; Viral envelope protein; Virion.
FT   SIGNAL        1     16       Potential.
FT   CHAIN        17    566       Potential.
FT                                /FTId=PRO_5000456093.
FT   CHAIN        17    345       HA1.
FT                                /FTId=PRO_5000456094.
FT   CHAIN       346    566       HA2.
FT                                /FTId=PRO_5000456095.
SQ   SEQUENCE   566 AA;  63593 MW;  D3585FC63C8AA1F1 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 DIKIDLWSYN AELLVALENQ HTIDLTDSEM NKLFERTKKQ LRENAEDMGN
     GCFKIYHKCD NACIGSIRNG TYDHDVYRDE ALNNRFQIKG VELKSGYKDW ILWISFAISC
     FLLCVALLGF IMWACQKGNI RCNICI
//