HEMA_I57A5
ID HEMA_I57A5 Reviewed; 562 AA.
AC Q67333;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-JUN-2021, entry version 111.
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/Singapore/1/1957 H2N2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=382781;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7684877; DOI=10.1006/viro.1993.1319;
RA Schafer J.R., Kawaoka Y., Bean W.J., Suss J., Senne D., Webster R.G.;
RT "Origin of the pandemic 1957 H2 influenza A virus and the persistence of
RT its possible progenitors in the avian reservoir.";
RL Virology 194:781-788(1993).
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; L11142; AAA43678.1; -; Genomic_RNA.
DR PDB; 2WR7; X-ray; 2.50 A; A/B/C=1-506.
DR PDB; 2WRB; X-ray; 3.10 A; A/B/C=1-506.
DR PDB; 2WRC; X-ray; 2.71 A; A/B/C=1-506.
DR PDBsum; 2WR7; -.
DR PDBsum; 2WRB; -.
DR PDBsum; 2WRC; -.
DR SMR; Q67333; -.
DR EvolutionaryTrace; Q67333; -.
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..15
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CHAIN 16..562
FT /note="Hemagglutinin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000440393"
FT CHAIN 16..339
FT /note="Hemagglutinin HA1 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000280201"
FT CHAIN 341..562
FT /note="Hemagglutinin HA2 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000280202"
FT TOPO_DOM 16..525
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TOPO_DOM 547..562
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT SITE 340..341
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 551
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 558
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 561
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 179
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 300
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 19..477
FT /note="Interchain (between HA1 and HA2 chains)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 57..288
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 70..82
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 105..149
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 292..316
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 484..488
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2WR7"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:2WR7"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2WR7"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 122..132
FT /evidence="ECO:0007829|PDB:2WR7"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 182..194
FT /evidence="ECO:0007829|PDB:2WR7"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 252..259
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 261..271
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 285..294
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:2WR7"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:2WR7"
FT HELIX 378..397
FT /evidence="ECO:0007829|PDB:2WR7"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:2WRB"
FT HELIX 415..466
FT /evidence="ECO:0007829|PDB:2WR7"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:2WR7"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:2WR7"
FT HELIX 486..494
FT /evidence="ECO:0007829|PDB:2WR7"
SQ SEQUENCE 562 AA; 63162 MW; 5178496D4EDF5172 CRC64;
MAIIYLILLF TAVRGDQICI GYHANNSTEK VDTILERNVT VTHAKDILEK THNGKLCKLN
GIPPLELGDC SIAGWLLGNP ECDRLLSVPE WSYIMEKENP RDGLCYPGSF NDYEELKHLL
SSVKHFEKVK ILPKDRWTQH TTTGGSRACA VSGNPSFFRN MVWLTEKGSN YPVAKGSYNN
TSGEQMLIIW GVHHPNDEKE QRTLYQNVGT YVSVGTSTLN KRSTPDIATR PKVNGLGSRM
EFSWTLLDMW DTINFESTGN LIAPEYGFKI SKRGSSGIMK TEGTLENCET KCQTPLGAIN
TTLPFHNVHP LTIGECPKYV KSEKLVLATG LRNVPQIESR GLFGAIAGFI EGGWQGMIDG
WYGYHHSNDQ GSGYAADKES TQKAFDGITN KVNSVIEKMN TQFEAVGKEF SNLERRLENL
NKKMEDGFLD VWTYNAELLV LMENERTLDF HDSNVKNLYD KVRMQLRDNV KELGNGCFEF
YHKCDDECMN SVKNGTYDYP KYEEESKLNR NEIKGVKLSS MGVYQILAIY ATVAGSLSLA
IMMAGISFWM CSNGSLQCRI CI
