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

 Q4ZH98_9INFA            Unreviewed;       562 AA.
Q4ZH98;
07-JUN-2005, integrated into UniProtKB/TrEMBL.
07-JUN-2005, sequence version 1.
16-JAN-2019, entry version 85.
RecName: Full=Hemagglutinin {ECO:0000256|HAMAP-Rule:MF_04072};
Contains:
RecName: Full=Hemagglutinin HA2 chain {ECO:0000256|HAMAP-Rule:MF_04072};
Contains:
RecName: Full=Hemagglutinin HA1 chain {ECO:0000256|HAMAP-Rule:MF_04072};
Name=HA {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000313|EMBL:AAY28987.1};
Influenza A virus (A/Canada/720/2005(H2N2)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Alphainfluenzavirus.
NCBI_TaxID=327255 {ECO:0000313|EMBL:AAY28987.1, ECO:0000313|Proteomes:UP000116423};
[1] {ECO:0000313|EMBL:AAY28987.1, ECO:0000313|Proteomes:UP000116423}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=A/Canada/720/05 {ECO:0000313|EMBL:AAY28987.1};
Li Y., Taylor T., Bowness D., Normand S., Graham M., Benedictson T.,
Hart L., Tam T., Plummer F.;
"Sequence analysis of an influenza A/H2N2 virus, A/Canada/720/05,
linked to a laboratory proficiency testing survey (specimen VR1-05,
survey panel VR1A-2005) from the College of American Pathologists
(CAP).";
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
-!- 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:0000256|HAMAP-
Rule:MF_04072, ECO:0000256|SAAS:SAAS01039073}.
-!- 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.
{ECO:0000256|RuleBase:RU003324}.
-!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2.
{ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|RuleBase:RU003324,
ECO:0000256|SAAS:SAAS00070616}.
-!- SUBCELLULAR LOCATION: Host apical cell membrane
{ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|SAAS:SAAS00554492};
Single-pass type I membrane protein {ECO:0000256|HAMAP-
Rule:MF_04072, ECO:0000256|SAAS:SAAS00554492}. Virion membrane
{ECO:0000256|HAMAP-Rule:MF_04072}; Single-pass type I membrane
protein {ECO:0000256|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:0000256|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:0000256|HAMAP-
Rule:MF_04072}.
-!- PTM: Palmitoylated. {ECO:0000256|HAMAP-Rule:MF_04072}.
-!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
{ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|RuleBase:RU003324,
ECO:0000256|SAAS:SAAS00963381}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04072}.
-----------------------------------------------------------------------
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EMBL; DQ009917; AAY28987.1; -; Genomic_RNA.
Proteomes; UP000116423; Genome.
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.
3: Inferred from homology;
Clathrin- and caveolin-independent endocytosis of virus by host
{ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|SAAS:SAAS01039036};
Clathrin-mediated endocytosis of virus by host {ECO:0000256|HAMAP-
Rule:MF_04072, ECO:0000256|SAAS:SAAS01038958};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000116423};
Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963411};
Fusion of virus membrane with host endosomal membrane
{ECO:0000256|HAMAP-Rule:MF_04072, ECO:0000256|SAAS:SAAS00963419};
Fusion of virus membrane with host membrane {ECO:0000256|HAMAP-
Rule:MF_04072, ECO:0000256|SAAS:SAAS00963419};
Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04072};
Hemagglutinin {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|RuleBase:RU003324, ECO:0000256|SAAS:SAAS00963391};
Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963415};
Host membrane {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963415};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963390};
Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04072};
Membrane {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963387, ECO:0000256|SAAS:SAAS00963415};
Palmitate {ECO:0000256|HAMAP-Rule:MF_04072};
Signal {ECO:0000256|HAMAP-Rule:MF_04072};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963387};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963387};
Viral attachment to host cell {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963390};
Viral envelope protein {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|RuleBase:RU003324, ECO:0000256|SAAS:SAAS00963382};
Viral penetration into host cytoplasm {ECO:0000256|HAMAP-
Rule:MF_04072, ECO:0000256|SAAS:SAAS00963419,
ECO:0000256|SAAS:SAAS01038958, ECO:0000256|SAAS:SAAS01039036};
Virion {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|RuleBase:RU003324, ECO:0000256|SAAS:SAAS00963382,
ECO:0000256|SAAS:SAAS00963390};
Virus endocytosis by host {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS01038958, ECO:0000256|SAAS:SAAS01039036};
Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000256|SAAS:SAAS00963390, ECO:0000256|SAAS:SAAS00963419,
ECO:0000256|SAAS:SAAS01038958, ECO:0000256|SAAS:SAAS01039036}.
TRANSMEM 527 550 Helical. {ECO:0000256|HAMAP-
Rule:MF_04072}.
COILED 396 430 {ECO:0000256|SAM:Coils}.
SITE 340 341 Cleavage; by host. {ECO:0000256|HAMAP-
Rule:MF_04072}.
LIPID 551 551 S-palmitoyl cysteine; by host.
{ECO:0000256|HAMAP-Rule:MF_04072}.
LIPID 558 558 S-palmitoyl cysteine; by host.
{ECO:0000256|HAMAP-Rule:MF_04072}.
LIPID 561 561 S-palmitoyl cysteine; by host.
{ECO:0000256|HAMAP-Rule:MF_04072}.
DISULFID 70 82 {ECO:0000256|HAMAP-Rule:MF_04072}.
DISULFID 292 316 {ECO:0000256|HAMAP-Rule:MF_04072}.
DISULFID 484 488 {ECO:0000256|HAMAP-Rule:MF_04072}.
SEQUENCE 562 AA; 63119 MW; 1B672DD06B3436A0 CRC64;
MAIIYLILLF TAVRGDQICI GYHANNSTEK VDTILERNVT VTHAKDILEK THNGKLCKLN
GIPPLELGDC SIAGWLLGNP ECDRLLSVPE WSYIMEKENP RDGLCYPGSF NDYEELKHLL
SSVKHFEKVK ILPKDRWTQH TTTGGSRACA VSGNPSFFRN MVWLTKKGSN YPVAQGSYNN
TSGEQMLIIW GVHHPNDETE QRTLYQNVGT YVSVGTSTLN KRSTPEIATR PKVNGQGGRM
EFSWTLLDMW DTINFESTGN LIAPEYGFKI SKRGSSGIMK TEGTLENCET KCQTPLGAIN
TTLPFHNVHP LTIGECPKYV KSEKLVLATG LRNVPQIESR GLFGAIAGFI EGGWQGMVDG
WYGYHHSNDQ GSGYAADKES TQKAFDGITN KVNSVIEKMN TQFEAVGKEF SNLERRLENL
NKKMEDGFLD VWTYNAELLV LMENERTLDF HDSNVKNLYD KVRMQLRDNV KELGNGCFEF
YHKCDDECMN SVKNGTYDYP KYEEESKLNR NEIKGVKLSS MGVYQILAIY ATVAGSLSLA
IMMAGISFWM CSNGSLQCRI CI


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Pathways :
WP1002: Electron Transport Chain
WP111: Electron Transport Chain
WP1119: Electron Transport Chain
WP1339: Electron Transport Chain
WP1502: Mitochondrial biogenesis
WP1614: 1- and 2-Methylnaphthalene degradation
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

Related Genes :
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]
[HA] Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]

Bibliography :
[30894620] Epitope mapping of diverse influenza Hemagglutinin drug candidates using HDX-MS.
[30889726] Fabrication of electrochemical biosensor consisted of multi-functional DNA structure/porous au nanoparticle for avian influenza virus (H5N1) in chicken serum.
[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.
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