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Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]

 HEMA_I34A1              Reviewed;         565 AA.
P03452; A4GXH4; Q20N38; Q83964; Q8JUU5;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
06-MAR-2007, sequence version 2.
22-NOV-2017, entry version 137.
RecName: Full=Hemagglutinin {ECO:0000255|HAMAP-Rule:MF_04072};
Contains:
RecName: Full=Hemagglutinin HA1 chain {ECO:0000255|HAMAP-Rule:MF_04072};
Contains:
RecName: Full=Hemagglutinin HA2 chain {ECO:0000255|HAMAP-Rule:MF_04072};
Flags: Precursor;
Name=HA {ECO:0000255|HAMAP-Rule:MF_04072};
Influenza A virus (strain A/Puerto Rico/8/1934 H1N1).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=211044;
NCBI_TaxID=8782; Aves.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=7278968; DOI=10.1038/292072a0;
Winter G., Fields S., Brownlee G.G.;
"Nucleotide sequence of the haemagglutinin gene of a human influenza
virus H1 subtype.";
Nature 292:72-75(1981).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=11779399; DOI=10.1098/rstb.2001.0979;
Schickli J.H., Flandorfer A., Nakaya T., Martinez-Sobrido L.,
Garcia-Sastre A., Palese P.;
"Plasmid-only rescue of influenza A virus vaccine candidates.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1965-1973(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND REVERSE GENETICS.
PubMed=15163504; DOI=10.1016/j.virusres.2004.02.028;
de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F.,
Osterhaus A.D.M.E., Fouchier R.A.M.;
"Efficient generation and growth of influenza virus A/PR/8/34 from
eight cDNA fragments.";
Virus Res. 103:155-161(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate EE12/E1;
Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V.,
Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H.,
Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y.,
Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
"The NIAID influenza genome sequencing project.";
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 18-343.
PubMed=6186384; DOI=10.1016/0092-8674(82)90135-0;
Caton A.J., Brownlee G.G., Yewdell J.W., Gerhard W.;
"The antigenic structure of the influenza virus A/PR/8/34
hemagglutinin (H1 subtype).";
Cell 31:417-427(1982).
-!- FUNCTION: Binds to sialic acid-containing receptors on the cell
surface, bringing about the attachment of the virus particle to
the cell. This attachment induces virion internalization either
through clathrin-dependent endocytosis or through clathrin- and
caveolin-independent pathway. Plays a major role in the
determination of host range restriction and virulence. Class I
viral fusion protein. Responsible for penetration of the virus
into the cell cytoplasm by mediating the fusion of the membrane of
the endocytosed virus particle with the endosomal membrane. Low pH
in endosomes induces an irreversible conformational change in HA2,
releasing the fusion hydrophobic peptide. Several trimers are
required to form a competent fusion pore. {ECO:0000255|HAMAP-
Rule:MF_04072}.
-!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2.
{ECO:0000255|HAMAP-Rule:MF_04072}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
Rule:MF_04072, ECO:0000305}; Single-pass type I membrane protein
{ECO:0000255|HAMAP-Rule:MF_04072, ECO:0000305}. Host apical cell
membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I
membrane protein {ECO:0000255|HAMAP-Rule:MF_04072, ECO:0000305}.
Note=Targeted to the apical plasma membrane in epithelial
polarized cells through a signal present in the transmembrane
domain. Associated with glycosphingolipid- and cholesterol-
enriched detergent-resistant lipid rafts. {ECO:0000255|HAMAP-
Rule:MF_04072}.
-!- PTM: Palmitoylated. {ECO:0000255|HAMAP-Rule:MF_04072}.
-!- PTM: In natural infection, inactive HA is matured into HA1 and HA2
outside the cell by one or more trypsin-like, arginine-specific
endoprotease secreted by the bronchial epithelial cells. One
identified protease that may be involved in this process is
secreted in lungs by Clara cells. {ECO:0000255|HAMAP-
Rule:MF_04072}.
