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

 HEMA_I68A0              Reviewed;         566 AA.
P03437; A0PC85; Q67132;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
07-JUN-2017, entry version 136.
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/Aichi/2/1968 H3N2).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=387139;
NCBI_TaxID=8782; Aves.
NCBI_TaxID=9721; Cetacea (whales).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9709; Phocidae (true seals).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=7402351; DOI=10.1038/286771a0;
Verhoeyen M., Fang R., Jou W.M., Devos R., Huylebroeck D., Saman E.,
Fiers W.;
"Antigenic drift between the haemagglutinin of the Hong Kong influenza
strains A/Aichi/2/68 and A/Victoria/3/75.";
Nature 286:771-776(1980).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Min J.W., Verhoeyen M., Fang R.-X., Devos R., Huylebroeck D.,
Fiers W.;
"Shift and drift in influenza viruses.";
(In) Carlile M.J., Collins J.F., Moseley B.E.B. (eds.);
Symposium of the Society for General Microbiology, pp.285-311,
Cambridge University Press, New York (1981).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=15331693; DOI=10.1128/JVI.78.18.9605-9611.2004;
Abe Y., Takashita E., Sugawara K., Matsuzaki Y., Muraki Y., Hongo S.;
"Effect of the addition of oligosaccharides on the biological
activities and antigenicity of influenza A/H3N2 virus hemagglutinin.";
J. Virol. 78:9605-9611(2004).
[4]
CLEAVAGE.
PubMed=9089405; DOI=10.1093/oxfordjournals.jbchem.a021588;
Beppu Y., Imamura Y., Tashiro M., Towatari T., Ariga H., Kido H.;
"Human mucus protease inhibitor in airway fluids is a potential
defensive compound against infection with influenza A and Sendai
viruses.";
J. Biochem. 121:309-316(1997).
[5]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=7464906; DOI=10.1038/289366a0;
Wilson I.A., Skehel J.J., Wiley D.C.;
"Structure of the haemagglutinin membrane glycoprotein of influenza
virus at 3-A resolution.";
Nature 289:366-373(1981).
[6]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
PubMed=3374584; DOI=10.1038/333426a0;
Weis W.I., Brown J.H., Cusack S.C., Paulson J.C., Skehel J.J.,
Wiley D.C.;
"Structure of the influenza virus haemagglutinin complexed with its
receptor, sialic acid.";
Nature 333:426-431(1988).
[7]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF A MUTANT WITH GLY-457.
PubMed=2295311;
Weis W.I., Cusack S.C., Brown J.H., Daniels R.S., Skehel J.J.,
Wiley D.C.;
"The structure of a membrane fusion mutant of the influenza virus
haemagglutinin.";
EMBO J. 9:17-24(1990).
[8]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
PubMed=2329580; DOI=10.1016/0022-2836(90)90234-D;
Weis W.I., Bruenger A.T., Skehel J.J., Wiley D.C.;
"Refinement of the influenza virus hemagglutinin by simulated
annealing.";
J. Mol. Biol. 212:737-761(1990).
[9]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=8072525; DOI=10.1038/371037a0;
Bullough P.A., Hughson F.M., Skehel J.J., Wiley D.C.;
"Structure of influenza haemagglutinin at the pH of membrane fusion.";
Nature 371:37-43(1994).
[10]
X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS).
PubMed=9461077; DOI=10.1038/nsb0298-119;
Fleury D., Wharton S.A., Skehel J.J., Knossow M., Bizebard T.;
"Antigen distortion allows influenza virus to escape neutralization.";
Nat. Struct. Biol. 5:119-123(1998).
-!- 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 of about
two third of the virus particles through clathrin-dependent
endocytosis and about one third through a 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.
-!- 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}; Single-pass type I membrane protein
{ECO:0000255|HAMAP-Rule:MF_04072}. Host apical cell membrane
{ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane
protein {ECO:0000255|HAMAP-Rule:MF_04072}. 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, ECO:0000269|PubMed:9089405}.
-!- 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}.
-----------------------------------------------------------------------
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EMBL; J02090; AAA43178.1; -; Genomic_RNA.
EMBL; V01085; CAA24269.1; -; Genomic_RNA.
EMBL; M55059; AAA43239.1; -; Genomic_RNA.
EMBL; AB284320; BAF37221.1; -; Genomic_RNA.
PIR; A93231; HMIVHA.
PDB; 1EO8; X-ray; 2.80 A; A=17-344, B=346-520.
PDB; 1FYT; X-ray; 2.60 A; C=322-334.
PDB; 1HA0; X-ray; 2.80 A; A=25-518.
PDB; 1HGG; X-ray; 2.90 A; A/C/E=17-344, B/D/F=346-520.
PDB; 1HTM; X-ray; 2.50 A; A/C/E=17-43, B/D/F=383-520.
PDB; 1J8H; X-ray; 2.40 A; C=322-334.
PDB; 1KEN; X-ray; 3.50 A; B/D/F=346-520.
PDB; 1KG0; X-ray; 2.65 A; D=322-334.
