HEMA_INBID
ID HEMA_INBID Reviewed; 366 AA.
AC P12441;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Hemagglutinin;
DE Contains:
DE RecName: Full=Hemagglutinin HA1 chain;
DE Contains:
DE RecName: Full=Hemagglutinin HA2 chain;
DE Flags: Precursor; Fragment;
GN Name=HA;
OS Influenza B virus (strain B/ID/1986).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Betainfluenzavirus.
OX NCBI_TaxID=11534;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3267218; DOI=10.1016/0042-6822(88)90238-3;
RA Yamashita M., Krystal M., Fitch W.M., Palese P.;
RT "Influenza B virus evolution: co-circulating lineages and comparison of
RT evolutionary pattern with those of influenza A and C viruses.";
RL Virology 163:112-122(1988).
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 -!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Host apical cell membrane; Single-pass
CC type I membrane protein. 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 -!- 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 (By similarity). {ECO:0000250}.
CC -!- PTM: Palmitoylated. {ECO:0000250}.
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:0000305}.
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DR EMBL; M22945; AAA43723.1; -; Genomic_RNA.
DR SMR; P12441; -.
DR PRIDE; P12441; -.
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: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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 3.90.209.20; -; 1.
DR InterPro; IPR008980; Capsid_hemagglutn.
DR InterPro; IPR013828; Hemagglutn_HA1_a/b_dom_sf.
DR InterPro; IPR001364; Hemagglutn_influenz_A/B.
DR Pfam; PF00509; Hemagglutinin; 1.
DR SUPFAM; SSF49818; SSF49818; 1.
PE 3: Inferred from homology;
KW Disulfide bond; 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; Viral attachment to host cell;
KW Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW Virus entry into host cell.
FT SIGNAL <1..12
FT CHAIN 13..357
FT /note="Hemagglutinin HA1 chain"
FT /id="PRO_0000039111"
FT CHAIN 359..>366
FT /note="Hemagglutinin HA2 chain"
FT /id="PRO_0000039112"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 366
SQ SEQUENCE 366 AA; 39432 MW; A9EE33B68CD2EF81 CRC64;
IIVLLMVVTS NADRICTGIT SSNSPHVVKT ATQGEVNVTG VIPLTTTPTK SHFANLKGTK
TRGKLCPKCL NCTDLDVALG RPKCMGTIPS AKASILHEVK PVTSGCFPIM HDRTKIRQLP
NLLRGYENIR LSTHNVINAE TAPGGPYIVG TSGSCPNVTN GNGFFATMAW AVPKNNNKTA
MNPLTVEVPF ICTEGEDQIT VWGFHSDDET QMVKLYGDSK PQKFTSSANG VTTHYVSQIG
GFPKQAEDGG LPQSGRIVVD YMVQKSGKTG TITYQRGILL PQKVWCASGR SKVIKRSLPL
IGEADCLHEK YGGLNKSKPY YTGEHAKAIG NCPIWVKTPL KQANGTKYRP AAKLLKERGF
FGAIAG