-!- MISCELLANEOUS: Major glycoprotein, comprises over 80% of the
envelope proteins present in virus particle.
-!- MISCELLANEOUS: The extent of infection into host organism is
determined by HA. Influenza viruses bud from the apical surface of
polarized epithelial cells (e.g. bronchial epithelial cells) into
lumen of lungs and are therefore usually pneumotropic. The reason
is that HA is cleaved by tryptase clara which is restricted to
lungs. However, HAs of H5 and H7 pantropic avian viruses subtypes
can be cleaved by furin and subtilisin-type enzymes, allowing the
virus to grow in other organs than lungs.
-!- MISCELLANEOUS: The influenza A genome consist of 8 RNA segments.
Genetic variation of hemagglutinin and/or neuraminidase genes
results in the emergence of new influenza strains. The mechanism
of variation can be the result of point mutations or the result of
genetic reassortment between segments of two different strains.
{ECO:0000305}.
-!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
{ECO:0000255|HAMAP-Rule:MF_04072}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; V01088; CAA24272.1; -; Genomic_RNA.
EMBL; AF389118; AAM75158.1; -; Genomic_RNA.
EMBL; EF467821; ABO21709.1; -; Genomic_RNA.
EMBL; CY009444; ABD77675.1; -; Genomic_RNA.
EMBL; J02144; AAA43194.1; -; Genomic_RNA.
RefSeq; NP_040980.1; NC_002017.1.
PDB; 1RU7; X-ray; 2.30 A; A/C/E/G/I/K=18-338, B/D/F/H/J/L=344-503.
PDB; 1RVX; X-ray; 2.20 A; A/C/E/G/I/K=14-338, B/D/F/H/J/L=344-503.
PDB; 1RVZ; X-ray; 2.25 A; A/C/E/G/I/K=14-338, B/D/F/H/J/L=344-503.
PDBsum; 1RU7; -.
PDBsum; 1RVX; -.
PDBsum; 1RVZ; -.
ProteinModelPortal; P03452; -.
SMR; P03452; -.
IntAct; P03452; 35.
MINT; MINT-3375119; -.
BindingDB; P03452; -.
ChEMBL; CHEMBL1075313; -.
PRIDE; P03452; -.
GeneID; 956529; -.
KEGG; vg:956529; -.
KO; K19251; -.
OrthoDB; VOG090000DU; -.
Reactome; R-HSA-168255; Influenza Life Cycle.
Reactome; R-HSA-168275; Entry of Influenza Virion into Host Cell via Endocytosis.
Reactome; R-HSA-168288; Fusion of the Influenza Virion to the Host Cell Endosome.
Reactome; R-HSA-168298; Release.
Reactome; R-HSA-168302; Budding.
Reactome; R-HSA-168303; Packaging of Eight RNA Segments.
Reactome; R-HSA-168316; Assembly of Viral Components at the Budding Site.
Reactome; R-HSA-168336; Uncoating of the Influenza Virion.
Reactome; R-HSA-168874; Transport of HA trimer, NA tetramer and M2 tetramer from the endoplasmic reticulum to the Golgi Apparatus.
Reactome; R-HSA-192823; Viral mRNA Translation.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
EvolutionaryTrace; P03452; -.
PRO; PR:P03452; -.
Proteomes; UP000009255; Genome.
Proteomes; UP000109386; Genome.
Proteomes; UP000116373; Genome.
Proteomes; UP000170967; Genome.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0031904; C:endosome lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; TAS:Reactome.
GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; TAS:Reactome.
GO; GO:0019060; P:intracellular transport of viral protein in host cell; TAS:Reactome.
GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; TAS:Reactome.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0019061; P:uncoating of virus; TAS:Reactome.
GO; GO:0046761; P:viral budding from plasma membrane; IDA:UniProtKB.
GO; GO:0019072; P:viral genome packaging; TAS:Reactome.
GO; GO:0019082; P:viral protein processing; TAS:Reactome.
GO; GO:0019076; P:viral release from host cell; TAS:Reactome.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
GO; GO:0019068; P:virion assembly; TAS:Reactome.
