ID   HEMA_I88A0              Reviewed;         344 AA.
AC   P28730;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   07-OCT-2020, entry version 108.
DE   RecName: Full=Hemagglutinin;
DE   Contains:
DE     RecName: Full=Hemagglutinin HA1 chain;
DE   Flags: Precursor; Fragment;
GN   Name=HA;
OS   Influenza A virus (strain A/Harbin/1/1988 H1N2).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=387156;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1538194; DOI=10.1099/0022-1317-73-2-383;
RA   Guo Y., Xu X., Cox N.J.;
RT   "Human influenza A (H1N2) viruses isolated from China.";
RL   J. Gen. Virol. 73:383-388(1992).
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 of about two third
CC       of the virus particles through clathrin-dependent endocytosis and about
CC       one third through a clathrin- and caveolin-independent pathway. Plays a
CC       major role in the determination of host range restriction and
CC       virulence. Class I viral fusion protein. Responsible for penetration of
CC       the virus into the cell cytoplasm by mediating the fusion of the
CC       membrane of the endocytosed virus particle with the endosomal membrane.
CC       Low pH in endosomes induces an irreversible conformational change in
CC       HA2, releasing the fusion hydrophobic peptide. Several trimers are
CC       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 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:0000305}.
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DR   EMBL; L19006; AAA43175.1; -; Genomic_RNA.
DR   SMR; P28730; -.
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   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   3: Inferred from homology;
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; Viral attachment to host cell;
KW   Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW   Virus endocytosis by host; Virus entry into host cell.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..343
FT                   /note="Hemagglutinin HA1 chain"
FT                   /id="PRO_0000038967"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        40
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        104
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        142
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        286
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        59..292
FT                   /evidence="ECO:0000250"
FT   DISULFID        72..84
FT                   /evidence="ECO:0000250"
FT   DISULFID        107..153
FT                   /evidence="ECO:0000250"
FT   DISULFID        296..320
FT                   /evidence="ECO:0000250"
FT   NON_TER         344
SQ   SEQUENCE   344 AA;  38564 MW;  4BAAB1B343087B89 CRC64;
     MKAKLLILFC AFTATDADTI CIGYHANNST DTVDTVLEKN VTVTHSVNLL EDSHNGKLCR
     LKGIAPLQLG NCSIAGWILG NPECESLFSQ KSWSYIAETP NSENGTCYPG YFADYEELRE
     QLSSVSSFER FEIFPKESSW PNHTVTKGVT ASCSHKGRSS FYRNLLWLTE KNGLYPNLSK
     SYVNNKEKEV LVLWGVHHPS NIGDQRAIYH TENAYVSVVS SHYNRRFIPE IAKRPKVRGQ
     EGRINYYWTL LEPRDTIIFE ANGNLIAPWY AFALSRGFGS GIITSNASMD ECDAKCQTPQ
     GAINSSLPFQ NVHPVTIGEC PKYVRSTKLR MATGLRNIPS IQSR