HEMA_I40A0
ID HEMA_I40A0 Reviewed; 566 AA.
AC Q0HD60;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 02-JUN-2021, entry version 73.
DE RecName: Full=Hemagglutinin {ECO:0000255|HAMAP-Rule:MF_04072};
DE Contains:
DE RecName: Full=Hemagglutinin HA1 chain {ECO:0000255|HAMAP-Rule:MF_04072};
DE Contains:
DE RecName: Full=Hemagglutinin HA2 chain {ECO:0000255|HAMAP-Rule:MF_04072};
DE Flags: Precursor;
GN Name=HA {ECO:0000255|HAMAP-Rule:MF_04072};
OS Influenza A virus (strain A/Hickox/1940 H1N1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=383543;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Spiro D., Ghedin E., Sengamalay N., Halpin R., Boyne A., Zaborsky J.,
RA Feldblyum T., Subbu V., Sparenborg J., Shumway M., Sitz J., Katzel D.,
RA Koo H., Salzberg S.L., Griesemer S., St George K., Bennett R., Taylor J.,
RA Bennink J.R., Yewdell J.W., Bao Y., Bolotov P., Dernovoy D., Kiryutin B.,
RA Lipman D.J., Tatusova T.;
RT "The NIAID influenza genome sequencing project.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RG The NIAID Influenza Genome Sequencing Consortium;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds to sialic acid-containing receptors on the cell
CC surface, bringing about the attachment of the virus particle to the
CC cell. This attachment induces virion internalization either through
CC clathrin-dependent endocytosis or through clathrin- and caveolin-
CC independent pathway. Plays a major role in the determination of host
CC range restriction and virulence. Class I viral fusion protein.
CC Responsible for penetration of the virus into the cell cytoplasm by
CC mediating the fusion of the membrane of the endocytosed virus particle
CC with the endosomal membrane. Low pH in endosomes induces an
CC irreversible conformational change in HA2, releasing the fusion
CC hydrophobic peptide. Several trimers are required to form a competent
CC fusion pore. {ECO:0000255|HAMAP-Rule:MF_04072}.
CC -!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2. Interacts with human
CC CACNA1C. {ECO:0000250|UniProtKB:Q289M7}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04072}. Host apical cell membrane {ECO:0000255|HAMAP-
CC Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04072}. Note=Targeted to the apical plasma membrane in
CC epithelial polarized cells through a signal present in the
CC transmembrane domain. Associated with glycosphingolipid- and
CC cholesterol-enriched detergent-resistant lipid rafts.
CC {ECO:0000255|HAMAP-Rule:MF_04072}.
CC -!- PTM: Palmitoylated. {ECO:0000255|HAMAP-Rule:MF_04072}.
CC -!- PTM: In natural infection, inactive HA is matured into HA1 and HA2
CC outside the cell by one or more trypsin-like, arginine-specific
CC endoprotease secreted by the bronchial epithelial cells. One identified
CC protease that may be involved in this process is secreted in lungs by
CC Clara cells. {ECO:0000255|HAMAP-Rule:MF_04072}.
CC -!- MISCELLANEOUS: Major glycoprotein, comprises over 80% of the envelope
CC proteins present in virus particle.
CC -!- MISCELLANEOUS: The extent of infection into host organism is determined
CC by HA. Influenza viruses bud from the apical surface of polarized
CC epithelial cells (e.g. bronchial epithelial cells) into lumen of lungs
CC and are therefore usually pneumotropic. The reason is that HA is
CC cleaved by tryptase clara which is restricted to lungs. However, HAs of
CC H5 and H7 pantropic avian viruses subtypes can be cleaved by furin and
CC subtilisin-type enzymes, allowing the virus to grow in other organs
CC than lungs.
CC -!- MISCELLANEOUS: The influenza A genome consist of 8 RNA segments.
CC Genetic variation of hemagglutinin and/or neuraminidase genes results
CC in the emergence of new influenza strains. The mechanism of variation
CC can be the result of point mutations or the result of genetic
CC reassortment between segments of two different strains. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
CC {ECO:0000255|HAMAP-Rule:MF_04072}.
