HEMA_I01A1
ID HEMA_I01A1 Reviewed; 552 AA.
AC Q80A30;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 02-JUN-2021, entry version 87.
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/YU562/2001 H5N1 genotype B).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=196426;
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=12077307; DOI=10.1073/pnas.132268999;
RA Guan Y., Peiris J.S.M., Lipatov A.S., Ellis T.M., Dyrting K.C., Krauss S.,
RA Zhang L.J., Webster R.G., Shortridge K.F.;
RT "Emergence of multiple genotypes of H5N1 avian influenza viruses in Hong
RT Kong SAR.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:8950-8955(2002).
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; AF509017; AAO52860.1; -; Genomic_DNA.
DR PDB; 3S12; X-ray; 3.10 A; A=6-328, B=336-511.
DR PDB; 3S13; X-ray; 2.96 A; A=6-328, B=336-511.
DR PDBsum; 3S12; -.
DR PDBsum; 3S13; -.
DR SMR; Q80A30; -.
DR UniLectin; Q80A30; -.
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..335
FT /note="Hemagglutinin HA1 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000440802"
FT CHAIN 336..552
FT /note="Hemagglutinin HA2 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000440803"
FT TOPO_DOM 1..520
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TOPO_DOM 542..552
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT SITE 335..336
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 546
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 9..472
FT /note="Interchain (between HA1 and HA2 chains)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 47..279
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 60..72
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 95..140
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 283..307
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 479..483
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT NON_TER 1
FT NON_TER 552
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:3S12"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:3S12"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:3S12"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:3S13"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:3S13"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:3S13"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:3S13"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 229..238
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 243..264
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 276..284
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:3S12"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:3S12"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:3S12"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:3S12"
FT HELIX 373..392
FT /evidence="ECO:0007829|PDB:3S12"
FT HELIX 410..435
FT /evidence="ECO:0007829|PDB:3S13"
FT STRAND 464..467
FT /evidence="ECO:0007829|PDB:3S12"
FT STRAND 469..477
FT /evidence="ECO:0007829|PDB:3S12"
FT HELIX 481..488
FT /evidence="ECO:0007829|PDB:3S12"
FT HELIX 494..497
FT /evidence="ECO:0007829|PDB:3S12"
SQ SEQUENCE 552 AA; 62439 MW; C5A89469C7BAFBA7 CRC64;
SLVKSDQICI GYHANNSTEQ VDTIMEKNVT VTHAQDILEK THNGKLCDLD GVKPLILRDC
SVAGWLLGNP MCDEFINVPE WSYIVEKASP ANDLCYPGDF NDYEELKHLL SRINHFEKIQ
IIPKSSWSNH EASSGVSSAC PYLGKSSFFR NVVWLIKKNS AYPTIKRSYN NTNQEDLLVL
WGIHHPNDAA EQTKLYQNPT TYISVGTSTL NQRLVPKIAT RSKVNGQSGR MEFFWTILKP
NDAINFESNG NFIAPEYAYK IVKKGDSAIM KSELEYGNCN TKCQTPMGAI NSSMPFHNIH
PLTIGECPKY VKSNRLVLAT GLRNTPQRER RRKKRGLFGA IAGFIEGGWQ GMVDGWYGYH
HSNEQGSGYA ADKESTQKAI DGVTNKVNSI IDKMNTQFEA VGREFNNLER RIENLNKKME
DGFLDVWTYN AELLVLMENE RTLDFHDSNV KNLYDKVRLQ LRDNAKELGN GCFEFYHKCD
NECMESVKNG TYDYPQYSEE ARLNREEISG VKLESMGTYQ ILSIYSTVAS SLTLAIMVAG
LSLWMCSNGS LQ