GO; GO:0019062; P:virion attachment to host cell; TAS:Reactome.
Gene3D; 3.90.209.20; -; 1.
HAMAP; MF_04072; INFV_HEMA; 1.
InterPro; IPR008980; Capsid_hemagglutn.
InterPro; IPR013828; Hemagglutn_HA1_a/b_dom_sf.
InterPro; IPR000149; Hemagglutn_influenz_A.
InterPro; IPR001364; Hemagglutn_influenz_A/B.
Pfam; PF00509; Hemagglutinin; 1.
PRINTS; PR00330; HEMAGGLUTN1.
PRINTS; PR00329; HEMAGGLUTN12.
SUPFAM; SSF49818; SSF49818; 1.
1: Evidence at protein level;
3D-structure;
Clathrin- and caveolin-independent endocytosis of virus by host;
Clathrin-mediated endocytosis of virus by host; Complete proteome;
Disulfide bond; Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Hemagglutinin; Host cell membrane; Host membrane;
Host-virus interaction; Lipoprotein; Membrane; Palmitate;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Viral attachment to host cell; Viral envelope protein;
Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell.
SIGNAL 1 17 {ECO:0000255|HAMAP-Rule:MF_04072}.
CHAIN 18 565 Hemagglutinin. {ECO:0000255|HAMAP-
Rule:MF_04072}.
/FTId=PRO_0000440377.
CHAIN 18 342 Hemagglutinin HA1 chain.
{ECO:0000255|HAMAP-Rule:MF_04072}.
/FTId=PRO_0000039034.
CHAIN 344 565 Hemagglutinin HA2 chain.
{ECO:0000255|HAMAP-Rule:MF_04072}.
/FTId=PRO_0000039035.
TOPO_DOM 18 528 Extracellular. {ECO:0000255|HAMAP-
Rule:MF_04072}.
TRANSMEM 529 549 Helical. {ECO:0000255|HAMAP-
Rule:MF_04072}.
TOPO_DOM 550 565 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_04072}.
SITE 343 344 Cleavage; by host. {ECO:0000255|HAMAP-
Rule:MF_04072}.
LIPID 554 554 S-palmitoyl cysteine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
LIPID 561 561 S-palmitoyl cysteine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
LIPID 564 564 S-palmitoyl cysteine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 27 27 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 28 28 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 40 40 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 303 303 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 497 497 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 21 480 Interchain (between HA1 and HA2 chains).
{ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 59 291 {ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 72 84 {ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 107 152 {ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 295 319 {ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 487 491 {ECO:0000255|HAMAP-Rule:MF_04072}.
CONFLICT 10 10 C -> S (in Ref. 2; AAM75158).
{ECO:0000305}.
CONFLICT 146 146 N -> TK (in Ref. 1; CAA24272).
{ECO:0000305}.
CONFLICT 155 155 E -> A (in Ref. 1; CAA24272).
{ECO:0000305}.
CONFLICT 199 199 P -> S (in Ref. 1; CAA24272).
{ECO:0000305}.
CONFLICT 203 203 E -> D (in Ref. 1; CAA24272).
{ECO:0000305}.
CONFLICT 207 207 L -> I (in Ref. 1; CAA24272 and 2;
AAM75158). {ECO:0000305}.
CONFLICT 268 268 M -> R (in Ref. 1; CAA24272).
{ECO:0000305}.
CONFLICT 308 308 Y -> F (in Ref. 1; CAA24272).
{ECO:0000305}.
CONFLICT 337 337 I -> N (in Ref. 3; ABO21709).
{ECO:0000305}.
CONFLICT 397 397 T -> S (in Ref. 1; CAA24272).
{ECO:0000305}.
STRAND 19 25 {ECO:0000244|PDB:1RVX}.
STRAND 39 44 {ECO:0000244|PDB:1RVX}.
STRAND 46 48 {ECO:0000244|PDB:1RVX}.
STRAND 56 61 {ECO:0000244|PDB:1RVX}.
