HEMA_I02A6
ID HEMA_I02A6 Reviewed; 559 AA.
AC Q6DQ18;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 02-JUN-2021, entry version 88.
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; Fragment;
GN Name=HA {ECO:0000255|HAMAP-Rule:MF_04072};
OS Influenza A virus (strain A/Chicken/Hong Kong/YU22/2002 H5N1 genotype Z).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=284177;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9691; Panthera pardus (Leopard) (Felis pardus).
OH NCBI_TaxID=9694; Panthera tigris (Tiger).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15241415; DOI=10.1038/nature02746;
RA Li K.S., Guan Y., Wang J., Smith G.J.D., Xu K.M., Duan L., Rahardjo A.P.,
RA Puthavathana P., Buranathai C., Nguyen T.D., Estoepangestie A.T.S.,
RA Chaisingh A., Auewarakul P., Long H.T., Hanh N.T.H., Webby R.J.,
RA Poon L.L.M., Chen H., Shortridge K.F., Yuen K.Y., Webster R.G.,
RA Peiris J.S.M.;
RT "Genesis of a highly pathogenic and potentially pandemic H5N1 influenza
RT virus in eastern Asia.";
RL Nature 430:209-213(2004).
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.
CC -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
CC {ECO:0000255|HAMAP-Rule:MF_04072}.
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DR EMBL; AY651349; AAT73289.1; -; Genomic_RNA.
DR PDB; 5JW4; X-ray; 3.70 A; B/D/F/H/J/L=339-500.
DR PDB; 6CF5; X-ray; 2.04 A; B/D/F=339-512.
DR PDB; 6CFG; X-ray; 2.32 A; B=339-512.
DR PDB; 6E3H; X-ray; 2.90 A; B=339-512.
DR PDB; 6E7G; X-ray; 3.09 A; B/D/F=339-512.
DR PDB; 6E7H; X-ray; 3.30 A; B/D/F=339-512.
DR PDBsum; 5JW4; -.
DR PDBsum; 6CF5; -.
DR PDBsum; 6CFG; -.
DR PDBsum; 6E3H; -.
DR PDBsum; 6E7G; -.
DR PDBsum; 6E7H; -.
DR SMR; Q6DQ18; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
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 1: Evidence at protein level;
KW 3D-structure;
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; Transmembrane; Transmembrane helix;
KW 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 CHAIN 1..338
FT /note="Hemagglutinin HA1 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000440823"
FT CHAIN 339..559
FT /note="Hemagglutinin HA2 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000440824"
FT TOPO_DOM 1..523
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TOPO_DOM 545..559
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT SITE 338..339
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 549
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 556
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 559
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 12..475
FT /note="Interchain (between HA1 and HA2 chains)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 50..282
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 63..75
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 98..143
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 286..310
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 482..486
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT NON_TER 1
FT NON_TER 559
FT TURN 344..347
FT /evidence="ECO:0007829|PDB:6E7G"
FT STRAND 359..366
FT /evidence="ECO:0007829|PDB:6E7G"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:6E7G"
FT HELIX 376..395
FT /evidence="ECO:0007829|PDB:6E7G"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:6E7G"
FT HELIX 413..463
FT /evidence="ECO:0007829|PDB:6E7G"
FT STRAND 464..470
FT /evidence="ECO:0007829|PDB:6E7G"
FT STRAND 472..480
FT /evidence="ECO:0007829|PDB:6E7G"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:6E7G"
FT HELIX 488..492
FT /evidence="ECO:0007829|PDB:6E7G"
FT HELIX 497..506
FT /evidence="ECO:0007829|PDB:6E7G"
FT TURN 507..510
FT /evidence="ECO:0007829|PDB:6E7G"
SQ SEQUENCE 559 AA; 63212 MW; 13F1B3525F513B3C CRC64;
AIVSLVKSDQ ICIGYHANNS TEQVDTIMEK NVTVTHAQDI LEKTHNGKLC DLDGVKPLIL
RDCSVAGWLL GNPMCDEFIN VPEWSYIVEK ASPANDLCYP GDFNDYEELK HLLSGINHFD
KIHIIPKSSW SNHEASSWVS SACPYQGKSS FFRNVVWLIK KNSSYPTIKR SYDNTNQEDL
LVLWGIHHPN DAAEQTRFYQ NPTTYIGVGT STLNQRLVPK IATTSKVDGQ SGRMEFFWTI
LKPNDAINFE SNGNFIAPEY AYKIVKKGDS AIMKSELEYG NCNTKCQTPM GAINSSMPFH
NIHPLTIGEC PKYVKSNRLV LATGLRNSPQ RERRRKKRGL FGAIAGFIEG GWQGMVDGWY
GYHHSNEQGS GYAADKESTQ KAIDGVTNKV NSIIDKMNTQ FEAVGREFNN LERRIENLNK
KMEDGFLDVW TYNAELLVLM ENERTLDFHD SNVKNLYDKV RLQLRDNAKE LGNGCFEFYH
KCDNECMESV RNGTYDYPQY SEEARLKREE ISGVKLESIG TYQILSIYST VASSLALAIM
VAGLSLWMCS NGSLQCRIC
