ID   HEMA_IACKS              Reviewed;         564 AA.
AC   P09345;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   09-JAN-2007, entry version 51.
DE   Hemagglutinin precursor [Contains: Hemagglutinin HA1 chain;
DE   Hemagglutinin HA2 chain].
GN   Name=HA;
OS   Influenza A virus (strain A/Chicken/Scotland/1959 H5N1).
OC   Viruses; ssRNA negative-strand viruses; Orthomyxoviridae;
OC   Influenzavirus A.
OX   NCBI_TaxID=173721;
OH   NCBI_TaxID=8830; Anatidae (waterfowl).
OH   NCBI_TaxID=9685; Felis silvestris catus (Cat).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9691; Panthera pardus (Leopard).
OH   NCBI_TaxID=9694; Panthera tigris (Tiger).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   MEDLINE=88234030; PubMed=3375087;
RA   De B.K., Brownlee G.G., Kendal A.P., Shaw M.W.;
RT   "Complete sequence of a cDNA clone of the hemagglutinin gene of
RT   influenza A/Chicken/Scotland/59 (H5N1) virus: comparison with
RT   contemporary North American and European strains.";
RL   Nucleic Acids Res. 16:4181-4182(1988).
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.
CC   -!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; apical cell membrane; single-
CC       pass type I membrane protein. Note=Targeted to the apical plasma
CC       membrane in epithelial polarized cells through a signal present in
CC       the transmembrane domain. Associated with glycosphingolipid- and
CC       cholesterol-enriched detergent-resistant lipid rafts.
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       tryptase Clara.
CC   -!- PTM: Palmitoylated (By similarity).
CC   -!- MISCELLANEOUS: Major glycoprotein, comprises over 80% of the
CC       envelope proteins present in virus particle.
CC   -!- MISCELLANEOUS: The extent of infection into host organism is
CC       determined by HA. Influenza viruses bud from the apical surface of
CC       polarized epithelial cells (e.g. bronchial epithelial cells) into
CC       lumen of lungs and are therefore usually pneumotropic. The reason
CC       is that HA is cleaved by tryptase clara which is restricted to
CC       lungs. However, HAs of H5 and H7 pantropic avian viruses subtypes
CC       can be cleaved by furin and subtilisin-type enzymes, allowing the
CC       virus to grow in other organs than lungs.
CC   -!- MISCELLANEOUS: The influenza A genome consist of 8 RNA segments.
CC       Genetic variation of hemagglutinin and/or neuraminidase genes
CC       results in the emergence of new influenza strains. The mechanism
CC       of variation can be the result of point mutations or the result of
CC       genetic reassortment between segments of two different strains.
CC   -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
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DR   EMBL; X07826; CAA30680.1; -; Genomic_RNA.
DR   EMBL; X07869; CAA30719.1; -; mRNA.
DR   HSSP; Q9DLP3; 1JSM.
DR   SMR; P09345; 17-337.
DR   InterPro; IPR008980; Capsid_haemagglutn.
DR   InterPro; IPR013827; Haemagglutn_HA1_b-ribbon.
DR   InterPro; IPR000149; Haemagglutn_influenz_HA1.
DR   InterPro; IPR001364; Haemagglutn_influenz_HA1/HA2.
DR   InterPro; IPR013829; Haemagglutn_stalk.
DR   Pfam; PF00509; Hemagglutinin; 1.
DR   PRINTS; PR00330; HEMAGGLUTN1.
DR   PRINTS; PR00329; HEMAGGLUTN12.
DR   ProDom; PD000225; Hemagglutn; 1.
KW   Envelope protein; Fusion protein; Glycoprotein; Hemagglutinin;
KW   Lipoprotein; Membrane; Palmitate; Signal; Transmembrane;
KW   Virion protein.
FT   SIGNAL        1     16
FT   CHAIN        17    338       Hemagglutinin HA1 chain.
FT                                /FTId=PRO_0000038899.
FT   CHAIN       343    564       Hemagglutinin HA2 chain.
FT                                /FTId=PRO_0000038900.
FT   TOPO_DOM     17    527       Extracellular (Potential).
FT   TRANSMEM    528    548       Potential.
FT   TOPO_DOM    549    564       Cytoplasmic (Potential).
FT   LIPID       553    553       S-palmitoyl cysteine; by host (By
FT                                similarity).
FT   LIPID       560    560       S-palmitoyl cysteine; by host (By
FT                                similarity).
FT   LIPID       563    563       S-palmitoyl cysteine; by host (By
FT                                similarity).
FT   CARBOHYD     26     26       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     39     39       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    170    170       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    181    181       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    302    302       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    496    496       N-linked (GlcNAc...) (Potential).
FT   DISULFID     20    479       Interchain (between HA1 and HA2 chains)
FT                                (By similarity).
FT   DISULFID     58    290       By similarity.
FT   DISULFID     71     83       By similarity.
FT   DISULFID    106    151       By similarity.
FT   DISULFID    294    318       By similarity.
FT   DISULFID    486    490       By similarity.
SQ   SEQUENCE   564 AA;  63861 MW;  5AF409EEBF965ADD CRC64;
     MERIVLLLAI VSLVKSDQIC IGYHANKSTK QVDTIMEKNV TVTHAQDILE RTHNGKLCSL
     NGVKPLILRD CSVAGWLLGN PMCDEFLNLP EWLYIVEKDN PINSLCYPGD FNDYEELKYL
     LSSTNHFEKI RIIPRSSWSN HDASSGVSSA CPYIGRSSFL RNVVWLIKKN NTYPTIKRSY
     NNTNQEDLLI LWGIHHPNDA AEQTKLYQNP TTYVSVGTST LNQRSIPEIA TRPKVNGQSG
     RMEFFWTILK PNDAINFESN GNFIAPRYAY KIVKKGDSAI MKSGLAYGNC DTKCQTPVGE
     INSSMPFHNI HPHTIGECPK YVKSDRLVLA TGLRNVPQRK KRGLFGAIAG FIEGGWQGMV
     DGWYGYHHSN EQGSGYAADK ESTQKAIDGI TNKVNSIIDK MNTRFEAVGK EFNNLERRVE
     NLNKKMEDGF LDVWTYNVEL LVLMENERTL DFHDSNVNNL YDKVRLQLKD NARELGNGCF
     EFYHKCDNEC MESVRNGTYD YPQYSEEARL NREEISGVKL ESMGVYQILS IYSTVASSLA
     LAIMIAGLSF WMCSNGSLQC RICI
//