HEMA_INBLE
ID HEMA_INBLE Reviewed; 584 AA.
AC P03460;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 23-FEB-2022, entry version 127.
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 B virus (strain B/Lee/1940).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Betainfluenzavirus.
OX NCBI_TaxID=518987;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6192436; DOI=10.1073/pnas.80.14.4527;
RA Krystal M., Young J.F., Palese P., Wilson I.A., Skehel J.J., Wiley D.C.;
RT "Sequential mutations in hemagglutinins of influenza B virus isolates:
RT definition of antigenic domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:4527-4531(1983).
RN [2]
RP ERRATUM OF PUBMED:6192436, AND SEQUENCE REVISION.
RA Krystal M., Young J.F., Palese P., Wilson I.A., Skehel J.J., Wiley D.C.;
RL Proc. Natl. Acad. Sci. U.S.A. 81:1261-1261(1984).
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. Plays a major role in the determination of host range restriction
CC and virulence. Class I viral fusion protein. Responsible for
CC penetration of the virus into the cell cytoplasm by mediating the
CC fusion of the membrane of the endocytosed virus particle with the
CC endosomal membrane. Low pH in endosomes induce an irreversible
CC conformational change in HA2, releasing the fusion hydrophobic peptide.
CC Several trimers are required to form a competent fusion pore.
CC {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-Rule:MF_04072,
CC ECO:0000305}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04072, ECO:0000305}. Host apical cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04072, ECO:0000305}. Note=Targeted to the
CC apical plasma membrane in epithelial polarized cells through a signal
CC present in the transmembrane domain. Associated with
CC glycosphingolipid- and cholesterol-enriched detergent-resistant lipid
CC rafts. {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 B 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; K00423; AAA43716.1; -; Genomic_RNA.
DR EMBL; J02093; AAA43700.1; ALT_SEQ; Genomic_RNA.
DR PIR; C93986; HMIVB.
DR RefSeq; NP_056660.1; NC_002207.1.
DR PDB; 4NRJ; X-ray; 2.53 A; A/C/E=16-361, B/D/F=362-537.
DR PDB; 4NRK; X-ray; 2.63 A; A/C/E=16-361, B/D/F=362-537.
DR PDB; 4NRL; X-ray; 2.72 A; A/C/E=16-361, B/D/F=362-537.
DR PDBsum; 4NRJ; -.
DR PDBsum; 4NRK; -.
DR PDBsum; 4NRL; -.
DR SMR; P03460; -.
DR GeneID; 956538; -.
DR KEGG; vg:956538; -.
DR Proteomes; UP000008158; 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:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
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; IPR001364; Hemagglutn_influenz_A/B.
DR InterPro; IPR000386; Hemagglutn_influenz_B.
DR Pfam; PF00509; Hemagglutinin; 1.
DR PRINTS; PR00329; HEMAGGLUTN12.
DR PRINTS; PR00331; HEMAGGLUTN2.
DR SUPFAM; SSF49818; SSF49818; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; 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..15
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CHAIN 16..584
FT /note="Hemagglutinin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000440547"
FT CHAIN 16..360
FT /note="Hemagglutinin HA1 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000039114"
FT CHAIN 362..584
FT /note="Hemagglutinin HA2 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000039115"
FT TOPO_DOM 16..552
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TOPO_DOM 574..584
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT SITE 361..362
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 580
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 583
FT /note="S-palmitoyl cysteine; 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 74
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 19..498
FT /note="Interchain (between HA1 and HA2 chains)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 75..87
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 109..158
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 505..509
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:4NRJ"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:4NRJ"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:4NRJ"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:4NRJ"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:4NRJ"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:4NRJ"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:4NRL"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 200..209
FT /evidence="ECO:0007829|PDB:4NRJ"
FT HELIX 212..219
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 305..311
FT /evidence="ECO:0007829|PDB:4NRJ"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:4NRJ"
FT HELIX 363..368
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 382..389
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:4NRJ"
FT HELIX 399..417
FT /evidence="ECO:0007829|PDB:4NRJ"
FT TURN 432..435
FT /evidence="ECO:0007829|PDB:4NRJ"
FT HELIX 436..470
FT /evidence="ECO:0007829|PDB:4NRJ"
FT HELIX 472..487
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:4NRJ"
FT STRAND 495..500
FT /evidence="ECO:0007829|PDB:4NRJ"
FT HELIX 507..514
FT /evidence="ECO:0007829|PDB:4NRJ"
FT HELIX 520..523
FT /evidence="ECO:0007829|PDB:4NRJ"
SQ SEQUENCE 584 AA; 63275 MW; 300F4C523D5C285E CRC64;
MKAIIVLLMV VTSNADRICT GITSSNSPHV VKTATQGEVN VTGVIPLTTT PTKSHFANLK
GTQTRGKLCP NCFNCTDLDV ALGRPKCMGN TPSAKVSILH EVKPATSGCF PIMHDRTKIR
QLPNLLRGYE NIRLSTSNVI NTETAPGGPY KVGTSGSCPN VANGNGFFNT MAWVIPKDNN
KTAINPVTVE VPYICSEGED QITVWGFHSD DKTQMERLYG DSNPQKFTSS ANGVTTHYVS
QIGGFPNQTE DEGLKQSGRI VVDYMVQKPG KTGTIVYQRG ILLPQKVWCA SGRSKVIKGS
LPLIGEADCL HEKYGGLNKS KPYYTGEHAK AIGNCPIWVK TPLKLANGTK YRPPAKLLKE
RGFFGAIAGF LEGGWEGMIA GWHGYTSHGA HGVAVAADLK STQEAINKIT KNLNYLSELE
VKNLQRLSGA MNELHDEILE LDEKVDDLRA DTISSQIELA VLLSNEGIIN SEDEHLLALE
RKLKKMLGPS AVEIGNGCFE TKHKCNQTCL DRIAAGTFNA GDFSLPTFDS LNITAASLND
DGLDNHTILL YYSTAASSLA VTLMIAIFIV YMVSRDNVSC SICL
