HEMA_I77AF
ID HEMA_I77AF Reviewed; 566 AA.
AC P13103; Q0A416;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 3.
DT 02-JUN-2021, entry version 136.
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 A virus (strain A/Gull/Maryland/704/1977 H13N6).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=384499;
OH NCBI_TaxID=8782; Aves.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2024485; DOI=10.1016/0042-6822(91)90588-3;
RA Nobusawa E., Aoyama T., Kato H., Suzuki Y., Tateno Y., Nakajima K.;
RT "Comparison of complete amino acid sequences and receptor-binding
RT properties among 13 serotypes of hemagglutinins of influenza A viruses.";
RL Virology 182:475-485(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2773315; DOI=10.1016/0042-6822(89)90119-0;
RA Chambers T.M., Yamnikova S., Kawaoka Y., Lvov D.K., Webster R.G.;
RT "Antigenic and molecular characterization of subtype H13 hemagglutinin of
RT influenza virus.";
RL Virology 172:180-188(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16439620; DOI=10.1126/science.1121586;
RA Obenauer J.C., Denson J., Mehta P.K., Su X., Mukatira S., Finkelstein D.B.,
RA Xu X., Wang J., Ma J., Fan Y., Rakestraw K.M., Webster R.G., Hoffmann E.,
RA Krauss S., Zheng J., Zhang Z., Naeve C.W.;
RT "Large-scale sequence analysis of avian influenza isolates.";
RL Science 311:1576-1580(2006).
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 -!- 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. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
CC {ECO:0000255|HAMAP-Rule:MF_04072}.
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DR EMBL; D90308; BAA14338.1; -; Genomic_RNA.
DR EMBL; M26090; AAA43214.1; -; Genomic_RNA.
DR EMBL; CY014694; ABI84566.1; -; Genomic_RNA.
DR PIR; A32664; HMIVT1.
DR PIR; C39987; HMIVGM.
DR PDB; 4KPQ; X-ray; 2.50 A; A/C/E=19-343, B/D/F=344-518.
DR PDB; 4KPS; X-ray; 2.59 A; A/C/E=19-340, B/D/F=345-509.
DR PDBsum; 4KPQ; -.
DR PDBsum; 4KPS; -.
DR SMR; P13103; -.
DR PRIDE; P13103; -.
DR PRO; PR:P13103; -.
DR Proteomes; UP000000828; 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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-UniRule.
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; 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; Signal; 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 SIGNAL 1..18
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CHAIN 19..566
FT /note="Hemagglutinin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000440469"
FT CHAIN 19..342
FT /note="Hemagglutinin HA1 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000038961"
FT CHAIN 344..566
FT /note="Hemagglutinin HA2 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000038962"
FT TOPO_DOM 19..532
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TOPO_DOM 554..566
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT SITE 343..344
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 555
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 565
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 488
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 DISULFID 22..480
FT /note="Interchain (between HA1 and HA2 chains)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 60..291
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 73..85
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 108..151
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 295..319
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 487..491
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CONFLICT 80
FT /note="V -> G (in Ref. 2; AAA43214)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="N -> T (in Ref. 1; BAA14338)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="L -> F (in Ref. 3; ABI84566)"
FT /evidence="ECO:0000305"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:4KPQ"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:4KPQ"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:4KPQ"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4KPS"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 185..197
FT /evidence="ECO:0007829|PDB:4KPQ"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 241..250
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 255..267
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 269..277
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 287..299
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:4KPQ"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 364..371
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:4KPQ"
FT HELIX 381..400
FT /evidence="ECO:0007829|PDB:4KPQ"
FT HELIX 418..469
FT /evidence="ECO:0007829|PDB:4KPQ"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:4KPQ"
FT STRAND 477..485
FT /evidence="ECO:0007829|PDB:4KPQ"
FT HELIX 489..496
FT /evidence="ECO:0007829|PDB:4KPQ"
FT TURN 503..508
FT /evidence="ECO:0007829|PDB:4KPQ"
SQ SEQUENCE 566 AA; 63308 MW; FD9B4187D53A460C CRC64;
MALNVIATLT LISVCVHADR ICVGYLSTNS SERVDTLLEN GVPVTSSIDL IETNHTGTYC
SLNGVSPVHL GDCSFEGWIV GNPACTSNFG IREWSYLIED PAAPHGLCYP GELNNNGELR
HLFSGIRSFS RTELIPPTSW GEVLDGTTSA CRDNTGTNSF YRNLVWFIKK NNRYPVISKT
YNNTTGRDVL VLWGIHHPVS VDETKTLYVN SDPYTLVSTK SWSEKYKLET GVRPGYNGQR
SWMKIYWSLI HPGEMITFES NGGFLAPRYG YIIEEYGKGR IFQSRIRMSR CNTKCQTSVG
GINTNRTFQN IDKNALGDCP KYIKSGQLKL ATGLRNVPAI SNRGLFGAIA GFIEGGWPGL
INGWYGFQHQ NEQGTGIAAD KESTQKAIDQ ITTKINNIID KMNGNYDSIR GEFNQVEKRI
NMLADRIDDA VTDIWSYNAK LLVLLENDKT LDMHDANVKN LHEQVRRELK DNAIDEGNGC
FELLHKCNDS CMETIRNGTY DHTEYAEESK LKRQEIDGIK LKSEDNVYKA LSIYSCIASS
VVLVGLILSF IMWACSSGNC RFNVCI
