ID   G8HIE5_9INFA            Unreviewed;       566 AA.
AC   G8HIE5;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   31-JAN-2018, entry version 36.
DE   RecName: Full=Hemagglutinin {ECO:0000256|HAMAP-Rule:MF_04072};
DE   Contains:
DE     RecName: Full=Hemagglutinin HA2 chain {ECO:0000256|HAMAP-Rule:MF_04072};
DE   Contains:
DE     RecName: Full=Hemagglutinin HA1 chain {ECO:0000256|HAMAP-Rule:MF_04072};
GN   Name=HA {ECO:0000256|HAMAP-Rule:MF_04072,
GN   ECO:0000313|EMBL:AEN68903.1};
OS   Influenza A virus (A/Cambodia/T028/2009(H1N1)).
OC   Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC   Orthomyxoviridae; Influenzavirus A.
OX   NCBI_TaxID=1076997 {ECO:0000313|EMBL:AEN68903.1};
RN   [1] {ECO:0000313|EMBL:AEN68903.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/Cambodia/T028/2009 {ECO:0000313|EMBL:AEN68903.1};
RA   Mardy S., Ly S., Heng S., Naughtin M., Vong S., Kitsutani P.,
RA   Vanra I., Rith S., Tarantola A., Ly S., Sar B., Nora C., Sokhal B.,
RA   Se Y., Timmermans A., Lon C., Barr I., Kelso A., Tyner S.,
RA   Saunders D., Ung S.A., Asgari N., Touch S., Buchy P.;
RT   "Characterization of human influenza virus circulation in Cambodia
RT   2006-2010.";
RL   Submitted (AUG-2011) 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. This attachment induces virion internalization either
CC       through clathrin-dependent endocytosis or through clathrin- and
CC       caveolin-independent pathway. Plays a major role in the
CC       determination of host range restriction and virulence. Class I
CC       viral fusion protein. Responsible for penetration of the virus
CC       into the cell cytoplasm by mediating the fusion of the membrane of
CC       the endocytosed virus particle with the endosomal membrane. Low pH
CC       in 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. {ECO:0000256|HAMAP-
CC       Rule:MF_04072, ECO:0000256|SAAS:SAAS00842802}.
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}.
CC   -!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2.
CC       {ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|RuleBase:RU003324,
CC       ECO:0000256|SAAS:SAAS00070616}.
CC   -!- SUBCELLULAR LOCATION: Host apical cell membrane
CC       {ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|SAAS:SAAS00554492};
CC       Single-pass type I membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_04072, ECO:0000256|SAAS:SAAS00554492}. Virion membrane
CC       {ECO:0000256|HAMAP-Rule:MF_04072}; Single-pass type I membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_04072}. Note=Targeted to the
CC       apical plasma membrane in epithelial polarized cells through a
CC       signal present in the transmembrane domain. Associated with
CC       glycosphingolipid- and cholesterol-enriched detergent-resistant
CC       lipid rafts. {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
CC       identified protease that may be involved in this process is
CC       secreted in lungs by Clara cells. {ECO:0000256|HAMAP-
CC       Rule:MF_04072}.
CC   -!- PTM: Palmitoylated. {ECO:0000256|HAMAP-Rule:MF_04072}.
CC   -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
CC       {ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|RuleBase:RU003324,
CC       ECO:0000256|SAAS:SAAS00963381}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04072}.
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DR   EMBL; JN588774; AEN68903.1; -; Viral_cRNA.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
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; 3.90.209.20; -; 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; SSF49818; SSF49818; 1.
