HEMA_I96A0
ID HEMA_I96A0 Reviewed; 568 AA.
AC Q9Q0U6; Q9WNX2;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 02-JUN-2021, entry version 121.
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/Goose/Guangdong/1/1996 H5N1 genotype Gs/Gd).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=93838;
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=10484749; DOI=10.1006/viro.1999.9820;
RA Xu X., Subbarao K., Cox N.J., Guo Y.;
RT "Genetic characterization of the pathogenic influenza
RT A/Goose/Guangdong/1/96 (H5N1) virus: similarity of its hemagglutinin gene
RT to those of H5N1 viruses from the 1997 outbreaks in Hong Kong.";
RL Virology 261:15-19(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen H., Yu K., Bu Z.;
RT "Molecular analysis of hemagglutinin gene of a goose origin highly
RT pathogenic avian influenza virus.";
RL Zhongguo Nong Ye Ke Xue 32:87-92(1999).
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; AF144305; AAD51927.1; -; Genomic_RNA.
DR EMBL; AF148678; AAD37782.1; -; mRNA.
DR RefSeq; YP_308669.1; NC_007362.1.
DR PDB; 3S11; X-ray; 2.50 A; A/C/E=17-339.
DR PDB; 4MHH; X-ray; 3.56 A; A/C/E=17-346.
DR PDB; 4MHI; X-ray; 2.60 A; A/C/E/G/I/K/M/O/Q=17-346, B/D/F/H/J/L/N/P/R=347-521.
DR PDB; 4MHJ; X-ray; 6.98 A; A/C/G/M/O/S=17-346, B/D/I/N/P/U=347-521.
DR PDBsum; 3S11; -.
DR PDBsum; 4MHH; -.
DR PDBsum; 4MHI; -.
DR PDBsum; 4MHJ; -.
DR SMR; Q9Q0U6; -.
DR UniLectin; Q9Q0U6; -.
DR ABCD; Q9Q0U6; 2 sequenced antibodies.
DR GeneID; 3654620; -.
DR KEGG; vg:3654620; -.
DR Proteomes; UP000131152; 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 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; 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..16
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CHAIN 17..568
FT /note="Hemagglutinin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000440536"
FT CHAIN 17..345
FT /note="Hemagglutinin HA1 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000440537"
FT CHAIN 347..568
FT /note="Hemagglutinin HA2 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000280186"
FT TOPO_DOM 17..531
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TOPO_DOM 553..568
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT SITE 346..347
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 557
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 564
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 567
FT /note="S-palmitoyl cysteine; 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 27
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 20..483
FT /note="Interchain (between HA1 and HA2 chains)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 58..290
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 71..83
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 106..151
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 294..318
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 490..494
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CONFLICT 3
FT /note="K -> R (in Ref. 2; AAD37782)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="K -> P (in Ref. 2; AAD37782)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="D -> N (in Ref. 2; AAD37782)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="N -> H (in Ref. 2; AAD37782)"
FT /evidence="ECO:0000305"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:3S11"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:3S11"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3S11"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:3S11"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 188..196
FT /evidence="ECO:0007829|PDB:3S11"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 254..266
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 268..275
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 287..296
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:3S11"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:3S11"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:4MHI"
FT STRAND 367..374
FT /evidence="ECO:0007829|PDB:4MHI"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:4MHI"
FT HELIX 384..404
FT /evidence="ECO:0007829|PDB:4MHI"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:4MHI"
FT HELIX 421..472
FT /evidence="ECO:0007829|PDB:4MHI"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:4MHI"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:4MHI"
FT STRAND 480..488
FT /evidence="ECO:0007829|PDB:4MHI"
FT HELIX 492..499
FT /evidence="ECO:0007829|PDB:4MHI"
FT HELIX 505..517
FT /evidence="ECO:0007829|PDB:4MHI"
SQ SEQUENCE 568 AA; 64257 MW; FBCD8D114879E52A CRC64;
MEKIVLLLAI VSLVKSDQIC IGYHANNSTE QVDTIMEKNV TVTHAQDILE KTHNGKLCDL
NGVKPLILRD CSVAGWLLGN PMCDEFINVP EWSYIVEKAS PANDLCYPGD FNDYEELKHL
LSRTNHFEKI QIIPKSSWSN HDASSGVSSA CPYHGRSSFF RNVVWLIKKN SAYPTIKRSY
NNTNQEDLLV LWGIHHPNDA AEQTKLYQNP TTYISVGTST LNQRLVPEIA TRPKVNGQSG
RMEFFWTILK PNDAINFESN GNFIAPEYAY KIVKKGDSAI MKSELEYGNC NTKCQTPMGA
INSSMPFHNI HPLTIGECPK YVKSNRLVLA TGLRNTPQRE RRRKKRGLFG AIAGFIEGGW
QGMVDGWYGY HHSNEQGSGY AADKESTQKA IDGVTNKVNS IIDKMNTQFE AVGREFNNLE
RRIENLNKQM EDGFLDVWTY NAELLVLMEN ERTLDFHDSN VKNLYDKVRL QLRDNAKELG
NGCFEFYHKC DNECMESVKN GTYDYPQYSE EARLNREEIS GVKLESMGTY QILSIYSTVA
SSLALAIMVA GLSLWMCSNG SLQCRICI
