HEMA_INBHK
ID HEMA_INBHK Reviewed; 575 AA.
AC P03462;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 02-JUN-2021, entry version 123.
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 B virus (strain B/Hong Kong/8/1973).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Betainfluenzavirus.
OX NCBI_TaxID=427826;
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-
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 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.
CC -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
CC {ECO:0000255|HAMAP-Rule:MF_04072}.
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DR EMBL; K00425; AAA43699.1; ALT_SEQ; Genomic_RNA.
DR PDB; 2RFT; X-ray; 2.80 A; A=9-352, B=353-528.
DR PDB; 2RFU; X-ray; 2.80 A; A=9-352, B=353-528.
DR PDB; 3BT6; X-ray; 2.80 A; A=9-350, B=353-521.
DR PDBsum; 2RFT; -.
DR PDBsum; 2RFU; -.
DR PDBsum; 3BT6; -.
DR SMR; P03462; -.
DR DIP; DIP-46215N; -.
DR UniLectin; P03462; -.
DR ABCD; P03462; 2 sequenced antibodies.
DR EvolutionaryTrace; P03462; -.
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: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-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; 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; 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..352
FT /note="Hemagglutinin HA1 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000440759"
FT CHAIN 353..575
FT /note="Hemagglutinin HA2 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000039107"
FT TOPO_DOM 1..543
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TOPO_DOM 565..575
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT SITE 352..353
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 571
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 574
FT /note="S-palmitoyl cysteine; 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 67
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 171
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 338
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 12..489
FT /note="Interchain (between HA1 and HA2 chains)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 68..80
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 102..151
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 496..500
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT NON_TER 1
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2RFT"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2RFU"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2RFT"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2RFT"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2RFT"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:2RFT"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2RFU"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 191..200
FT /evidence="ECO:0007829|PDB:2RFT"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 250..258
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:2RFT"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:2RFT"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 373..380
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:2RFT"
FT HELIX 392..407
FT /evidence="ECO:0007829|PDB:2RFT"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:2RFT"
FT HELIX 427..478
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 486..491
FT /evidence="ECO:0007829|PDB:2RFT"
FT HELIX 498..505
FT /evidence="ECO:0007829|PDB:2RFT"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:2RFT"
SQ SEQUENCE 575 AA; 62059 MW; C029241041DBEEA9 CRC64;
LMVVTSNADR ICTGITSSNS PHVVKTATQG EVNVTGVIPL TTTPTKSHFA NLKGTQTRGK
LCPNCLNCTD LDVALGRPKC MGNIPSAKAS ILHEVKPGTS GCFPIMHDRT KIRQLPNLLR
GYENIRLSAR NVTNAETAPG GPYIVGTSGS CPNVTNGNGF FATMAWAVPK NKTATNPLTV
EVPYICTKGE DQITVWGFHS DDETQMVKLY GDSKPQKFTS SANGVTTHYV SQIGGFPNQA
EDEGLPQSGR IVVDYMVQKP GKTGTIAYQR GVLLPQKVWC ASGRRKVIEG SLPLIGEADC
LHEKYGGLNK SKPYYTGEHA KAIGNCPIWV KTPLKLANGT KYRPPAKLLK ERGFFGAIAG
FLEGGWEGMI AGWHGYTSHG AHGVAVAADL KSTQEAINKI TKNLFSLSEL EVKNLHRLSG
AMDELHNEIL ELDEKVDDLR ADTISSQIEL AVLLSNEGII NSEDEHLLAL ERKLKKMLGP
SAVEIGNGCF ETKHKCNQTC LDRIAAGTFN AGEFSLPTFD SLNITAASLN DDGLDNHTIL
LYYSTAASSL AVTLMIAIFI VYMVSRDNVS CSICL
