ID   G8HIE5_9INFA            Unreviewed;       566 AA.
AC   G8HIE5;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   07-APR-2021, entry version 49.
DE   RecName: Full=Hemagglutinin {ECO:0000256|HAMAP-Rule:MF_04072};
DE   Contains:
DE     RecName: Full=Hemagglutinin HA1 chain {ECO:0000256|HAMAP-Rule:MF_04072};
DE   Contains:
DE     RecName: Full=Hemagglutinin HA2 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; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
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., Vanra I.,
RA   Rith S., Tarantola A., Ly S., Sar B., Nora C., Sokhal B., Se Y.,
RA   Timmermans A., Lon C., Barr I., Kelso A., Tyner S., Saunders D., Ung S.A.,
RA   Asgari N., Touch S., Buchy P.;
RT   "Characterization of human influenza virus circulation in Cambodia 2006-
RT   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 the
CC       cell. This attachment induces virion internalization either through
CC       clathrin-dependent endocytosis or through clathrin- and caveolin-
CC       independent pathway. Plays a major role in the determination of host
CC       range restriction and virulence. Class I viral fusion protein.
CC       Responsible for penetration of the virus into the cell cytoplasm by
CC       mediating the fusion of the membrane of the endocytosed virus particle
CC       with the endosomal membrane. Low pH in endosomes induces an
CC       irreversible conformational change in HA2, releasing the fusion
CC       hydrophobic peptide. Several trimers are required to form a competent
CC       fusion pore. {ECO:0000256|HAMAP-Rule:MF_04072}.
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. {ECO:0000256|HAMAP-
CC       Rule:MF_04072, 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, ECO:0000256|HAMAP-Rule:MF_04072};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004310,
CC       ECO:0000256|HAMAP-Rule:MF_04072}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479}. Virion membrane {ECO:0000256|HAMAP-
CC       Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_04072}. Note=Targeted to the apical plasma membrane in
CC       epithelial polarized cells through a signal present in the
CC       transmembrane domain. Associated with glycosphingolipid- and
CC       cholesterol-enriched detergent-resistant lipid rafts.
CC       {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 identified
CC       protease that may be involved in this process is secreted in lungs by
CC       Clara cells. {ECO:0000256|HAMAP-Rule:MF_04072}.
CC   -!- PTM: Palmitoylated. {ECO:0000256|HAMAP-Rule:MF_04072}.
CC   -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
CC       {ECO:0000256|ARBA:ARBA00006321, ECO:0000256|HAMAP-Rule:MF_04072,
CC       ECO:0000256|RuleBase:RU003324}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_04072}.
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DR   EMBL; JN588774; AEN68903.1; -; Viral_cRNA.
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: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|ARBA:ARBA00023261, ECO:0000256|HAMAP-Rule:MF_04072};
KW   Clathrin-mediated endocytosis of virus by host
KW   {ECO:0000256|ARBA:ARBA00022570, ECO:0000256|HAMAP-Rule:MF_04072};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW   Rule:MF_04072};
KW   Fusion of virus membrane with host endosomal membrane
KW   {ECO:0000256|ARBA:ARBA00022510, ECO:0000256|HAMAP-Rule:MF_04072};
KW   Fusion of virus membrane with host membrane {ECO:0000256|ARBA:ARBA00022506,
KW   ECO:0000256|HAMAP-Rule:MF_04072};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|HAMAP-
KW   Rule:MF_04072};
KW   Hemagglutinin {ECO:0000256|ARBA:ARBA00022546, ECO:0000256|HAMAP-
KW   Rule:MF_04072};
KW   Host cell membrane {ECO:0000256|ARBA:ARBA00022511, ECO:0000256|HAMAP-
KW   Rule:MF_04072};
KW   Host membrane {ECO:0000256|ARBA:ARBA00022870, ECO:0000256|HAMAP-
KW   Rule:MF_04072};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, ECO:0000256|HAMAP-
KW   Rule:MF_04072};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW   Rule:MF_04072};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_04072};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_04072};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_04072};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_04072};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04072};
KW   Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804,
KW   ECO:0000256|HAMAP-Rule:MF_04072};
KW   Viral envelope protein {ECO:0000256|ARBA:ARBA00022879, ECO:0000256|HAMAP-
KW   Rule:MF_04072};
KW   Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595,
KW   ECO:0000256|HAMAP-Rule:MF_04072};
KW   Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04072};
KW   Virus endocytosis by host {ECO:0000256|ARBA:ARBA00022890,
KW   ECO:0000256|HAMAP-Rule:MF_04072};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296,
KW   ECO:0000256|HAMAP-Rule:MF_04072}.
FT   CHAIN           345..566
FT                   /note="Hemagglutinin HA2 chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT                   /id="PRO_5023560325"
FT   TRANSMEM        531..554
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT   COILED          382..402
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   SITE            344..345
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT   LIPID           555
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT   LIPID           562
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT   LIPID           565
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT   DISULFID        72..84
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT   DISULFID        296..320
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04072"
FT   DISULFID        488..492
FT                   /evidence="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
//