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HEMA_I68A5
ID   HEMA_I68A5              Reviewed;         562 AA.
AC   Q67143;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 118.
DE   RecName: Full=Hemagglutinin {ECO:0000255|HAMAP-Rule:MF_04072};
DE   Contains:
DE     RecName: Full=Hemagglutinin HA1 chain {ECO:0000255|HAMAP-Rule:MF_04072};
DE   Contains:
DE     RecName: Full=Hemagglutinin HA2 chain {ECO:0000255|HAMAP-Rule:MF_04072};
DE   Flags: Precursor;
GN   Name=HA {ECO:0000255|HAMAP-Rule:MF_04072};
OS   Influenza A virus (strain A/Korea/426/1968 H2N2).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=488241;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=7684877; DOI=10.1006/viro.1993.1319;
RA   Schafer J.R., Kawaoka Y., Bean W.J., Suss J., Senne D., Webster R.G.;
RT   "Origin of the pandemic 1957 H2 influenza A virus and the persistence of
RT   its possible progenitors in the avian reservoir.";
RL   Virology 194:781-788(1993).
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:0000255|HAMAP-Rule:MF_04072}.
CC   -!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2. {ECO:0000255|HAMAP-
CC       Rule:MF_04072}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_04072}. Host apical cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|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:0000255|HAMAP-Rule:MF_04072}.
CC   -!- PTM: Palmitoylated. {ECO:0000255|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:0000255|HAMAP-Rule:MF_04072}.
CC   -!- MISCELLANEOUS: Major glycoprotein, comprises over 80% of the envelope
CC       proteins present in virus particle.
CC   -!- MISCELLANEOUS: The extent of infection into host organism is determined
CC       by HA. Influenza viruses bud from the apical surface of polarized
CC       epithelial cells (e.g. bronchial epithelial cells) into lumen of lungs
CC       and are therefore usually pneumotropic. The reason is that HA is
CC       cleaved by tryptase clara which is restricted to lungs. However, HAs of
CC       H5 and H7 pantropic avian viruses subtypes can be cleaved by furin and
CC       subtilisin-type enzymes, allowing the virus to grow in other organs
CC       than lungs.
CC   -!- MISCELLANEOUS: The influenza A genome consist of 8 RNA segments.
CC       Genetic variation of hemagglutinin and/or neuraminidase genes results
CC       in the emergence of new influenza strains. The mechanism of variation
CC       can be the result of point mutations or the result of genetic
CC       reassortment between segments of two different strains. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
CC       {ECO:0000255|HAMAP-Rule:MF_04072}.
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DR   EMBL; L11133; AAA43247.1; -; Genomic_RNA.
DR   RefSeq; YP_308850.1; NC_007374.1.
DR   SMR; Q67143; -.
DR   GeneID; 3655103; -.
DR   KEGG; vg:3655103; -.
DR   PRO; PR:Q67143; -.
DR   Proteomes; UP000200640; Genome.
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   Clathrin-mediated endocytosis of virus by host; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein; Hemagglutinin;
KW   Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW   Membrane; Palmitate; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW   Virus entry into host cell.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CHAIN           16..562
FT                   /note="Hemagglutinin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT                   /id="PRO_0000440416"
FT   CHAIN           16..339
FT                   /note="Hemagglutinin HA1 chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT                   /id="PRO_0000280195"
FT   CHAIN           341..562
FT                   /note="Hemagglutinin HA2 chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT                   /id="PRO_0000280196"
FT   TOPO_DOM        16..525
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   TRANSMEM        526..546
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   TOPO_DOM        547..562
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   SITE            340..341
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   LIPID           551
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   LIPID           558
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   LIPID           561
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        300
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   CARBOHYD        494
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        19..477
FT                   /note="Interchain (between HA1 and HA2 chains)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        57..288
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        70..82
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        105..149
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        292..316
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT   DISULFID        484..488
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
SQ   SEQUENCE   562 AA;  63295 MW;  427AFDA3BF5E6696 CRC64;
     MAIIYLILLF TAVRGDQICI GYHANNSTEK VDTILERNVT VTHAKDILEK THNGKLCKLN
     GIPPLELGDC SIAGWLLGNP ECDRLLSVPE WSYIMEKENP RYSLCYPGSF NDYEELKHLL
     SSVKHFEKVK ILPKDRWTQH TTTGGSWACA VSGKPSFFRN MVWLTRKGSN YPVAKGSYNN
     TSGEQMLIIW GVHHPNDEAE QRALYQNVGT YVSVATSTLY KRSIPEIAAR PKVNGLGRRM
     EFSWTLLDMW DTINFESTGN LVAPEYGFKI SKRGSSGIMK TEGTLENCET KCQTPLGAIN
     TTLPFHNVHP LTIGECPKYV KSEKLVLATG LRNVPQIESR GLFGAIAGFI EGGWQGMVDG
     WYGYHHSNDQ GSGYAADKES TQKAFNGITN KVNSVIEKMN TQFEAVGKEF SNLEKRLENL
     NKKMEDGFLD VWTYNAELLV LMENERTLDF HDSNVKNLYD KVRMQLRDNV KELGNGCFEF
     YHKCDNECMD SVKNGTYDYP KYEEESKLNR NEIKGVKLSS MGVYQILAIY ATVAGSLSLA
     IMMAGISFWM CSNGSLQCRI CI
 
 
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