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

 HEMA_I68A6              Reviewed;         566 AA.
P03436; Q67095; Q84107;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
10-OCT-2018, entry version 122.
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/Northern Territory/60/1968 H3N2)
(Influenza A virus (strain NT60)) (Influenza A virus (strain
A/NT/60/1968 H3N2)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Alphainfluenzavirus.
NCBI_TaxID=384505;
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 [MRNA].
STRAIN=Subtype 29C;
PubMed=6253883; DOI=10.1093/nar/8.12.2561;
Both G.W., Sleigh M.J.;
"Complete nucleotide sequence of the haemagglutinin gene from a human
influenza virus of the Hong Kong subtype.";
Nucleic Acids Res. 8:2561-2575(1980).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 237-261.
STRAIN=Subtype 29C;
PubMed=388351; DOI=10.1093/nar/7.4.879;
Sleigh M.J., Both G.W., Brownlee G.G.;
"The influenza virus haemagglutinin gene: cloning and characterisation
of a double-stranded DNA copy.";
Nucleic Acids Res. 7:879-893(1979).
[3]
DISULFIDE BONDS.
PubMed=6768586; DOI=10.1016/0014-5793(80)80067-6;
Dopheide T.A., Ward C.W.;
"The disulphide bonds of a Hong Kong influenza virus hemagglutinin.";
FEBS Lett. 110:181-183(1980).
-!- 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, ECO:0000269|PubMed:6768586}.
-!- 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}.
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=CAA24291.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; V01103; CAA24290.1; ALT_TERM; mRNA.
EMBL; V01103; CAA24291.1; ALT_INIT; mRNA.
EMBL; M25434; AAA43163.1; -; Genomic_RNA.
PIR; A93705; HMIVH.
PDB; 5T6N; X-ray; 2.54 A; B/D/F=346-519.
PDB; 6BKM; X-ray; 2.20 A; B/D/F=346-519.
PDB; 6CEX; X-ray; 2.57 A; B/D/F=346-519.
PDBsum; 5T6N; -.
PDBsum; 6BKM; -.
PDBsum; 6CEX; -.
ProteinModelPortal; P03436; -.
SMR; P03436; -.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0046789; F:host cell surface receptor binding; IEA:UniProtKB-UniRule.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-UniRule.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
GO; GO:0046761; P:viral budding from plasma membrane; IEA:UniProtKB-UniRule.
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_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; 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_0000440417.
CHAIN 17 344 Hemagglutinin HA1 chain.
/FTId=PRO_0000039032.
CHAIN 346 566 Hemagglutinin HA2 chain.
{ECO:0000255|HAMAP-Rule:MF_04072}.
/FTId=PRO_0000039033.
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,
ECO:0000269|PubMed:6768586}.
DISULFID 68 293 {ECO:0000255|HAMAP-Rule:MF_04072,
ECO:0000269|PubMed:6768586}.
DISULFID 80 92 {ECO:0000255|HAMAP-Rule:MF_04072,
ECO:0000269|PubMed:6768586}.
DISULFID 113 155 {ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 297 321 {ECO:0000255|HAMAP-Rule:MF_04072,
ECO:0000269|PubMed:6768586}.
DISULFID 489 493 {ECO:0000255|HAMAP-Rule:MF_04072}.
TURN 352 354 {ECO:0000244|PDB:6BKM}.
STRAND 366 373 {ECO:0000244|PDB:6BKM}.
STRAND 376 381 {ECO:0000244|PDB:6BKM}.
HELIX 383 400 {ECO:0000244|PDB:6BKM}.
STRAND 406 409 {ECO:0000244|PDB:5T6N}.
HELIX 421 470 {ECO:0000244|PDB:6BKM}.
TURN 471 473 {ECO:0000244|PDB:6BKM}.
STRAND 474 477 {ECO:0000244|PDB:6BKM}.
STRAND 479 485 {ECO:0000244|PDB:6BKM}.
HELIX 491 498 {ECO:0000244|PDB:6BKM}.
HELIX 504 515 {ECO:0000244|PDB:6BKM}.
SEQUENCE 566 AA; 63488 MW; 9A187F6A5E383671 CRC64;
MKTIIALSYI FCLALGQDLP GNDNNTATLC LGHHAVPNGT LVKTITDDQI EVTNATELVQ
SSSTGKICNN PHRILDGIDC TLIDALLGDP HCDVFQNETW DLFVERSKAF SNCYPYDVPD
YASLRSLVAS SGTLEFITEG FTWTGVTQNG GSNACKRGPD SGFFSRLNWL TKSGSTYPVL
NVTMPNNDNF DKLYIWGVHH PSTNQEQTSL YVQASGRVTV STRRSQQTII PNIGSRPWVR
GQSSRISIYW TIVKPGDVLV INSNGNLIAP RGYFKMRTGK SSIMRSDAPI DTCISECITP
NGSIPNDKPF QNVNKITYGA CPKYVKQNTL KLATGMRNVP EKQTRGLFGA IAGFIENGWE
GMIDGWYGFR HQNSEGTGQA ADLKSTQAAI DQINGKLNRV IEKTNEKFHQ IEKEFSEVEG
RIQDLEKYVE DTKIDLWSYN AELLVALENQ HTIDLTDSEM NKLFEKTRRQ LRENAEDMGN
GCFKIYHKCD NACIESIRNG TYDHDVYRDE ALNNRFQIKG VELKSGYKDW ILWISFAISC
FLLCVVLLGF IMWACQRGNI RCNICI


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WP1119: Electron Transport Chain
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WP1626: Benzoate degradation via CoA ligation
WP1633: Bisphenol A degradation
WP1647: Fatty acid biosynthesis
WP1654: gamma-Hexachlorocyclohexane degradation
WP1665: Limonene and pinene degradation
WP1673: Naphthalene and anthracene degradation
WP1708: Terpenoid backbone biosynthesis
WP1996: Linoleate Biosynthesis
WP2347: vitamin B5 (pantothenate) and CoA biosynthesis Pathway
WP2434: very-long-chain-fatty-acid-biosynthesis
WP295: Electron Transport Chain
WP542: Electron Transport Chain
WP59: Electron Transport Chain
WP772: Electron Transport Chain
WP884: Electron Transport Chain

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[30886361] Antigenic drift originating from changes to the lateral surface of the neuraminidase head of influenza A virus.
[30885512] Efficacy of novel recombinant fowlpox vaccine against recent Mexican H7N3 highly pathogenic avian influenza virus.
[30882796] Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting.
[30882742] Integrated Safety Profile of a New Approved, Fully Liquid DTaP5-HB-IPV-Hib Vaccine.
[30880029] Fusion and hemagglutinin proteins of canine distemper virus promote osteoclast formation through NF-κB dependent and independent mechanisms.
[30879322] Isolation of H8N4 avian influenza virus from wild birds in Shanghai, China.
[30877453] Rescue and characterization of a recombinant HY12 bovine enterovirus carrying a foreign HA epitope in the 3A nonstructural protein.
[30875489] Local structural changes of the influenza A virus ribonucleoprotein complex by single mutations in the specific residues involved in efficient genome packaging.
[30872685] An Effective Neutralizing Antibody Against Influenza Virus H1N1 from Human B Cells.
[30869003] Predominance of influenza B/Yamagata lineage viruses in Bulgaria during the 2017/2018 season.
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