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

 HEMA_I63A2              Reviewed;         565 AA.
P15658; Q67097; Q67098; Q83987; Q83988;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 2.
07-JUN-2017, entry version 109.
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/Equine/Miami/1/1963 H3N8).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=387222;
NCBI_TaxID=8782; Aves.
NCBI_TaxID=9796; Equus caballus (Horse).
[1]
NUCLEOTIDE SEQUENCE.
PubMed=2705299; DOI=10.1016/0042-6822(89)90153-0;
Kawaoka Y., Bean W.J., Webster R.G.;
"Evolution of the hemagglutinin of equine H3 influenza viruses.";
Virology 169:283-292(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3973560; DOI=10.1099/0022-1317-66-3-457;
Daniels R.S., Skehel J.J., Wiley D.C.;
"Amino acid sequences of haemagglutinins of influenza viruses of the
H3 subtype isolated from horses.";
J. Gen. Virol. 66:457-464(1985).
-!- 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}.
-!- 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; M24719; AAA43105.1; ALT_SEQ; Genomic_RNA.
EMBL; M29257; AAA43164.1; -; Genomic_DNA.
ProteinModelPortal; P15658; -.
SMR; P15658; -.
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.
3: Inferred from homology;
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 17 565 Hemagglutinin. {ECO:0000255|HAMAP-
Rule:MF_04072}.
/FTId=PRO_0000440399.
CHAIN 17 343 Hemagglutinin HA1 chain.
/FTId=PRO_0000038986.
CHAIN 345 565 Hemagglutinin HA2 chain.
{ECO:0000255|HAMAP-Rule:MF_04072}.
/FTId=PRO_0000038987.
TOPO_DOM 17 529 Extracellular. {ECO:0000255|HAMAP-
Rule:MF_04072}.
TRANSMEM 530 550 Helical. {ECO:0000255|HAMAP-
Rule:MF_04072}.
TOPO_DOM 551 565 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_04072}.
SITE 344 345 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 23 23 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 37 37 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 180 180 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 300 300 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
CARBOHYD 498 498 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 29 481 Interchain (between HA1 and HA2 chains).
{ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 67 292 {ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 112 154 {ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 296 320 {ECO:0000255|HAMAP-Rule:MF_04072}.
DISULFID 488 492 {ECO:0000255|HAMAP-Rule:MF_04072}.
CONFLICT 13 15 WVH -> AAD (in Ref. 2; AAA43164).
{ECO:0000305}.
CONFLICT 72 73 RV -> SG (in Ref. 2; AAA43164).
{ECO:0000305}.
CONFLICT 173 173 E -> G (in Ref. 2; AAA43164).
{ECO:0000305}.
CONFLICT 293 293 V -> W (in Ref. 2; AAA43164).
{ECO:0000305}.
CONFLICT 377 377 L -> G (in Ref. 2; AAA43164).
{ECO:0000305}.
CONFLICT 380 380 G -> A (in Ref. 2; AAA43164).
{ECO:0000305}.
CONFLICT 400 400 I -> F (in Ref. 2; AAA43164).
{ECO:0000305}.
CONFLICT 555 555 Q -> E (in Ref. 2; AAA43164).
{ECO:0000305}.
SEQUENCE 565 AA; 63729 MW; EA41FEE2DD40AC2A CRC64;
MKTTTILILL THWVHSQNPT GGNNTATLCL GHHAVANGTL VKTITDDQIE VTNATELVQS
TSTGKICNNP YRVLDGRNCT LIDAMLGDPH YDVFQYENWD LFIERSSAFS NCYPYDVPDY
ASLRSLVASS GTLEFMAEGF TWTGVTQNGG SSACRRGSAD SFFSRLNWLT QSESSYPTLN
VTMPNNDNFD KLYIWGIHHP STNNEQTKLY VQASGRVTVS TKRSQQTIIP NIGSRPWVRG
QSGRISIYWT IVKPGDVLMI NSNGNLIAPR GYFKMRTGKS SIMRSDAPID TCVSECITPN
GSIPNDKPFQ NVNKVTYGKC PKYVKQSTLK LATGMRNVPE KQIRGIFGAI AGFIENGWEG
MVDGWYGFRY QNSEGTLQAG DLKSTQAAID QINGKLNRVI EKTNEKFHQI EKEFSEVEGR
IQDLEKYVED TKIDLWSYNA ELLVALENQH TIDLTDAEMN KLFEKTRRQL RENAEDMGNG
CFKIYHKCDN ACIESIRNGT YDHDIYRDEA LNNRFQIRGV ELKSGYKDWI LWISFAISCF
LICVVLLGFI MWACQKGNIR CNICI


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