PE   3: Inferred from homology;
KW   Clathrin- and caveolin-independent endocytosis of virus by host
KW   {ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|SAAS:SAAS00452788};
KW   Clathrin-mediated endocytosis of virus by host {ECO:0000256|HAMAP-
KW   Rule:MF_04072, ECO:0000256|SAAS:SAAS00453157};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04072,
KW   ECO:0000256|SAAS:SAAS00963411};
KW   Fusion of virus membrane with host endosomal membrane
KW   {ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|SAAS:SAAS00963419};
KW   Fusion of virus membrane with host membrane {ECO:0000256|HAMAP-
KW   Rule:MF_04072, ECO:0000256|SAAS:SAAS00963379};
KW   Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04072};
KW   Hemagglutinin {ECO:0000256|HAMAP-Rule:MF_04072,
KW   ECO:0000256|RuleBase:RU003324, ECO:0000256|SAAS:SAAS00963391};
KW   Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04072,
KW   ECO:0000256|SAAS:SAAS00963415};
KW   Host membrane {ECO:0000256|HAMAP-Rule:MF_04072,
KW   ECO:0000256|SAAS:SAAS00963389};
KW   Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04072,
KW   ECO:0000256|SAAS:SAAS00963361};
KW   Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04072};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_04072,
KW   ECO:0000256|SAAS:SAAS00963418};
KW   Palmitate {ECO:0000256|HAMAP-Rule:MF_04072};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_04072};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_04072,
KW   ECO:0000256|SAAS:SAAS00963395};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04072,
KW   ECO:0000256|SAAS:SAAS00963387};
KW   Viral attachment to host cell {ECO:0000256|HAMAP-Rule:MF_04072,
KW   ECO:0000256|SAAS:SAAS00963390};
KW   Viral envelope protein {ECO:0000256|HAMAP-Rule:MF_04072,
KW   ECO:0000256|RuleBase:RU003324, ECO:0000256|SAAS:SAAS00963382};
KW   Viral penetration into host cytoplasm {ECO:0000256|HAMAP-
KW   Rule:MF_04072, ECO:0000256|SAAS:SAAS00963370};
KW   Virion {ECO:0000256|HAMAP-Rule:MF_04072,
KW   ECO:0000256|SAAS:SAAS00070858};
KW   Virus endocytosis by host {ECO:0000256|HAMAP-Rule:MF_04072,
KW   ECO:0000256|SAAS:SAAS00963339};
KW   Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04072,
KW   ECO:0000256|SAAS:SAAS00963443}.
FT   TRANSMEM    531    554       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_04072}.
FT   COILED      382    402       {ECO:0000256|SAM:Coils}.
FT   SITE        344    345       Cleavage; by host. {ECO:0000256|HAMAP-
FT                                Rule:MF_04072}.
FT   LIPID       555    555       S-palmitoyl cysteine; by host.
FT                                {ECO:0000256|HAMAP-Rule:MF_04072}.
FT   LIPID       562    562       S-palmitoyl cysteine; by host.
FT                                {ECO:0000256|HAMAP-Rule:MF_04072}.
FT   LIPID       565    565       S-palmitoyl cysteine; by host.
FT                                {ECO:0000256|HAMAP-Rule:MF_04072}.
FT   DISULFID     72     84       {ECO:0000256|HAMAP-Rule:MF_04072}.
FT   DISULFID    296    320       {ECO:0000256|HAMAP-Rule:MF_04072}.
FT   DISULFID    488    492       {ECO:0000256|HAMAP-Rule:MF_04072}.
SQ   SEQUENCE   566 AA;  63222 MW;  99D3C9ADD706221D CRC64;
     MKAILVVLLY TFATANADTL CVGYHANNST DTVDTVLEKN VTVTHSVNLL EDKHNGKLCK
     LRGVAPLHLG KCNIAGWILG NPECESLSTA SSWSYIVETS SSDNGTCYPG DFIDYEELRE
     QLSSVSSFER FEIFPKTSSW PNHDSNKGVT AACPHAGAKS FYKNLIWLVK KGNSYPKLSK
     SYINDKGKEV LVLWGIHHPS TSADQQSLYQ NADAYVFVGT SRYSKKFKPE IAIRPKVRDQ
     EGRMNYYWTL VEPGDKITFE ATGNLVVPRY AFAMERNAGS GIIISDTPVH DCNTTCQTPK
     GAINTSLPFQ NIHPITIGKC PKYVKSTKLR LATGLRNVPS IQSRGLFGAI AGFIEGGWTG
     MVDGWYGYHH QNEQGSGYAA DLKSTQNAID EITNKVNSVI EKMNTQFTAV GKEFNHLEKR
     IENLNKKVDD GFLDIWTYNA ELLVLLENER TLDYHDSNVK NLYEKVRSQL KNNAKEIGNG
     CFEFYHKCDN TCMESVKNGT YDYPKYSEEA KLNREEIDGV KLESTRIYQI LAIYSTVASS
     LVLVVSLGAI SFWMCSNGSL QCRICI
//