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DR EMBL; CY013271; ABI20826.1; -; Other_RNA.
DR PDB; 6ONA; X-ray; 1.95 A; A/B/C=18-509.
DR PDBsum; 6ONA; -.
DR SMR; Q0HD60; -.
DR PRO; PR:Q0HD60; -.
DR Proteomes; UP000156248; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046789; F:host cell surface receptor binding; IEA:UniProtKB-UniRule.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
DR GO; GO:0046761; P:viral budding from plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 3.90.209.20; -; 1.
DR HAMAP; MF_04072; INFV_HEMA; 1.
DR InterPro; IPR008980; Capsid_hemagglutn.
DR InterPro; IPR013828; Hemagglutn_HA1_a/b_dom_sf.
DR InterPro; IPR000149; Hemagglutn_influenz_A.
DR InterPro; IPR001364; Hemagglutn_influenz_A/B.
DR Pfam; PF00509; Hemagglutinin; 1.
DR PRINTS; PR00330; HEMAGGLUTN1.
DR PRINTS; PR00329; HEMAGGLUTN12.
DR SUPFAM; SSF49818; SSF49818; 1.
PE 1: Evidence at protein level;
KW 3D-structure;
KW Clathrin- and caveolin-independent endocytosis of virus by host;
KW Clathrin-mediated endocytosis of virus by host; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein; Hemagglutinin;
KW Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW Membrane; Palmitate; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CHAIN 18..566
FT /note="Hemagglutinin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000440380"
FT CHAIN 18..343
FT /note="Hemagglutinin HA1 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000372877"
FT CHAIN 345..566
FT /note="Hemagglutinin HA2 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000372878"
FT TOPO_DOM 18..529
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TOPO_DOM 551..566
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT SITE 344..345
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 555
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 562
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 565
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 21..481
FT /note="Interchain (between HA1 and HA2 chains)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 59..292
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 72..84
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 107..153
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 296..320
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 488..492
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:6ONA"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:6ONA"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:6ONA"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 186..198
FT /evidence="ECO:0007829|PDB:6ONA"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 240..251
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 265..276
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 288..297
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:6ONA"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 365..372
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:6ONA"
FT HELIX 382..401
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:6ONA"
FT HELIX 419..470
FT /evidence="ECO:0007829|PDB:6ONA"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:6ONA"
FT STRAND 478..486
FT /evidence="ECO:0007829|PDB:6ONA"
FT HELIX 490..497
FT /evidence="ECO:0007829|PDB:6ONA"
SQ SEQUENCE 566 AA; 63513 MW; 9AD56C9D1367D89A CRC64;
MKAKLLILLC ALSATDADTI CIGYHANNST DTVDTVLEKN VTVTHSVNLL EDSHNGKLCR
LKGIAPLQLG KCNIAGWILG NPECESLLSK RSWSYIAETP NSENGTCYPG DFADYEELRE
QLSSVSSFER FEIFPKERSW PNHNINIGVT AACSHAGKSS FYKNLLWLTE KDGSYPNLNK
SYVNKKEKEV LVLWGVHHPS NIENQKTLYR KENAYVSVVS SNYNRRFTPE IAERPKVRGQ
AGRMNYYWTL LEPGDTIIFE ANGNLIAPWY AFALSRGLGS GIITSNASMD ECDTKCQTPQ
GAINSSLPFQ NIHPFTIGEC PKYVRSTKLR MVTGLRNIPS IQSRGLFGAI AGFIEGGWAG
MIDGWYGYHH QNEQGSGYAA DQKSTQNAIN GITNKVNSVI EKMNTQFTAV GKEFNKLEKR
MENLNKKVDD GFLDIWTYNA ELLVLLENER TLDFHDSNVK NLYEKVKNQL RNNAKEIGNG
CFEFYHKCNN ECMESVKNGT YDYPKYSEES KLNREKIDGV KLESMGVYQI LAIYSTVASS
LVLLVSLGAI SFWMCSNGSL QCRICI
