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

 H9XL17_9INFA            Unreviewed;       566 AA.
H9XL17;
13-JUN-2012, integrated into UniProtKB/TrEMBL.
13-JUN-2012, sequence version 1.
16-JAN-2019, entry version 44.
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:AFG99877.1};
Influenza A virus (A/Paris/457/1991(H3N2)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Alphainfluenzavirus.
NCBI_TaxID=1086998 {ECO:0000313|EMBL:AFG99877.1, ECO:0000313|Proteomes:UP000125375};
[1] {ECO:0000313|EMBL:AFG99877.1, ECO:0000313|Proteomes:UP000125375}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=A/Paris/457/1991 {ECO:0000313|EMBL:AFG99877.1};
Wentworth D.E., Dugan V., Halpin R., Lin X., Bera J., Ghedin E.,
Fedorova N., Overton L., Tsitrin T., Stockwell T., Amedeo P.,
Bishop B., Chen H., Edworthy P., Gupta N., Katzel D., Li K.,
Schobel S., Shrivastava S., Thovarai V., Wang S., Westgeest K.B.,
van Beek R., Bestebroer T.M., de Jong J.C., Rimmelzwaan G.F.,
Osterhaus A.D.M.E., Fouchier R.A.M., Bao Y., Sanders R., Dernovoy D.,
Kiryutin B., Lipman D.J., Tatusova T.;
"The NIAID Influenza Genome Sequencing Project.";
Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:AFG99877.1, ECO:0000313|Proteomes:UP000125375}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=A/Paris/457/1991 {ECO:0000313|EMBL:AFG99877.1};
The NIAID Influenza Genome Sequencing Consortium;
Submitted (MAY-2012) 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; CY113821; AFG99877.1; -; Viral_cRNA.
Proteomes; UP000125375; 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:UP000125375};
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 530 554 Helical. {ECO:0000256|HAMAP-
Rule:MF_04072}.
COILED 383 421 {ECO:0000256|SAM:Coils}.
SITE 345 346 Cleavage; by host. {ECO:0000256|HAMAP-
Rule:MF_04072}.
LIPID 555 555 S-palmitoyl cysteine; by host.
{ECO:0000256|HAMAP-Rule:MF_04072}.
LIPID 562 562 S-palmitoyl cysteine; by host.
{ECO:0000256|HAMAP-Rule:MF_04072}.
LIPID 565 565 S-palmitoyl cysteine; by host.
{ECO:0000256|HAMAP-Rule:MF_04072}.
DISULFID 80 92 {ECO:0000256|HAMAP-Rule:MF_04072}.
DISULFID 297 321 {ECO:0000256|HAMAP-Rule:MF_04072}.
DISULFID 489 493 {ECO:0000256|HAMAP-Rule:MF_04072}.
SEQUENCE 566 AA; 63680 MW; 087C5A9AFB6BA401 CRC64;
MKTIIALSYI LCLVFAQKLP GNDNSTATLC LGHHAVPNGT LVKTITNDQI EVTNATELVQ
SSSTGRICDS PHRILDGKNC TLIDALLGDP HCDGFQNKEW DLFVERSKAY SNCYPYDVPD
YASLRSLVAS SGTLEFTNED FNWTGVAQSG ESYACKRGSV KSFFSRLNWL HESDYKYPAL
NVTMPNNGKF DKLYIWGVHH PSTDREQTSL YVRASGRVTV STKRSQQTVI PNIGSRPWVR
GLSSRISIYW TIVKPGDILL INSTGNLIAP RGYFKIRTGK SSIMRSDAPI GTCSSECITP
NGSIPNDKPF QNVNRITYGA CPRYVKQNTL KLATGMRNVP EKQTRGIFGA IAGFIENGWE
GMVDGWYGFR HQNSEGTGQA ADLKSTQAAI DQINGKLNRL IEKTNEKFHQ IEKEFSEVEG
RIQDLEKYVE DTKIDLWSYN AELLVALENQ HTIDLTDSEM NKLFEKTRKQ LRENAEDMGN
GCFKIYHKCD NACIGSIRNG TYDHDVYRDE ALNNRFQIKG VELKSGYKDW ILWISFAISC
FLLCVVLLGF IMWACQKGNI RCNICI


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