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Hemagglutinin

 A0A172QYS4_9INFA        Unreviewed;       565 AA.
A0A172QYS4;
07-SEP-2016, integrated into UniProtKB/TrEMBL.
07-SEP-2016, sequence version 1.
23-MAY-2018, entry version 14.
RecName: Full=Hemagglutinin {ECO:0000256|HAMAP-Rule:MF_04072};
Contains:
RecName: Full=Hemagglutinin HA1 chain {ECO:0000256|HAMAP-Rule:MF_04072};
Contains:
RecName: Full=Hemagglutinin HA2 chain {ECO:0000256|HAMAP-Rule:MF_04072};
Flags: Precursor;
Name=HA {ECO:0000256|HAMAP-Rule:MF_04072,
ECO:0000313|EMBL:ANE05869.1};
Influenza A virus (A/mallard/Southcentral
Alaska/15ML00407/2015(H11N9)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Alphainfluenzavirus.
NCBI_TaxID=1821095 {ECO:0000313|EMBL:ANE05869.1};
[1] {ECO:0000313|EMBL:ANE05869.1}
NUCLEOTIDE SEQUENCE.
STRAIN=A/mallard/Southcentral Alaska/15ML00407/2015
{ECO:0000313|EMBL:ANE05869.1};
Das S.R., Halpin R.A., Lin X., Simenauer A., Akopov A., Fedorova N.,
Puri V., Stockwell T., Amedeo P., Katzel D., Schobel S.,
Shrivastava S., Hill N., Bao Y., Sanders R., Zhdanov S., Kiryutin B.,
Lipman D.J., Tatusova T., Runstadler J.;
"The NIAID Influenza Genome Sequencing Project.";
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:ANE05869.1}
NUCLEOTIDE SEQUENCE.
STRAIN=A/mallard/Southcentral Alaska/15ML00407/2015
{ECO:0000313|EMBL:ANE05869.1};
The NIAID Influenza Genome Sequencing Consortium;
Submitted (MAY-2016) 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}.
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EMBL; CY206854; ANE05869.1; -; Viral_cRNA.
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};
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 530 553 Helical. {ECO:0000256|HAMAP-
Rule:MF_04072}.
COILED 398 425 {ECO:0000256|SAM:Coils}.
SITE 342 343 Cleavage; by host. {ECO:0000256|HAMAP-
Rule:MF_04072}.
LIPID 554 554 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}.
LIPID 564 564 S-palmitoyl cysteine; by host.
{ECO:0000256|HAMAP-Rule:MF_04072}.
DISULFID 20 479 Interchain (between HA1 and HA2 chains).
{ECO:0000256|HAMAP-Rule:MF_04072}.
DISULFID 58 290 {ECO:0000256|HAMAP-Rule:MF_04072}.
DISULFID 71 83 {ECO:0000256|HAMAP-Rule:MF_04072}.
DISULFID 106 151 {ECO:0000256|HAMAP-Rule:MF_04072}.
DISULFID 294 318 {ECO:0000256|HAMAP-Rule:MF_04072}.
DISULFID 486 490 {ECO:0000256|HAMAP-Rule:MF_04072}.
SEQUENCE 565 AA; 62902 MW; DD11DDAED7E1F88B CRC64;
MKKTLLLAAI IICIQADEIC IGYLSNNSTE KVDTIIESNV TVTSSVELVE NEHTGSFCSI
DGKAPISLGD CSFAGWILGN PMCDDLIGKT SWSYIVEKPN PTNGICYPGT LENEEELRLK
FSGVLEFNKF EAFTSNGWGA VNSGAGVTAA CKFGSSNAFF RNMVWLIHQS GTYPVIRRTF
NNTKGRDVLM VWGVHHPATL KEHQDLYKKD SSYVAVGSES YNRRFTPEIS TRPKVNGQAG
RMTFYWTIVK PGEAITFESN GAFLAPRYAF ELVSLGNGKL FRSDLSIESC STKCQSEIGG
INTNRSFHNV HRNTIGDCPK YVNVKSLKLA TGLRNVPAIA TRGLFGAIAG FIEGGWPGLI
NGWYGFQHRN EEGTGIAADK ESTQKAIDQI TSKVNNVVDR MNTNFESVQH EFSEIEERIN
QLSKHVDDSV IDIWSYNAQL LVLLENEKTL DLHDSNVRNL HEKVRRMLKD NAKDEGNGCF
TFYHKCDNEC IEKVRNGTYD HKEFEEESKL NRQEIEGVKL DSNGNVYKIL SIYSCIASSL
VLAAIIMGFI FWACSNGSCR CTICI


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