STRAND 67 70 {ECO:0000244|PDB:1RVX}.
HELIX 74 79 {ECO:0000244|PDB:1RVX}.
HELIX 82 87 {ECO:0000244|PDB:1RVX}.
STRAND 94 98 {ECO:0000244|PDB:1RVX}.
STRAND 107 110 {ECO:0000244|PDB:1RVX}.
HELIX 115 122 {ECO:0000244|PDB:1RVX}.
STRAND 125 134 {ECO:0000244|PDB:1RVX}.
TURN 136 138 {ECO:0000244|PDB:1RVX}.
STRAND 149 154 {ECO:0000244|PDB:1RVX}.
STRAND 157 159 {ECO:0000244|PDB:1RVX}.
STRAND 162 166 {ECO:0000244|PDB:1RVX}.
STRAND 170 172 {ECO:0000244|PDB:1RVX}.
STRAND 177 182 {ECO:0000244|PDB:1RVX}.
STRAND 185 197 {ECO:0000244|PDB:1RVX}.
HELIX 201 208 {ECO:0000244|PDB:1RVX}.
STRAND 215 218 {ECO:0000244|PDB:1RVX}.
STRAND 223 226 {ECO:0000244|PDB:1RVX}.
STRAND 242 250 {ECO:0000244|PDB:1RVX}.
STRAND 255 262 {ECO:0000244|PDB:1RVX}.
STRAND 264 275 {ECO:0000244|PDB:1RVX}.
STRAND 281 283 {ECO:0000244|PDB:1RVX}.
STRAND 288 297 {ECO:0000244|PDB:1RVX}.
STRAND 300 302 {ECO:0000244|PDB:1RVX}.
STRAND 307 309 {ECO:0000244|PDB:1RVX}.
STRAND 315 319 {ECO:0000244|PDB:1RVX}.
STRAND 329 331 {ECO:0000244|PDB:1RVX}.
TURN 350 352 {ECO:0000244|PDB:1RVX}.
STRAND 364 367 {ECO:0000244|PDB:1RVX}.
STRAND 376 379 {ECO:0000244|PDB:1RVZ}.
HELIX 381 401 {ECO:0000244|PDB:1RVX}.
STRAND 405 408 {ECO:0000244|PDB:1RVZ}.
HELIX 418 469 {ECO:0000244|PDB:1RVX}.
STRAND 472 475 {ECO:0000244|PDB:1RVX}.
STRAND 477 485 {ECO:0000244|PDB:1RVX}.
HELIX 491 496 {ECO:0000244|PDB:1RVX}.
SEQUENCE 565 AA; 63353 MW; 47F34821748F494E CRC64;
MKANLLVLLC ALAAADADTI CIGYHANNST DTVDTVLEKN VTVTHSVNLL EDSHNGKLCR
LKGIAPLQLG KCNIAGWLLG NPECDPLLPV RSWSYIVETP NSENGICYPG DFIDYEELRE
QLSSVSSFER FEIFPKESSW PNHNTNGVTA ACSHEGKSSF YRNLLWLTEK EGSYPKLKNS
YVNKKGKEVL VLWGIHHPPN SKEQQNLYQN ENAYVSVVTS NYNRRFTPEI AERPKVRDQA
GRMNYYWTLL KPGDTIIFEA NGNLIAPMYA FALSRGFGSG IITSNASMHE CNTKCQTPLG
AINSSLPYQN IHPVTIGECP KYVRSAKLRM VTGLRNIPSI QSRGLFGAIA GFIEGGWTGM
IDGWYGYHHQ NEQGSGYAAD QKSTQNAING ITNKVNTVIE KMNIQFTAVG KEFNKLEKRM
ENLNKKVDDG FLDIWTYNAE LLVLLENERT LDFHDSNVKN LYEKVKSQLK NNAKEIGNGC
FEFYHKCDNE CMESVRNGTY DYPKYSEESK LNREKVDGVK LESMGIYQIL AIYSTVASSL
VLLVSLGAIS FWMCSNGSLQ CRICI


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