HEMA_I82A0
ID HEMA_I82A0 Reviewed; 563 AA.
AC P26137;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 02-JUN-2021, entry version 112.
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; Fragment;
GN Name=HA {ECO:0000255|HAMAP-Rule:MF_04072};
OS Influenza A virus (strain A/Mallard/Astrakhan/244/1982 H14N6) (Influenza A
OS virus (strain A/Mallard/Gurjev/244/1982 H14N6)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=11433;
OH NCBI_TaxID=8782; Aves.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2238469; DOI=10.1016/0042-6822(90)90143-f;
RA Kawaoka Y., Yamnikova S., Chambers T.M., Lvov D.K., Webster R.G.;
RT "Molecular characterization of a new hemagglutinin, subtype H14, of
RT influenza A virus.";
RL Virology 179:759-767(1990).
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. {ECO:0000255|HAMAP-
CC Rule:MF_04072}.
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.
CC -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
CC {ECO:0000255|HAMAP-Rule:MF_04072}.
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DR EMBL; M35996; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR PDB; 3EYJ; X-ray; 2.60 A; A=20-342, B=343-514.
DR PDB; 3EYK; X-ray; 2.50 A; A=20-342, B=343-514.
DR PDBsum; 3EYJ; -.
DR PDBsum; 3EYK; -.
DR SMR; P26137; -.
DR DrugBank; DB07726; t-Butylhydroquinone.
DR EvolutionaryTrace; P26137; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046789; F:host cell surface receptor binding; IEA:InterPro.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
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; 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 CHAIN 1..342
FT /note="Hemagglutinin HA1 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000440845"
FT CHAIN 343..563
FT /note="Hemagglutinin HA2 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000039019"
FT TOPO_DOM 1..526
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TOPO_DOM 548..563
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 552
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 559
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 CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 25..479
FT /note="Interchain (between HA1 and HA2 chains)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 63..290
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 75..87
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 108..150
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 294..318
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 486..490
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT NON_TER 1
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:3EYK"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:3EYK"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:3EYK"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 184..196
FT /evidence="ECO:0007829|PDB:3EYK"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 263..272
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:3EYK"
FT HELIX 347..351
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 363..370
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:3EYK"
FT HELIX 380..396
FT /evidence="ECO:0007829|PDB:3EYK"
FT HELIX 418..468
FT /evidence="ECO:0007829|PDB:3EYK"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:3EYK"
FT STRAND 476..484
FT /evidence="ECO:0007829|PDB:3EYK"
FT HELIX 488..495
FT /evidence="ECO:0007829|PDB:3EYK"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:3EYK"
FT HELIX 505..512
FT /evidence="ECO:0007829|PDB:3EYK"
SQ SEQUENCE 563 AA; 62591 MW; FBD2BA976A3D5977 CRC64;
LVALALSQTA YSQITNGTTG NPIICLGHHA VENGTSVKTL TDNHVEVVSA KELVETKHTD
ELCPSPLKLV DGQDCDLING ALGSPGCDRL QDTTWDVFIE RPTAVDTCYP FDVPDYQSLR
SILASSGSLE FIAEQFTWNG VKVDGSSSAC LRGGRNSFFS RLNWLTKATN GNYGPINVTK
ENTGSYVRLY LWGVHHPSSD NEQTDLYKVA TGRVTVSTRS DQISIVPNIG SRPRVRNQSG
RISIYWTLVN PGDSIIFNSI GNLIAPRGHY KISKSTKSTV LKSDKRIGSC TSPCLTDKGS
IQSDKPFQNV SRIAIGNCPK YVKQGSLMLA TGMRNIPGKQ AKGLFGAIAG FIENGWQGLI
DGWYGFRHQN AEGTGTAADL KSTQAAIDQI NGKLNRLIEK TNEKYHQIEK EFEQVEGRIQ
DLEKYVEDTK IDLWSYNAEL LVALENQHTI DVTDSEMNKL FERVRRQLRE NAEDQGNGCF
EIFHQCDNNC IESIRNGTYD HNIYRDEAIN NRIKINPVTL TMGYKDIILW ISFSMSCFVF
VALILGFVLW ACQNGNIRCQ ICI