PDB; 1PYW; X-ray; 2.10 A; C=324-332.
PDB; 1QFU; X-ray; 2.80 A; B=346-520.
PDB; 1QU1; X-ray; 1.90 A; A/B/C/D/E/F=376-530.
PDB; 2HMG; X-ray; 3.00 A; A/C/E=17-344, B/D/F=346-520.
PDB; 2VIR; X-ray; 3.25 A; C=44-325.
PDB; 2VIS; X-ray; 3.25 A; C=44-325.
PDB; 2VIT; X-ray; 3.25 A; C=44-325.
PDB; 2VIU; X-ray; 2.50 A; A=17-344, B=346-520.
PDB; 2YPG; X-ray; 2.85 A; A/C/E=17-344, B/D/F=346-520.
PDB; 3EYM; X-ray; 2.80 A; A/C/E=25-345, B/D/F=346-517.
PDB; 3HMG; X-ray; 2.90 A; A/C/E=17-344, B/D/F=346-520.
PDB; 3S4S; X-ray; 2.40 A; C/F=322-334.
PDB; 3S5L; X-ray; 2.10 A; C/F=322-334.
PDB; 3VUN; X-ray; 3.00 A; A/C/E=17-345, B/D/F=346-520.
PDB; 4C56; X-ray; 2.90 A; F/L=322-334.
PDB; 4HMG; X-ray; 3.00 A; A/C/E=17-344, B/D/F=346-520.
PDB; 5HMG; X-ray; 3.20 A; A/C/E=17-344, B/D/F=346-520.
PDBsum; 1EO8; -.
PDBsum; 1FYT; -.
PDBsum; 1HA0; -.
PDBsum; 1HGG; -.
PDBsum; 1HTM; -.
PDBsum; 1J8H; -.
PDBsum; 1KEN; -.
PDBsum; 1KG0; -.
PDBsum; 1PYW; -.
PDBsum; 1QFU; -.
PDBsum; 1QU1; -.
PDBsum; 2HMG; -.
PDBsum; 2VIR; -.
PDBsum; 2VIS; -.
PDBsum; 2VIT; -.
PDBsum; 2VIU; -.
PDBsum; 2YPG; -.
PDBsum; 3EYM; -.
PDBsum; 3HMG; -.
PDBsum; 3S4S; -.
PDBsum; 3S5L; -.
PDBsum; 3VUN; -.
PDBsum; 4C56; -.
PDBsum; 4HMG; -.
PDBsum; 5HMG; -.
ProteinModelPortal; P03437; -.
SMR; P03437; -.
DIP; DIP-45342N; -.
IntAct; P03437; 1.
BindingDB; P03437; -.
ChEMBL; CHEMBL1932897; -.
EvolutionaryTrace; P03437; -.
Proteomes; UP000137932; Genome.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
Gene3D; 3.90.209.20; -; 1.
HAMAP; MF_04072; INFV_HEMA; 1.
InterPro; IPR008980; Capsid_hemagglutn.
InterPro; IPR013828; Hemagglutn_HA1_a/b_dom.
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; 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 16 {ECO:0000255|HAMAP-Rule:MF_04072}.
CHAIN 17 566 Hemagglutinin. {ECO:0000255|HAMAP-
Rule:MF_04072}.
/FTId=PRO_0000440411.
CHAIN 17 344 Hemagglutinin HA1 chain.
/FTId=PRO_0000038885.
CHAIN 346 566 Hemagglutinin HA2 chain.
{ECO:0000255|HAMAP-Rule:MF_04072}.
/FTId=PRO_0000038886.
TOPO_DOM 17 530 Extracellular. {ECO:0000255|HAMAP-
Rule:MF_04072}.
TRANSMEM 531 551 Helical. {ECO:0000255|HAMAP-
Rule:MF_04072}.
TOPO_DOM 552 566 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_04072}.
SITE 345 346 Cleavage; by host. {ECO:0000255|HAMAP-
Rule:MF_04072}.
LIPID 555 555 S-palmitoyl cysteine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
LIPID 562 562 S-palmitoyl cysteine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
LIPID 565 565 S-palmitoyl cysteine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 24 24 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 181 181 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 301 301 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 499 499 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 30 482 Interchain (between HA1 and HA2 chains).
{ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 68 293 {ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 80 92 {ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 113 155 {ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 297 321 {ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 489 493 {ECO:0000255|HAMAP-Rule:MF_04072}.
CONFLICT 14 14 A -> P (in Ref. 2; AAA43239).
{ECO:0000305}.
CONFLICT 15 15 L -> I (in Ref. 3; BAF37221).
{ECO:0000305}.
CONFLICT 160 160 G -> S (in Ref. 3; BAF37221).
{ECO:0000305}.
CONFLICT 198 198 I -> V (in Ref. 3; BAF37221).
{ECO:0000305}.
CONFLICT 240 240 R -> G (in Ref. 3; BAF37221).
{ECO:0000305}.
CONFLICT 477 477 E -> D (in Ref. 3; BAF37221).
{ECO:0000305}.
STRAND 27 35 {ECO:0000244|PDB:2VIU}.
STRAND 40 42 {ECO:0000244|PDB:2VIU}.
STRAND 50 53 {ECO:0000244|PDB:2VIU}.
STRAND 55 57 {ECO:0000244|PDB:2VIU}.
STRAND 65 72 {ECO:0000244|PDB:2VIU}.
STRAND 74 76 {ECO:0000244|PDB:2VIU}.
HELIX 82 87 {ECO:0000244|PDB:2VIU}.
HELIX 90 95 {ECO:0000244|PDB:2VIU}.
STRAND 101 105 {ECO:0000244|PDB:2VIU}.
HELIX 121 131 {ECO:0000244|PDB:2VIU}.
STRAND 136 138 {ECO:0000244|PDB:2VIU}.
TURN 144 146 {ECO:0000244|PDB:1HA0}.
STRAND 152 157 {ECO:0000244|PDB:2VIU}.
STRAND 160 162 {ECO:0000244|PDB:2VIU}.
STRAND 167 169 {ECO:0000244|PDB:2VIU}.
STRAND 171 173 {ECO:0000244|PDB:2VIU}.
STRAND 180 185 {ECO:0000244|PDB:2VIU}.
STRAND 188 190 {ECO:0000244|PDB:2VIU}.
STRAND 192 200 {ECO:0000244|PDB:2VIU}.
HELIX 204 211 {ECO:0000244|PDB:2VIU}.
STRAND 212 215 {ECO:0000244|PDB:2VIU}.
STRAND 217 221 {ECO:0000244|PDB:2VIU}.
STRAND 226 229 {ECO:0000244|PDB:2VIU}.
STRAND 245 253 {ECO:0000244|PDB:2VIU}.
STRAND 258 265 {ECO:0000244|PDB:2VIU}.
STRAND 267 270 {ECO:0000244|PDB:2VIU}.
STRAND 272 275 {ECO:0000244|PDB:2VIU}.
STRAND 282 285 {ECO:0000244|PDB:2VIU}.
STRAND 290 294 {ECO:0000244|PDB:2VIU}.
STRAND 296 299 {ECO:0000244|PDB:2VIU}.
STRAND 302 304 {ECO:0000244|PDB:2VIU}.
STRAND 307 311 {ECO:0000244|PDB:2VIU}.
STRAND 318 320 {ECO:0000244|PDB:2VIU}.
STRAND 331 333 {ECO:0000244|PDB:2VIU}.
STRAND 337 339 {ECO:0000244|PDB:1HA0}.
TURN 352 354 {ECO:0000244|PDB:2VIU}.
STRAND 366 373 {ECO:0000244|PDB:2VIU}.
STRAND 376 382 {ECO:0000244|PDB:2VIU}.
HELIX 383 449 {ECO:0000244|PDB:1QU1}.
STRAND 455 457 {ECO:0000244|PDB:1HTM}.
HELIX 458 470 {ECO:0000244|PDB:1QU1}.
HELIX 472 474 {ECO:0000244|PDB:2VIU}.
STRAND 475 479 {ECO:0000244|PDB:1QU1}.
STRAND 485 487 {ECO:0000244|PDB:1KEN}.
HELIX 491 499 {ECO:0000244|PDB:1QU1}.
HELIX 504 515 {ECO:0000244|PDB:2VIU}.
TURN 516 519 {ECO:0000244|PDB:1HGG}.
STRAND 524 526 {ECO:0000244|PDB:1QU1}.
SEQUENCE 566 AA; 63416 MW; E395659C23CAFECA CRC64;
MKTIIALSYI FCLALGQDLP GNDNSTATLC LGHHAVPNGT LVKTITDDQI EVTNATELVQ
SSSTGKICNN PHRILDGIDC TLIDALLGDP HCDVFQNETW DLFVERSKAF SNCYPYDVPD
YASLRSLVAS SGTLEFITEG FTWTGVTQNG GSNACKRGPG SGFFSRLNWL TKSGSTYPVL
NVTMPNNDNF DKLYIWGIHH PSTNQEQTSL YVQASGRVTV STRRSQQTII PNIGSRPWVR
GLSSRISIYW TIVKPGDVLV INSNGNLIAP RGYFKMRTGK SSIMRSDAPI DTCISECITP
NGSIPNDKPF QNVNKITYGA CPKYVKQNTL KLATGMRNVP EKQTRGLFGA IAGFIENGWE
GMIDGWYGFR HQNSEGTGQA ADLKSTQAAI DQINGKLNRV IEKTNEKFHQ IEKEFSEVEG
RIQDLEKYVE DTKIDLWSYN AELLVALENQ HTIDLTDSEM NKLFEKTRRQ LRENAEEMGN
GCFKIYHKCD NACIESIRNG TYDHDVYRDE ALNNRFQIKG VELKSGYKDW ILWISFAISC
FLLCVVLLGF IMWACQRGNI RCNICI


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