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P03437

- HEMA_I68A0

UniProt

P03437 - HEMA_I68A0

Protein

Hemagglutinin

Gene

HA

Organism
Influenza A virus (strain A/Aichi/2/1968 H3N2)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei345 – 3462Cleavage; by host

    GO - Biological processi

    1. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
    2. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
    3. fusion of virus membrane with host plasma membrane Source: InterPro
    4. virion attachment to host cell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hemagglutinin

    Keywords - Biological processi

    Clathrin- and caveolin-independent endocytosis of virus by host, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus endocytosis by host, Virus entry into host cell

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hemagglutinin
    Cleaved into the following 2 chains:
    Gene namesi
    Name:HA
    OrganismiInfluenza A virus (strain A/Aichi/2/1968 H3N2)
    Taxonomic identifieri387139 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
    Virus hostiAves [TaxID: 8782]
    Cetacea (whales) [TaxID: 9721]
    Homo sapiens (Human) [TaxID: 9606]
    Phocidae (true seals) [TaxID: 9709]
    Sus scrofa (Pig) [TaxID: 9823]

    Subcellular locationi

    Virion membrane Curated; Single-pass type I membrane protein Curated. Host apical cell membrane; Single-pass type I membrane protein
    Note: Targeted to the apical plasma membrane in epithelial polarized cells through a signal present in the transmembrane domain. Associated with glycosphingolipid- and cholesterol-enriched detergent-resistant lipid rafts.

    GO - Cellular componenti

    1. host cell plasma membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. viral envelope Source: UniProtKB-KW
    4. virion membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 344328Hemagglutinin HA1 chainPRO_0000038885Add
    BLAST
    Chaini346 – 566221Hemagglutinin HA2 chainPRO_0000038886Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi24 – 241N-linked (GlcNAc...); by host
    Disulfide bondi30 ↔ 482Interchain (between HA1 and HA2 chains)
    Glycosylationi38 – 381N-linked (GlcNAc...); by host
    Glycosylationi54 – 541N-linked (GlcNAc...); by host
    Disulfide bondi68 ↔ 293
    Disulfide bondi80 ↔ 92
    Glycosylationi97 – 971N-linked (GlcNAc...); by host
    Disulfide bondi113 ↔ 155
    Glycosylationi181 – 1811N-linked (GlcNAc...); by host
    Disulfide bondi297 ↔ 321
    Glycosylationi301 – 3011N-linked (GlcNAc...); by host
    Disulfide bondi489 ↔ 493
    Glycosylationi499 – 4991N-linked (GlcNAc...); by host
    Lipidationi555 – 5551S-palmitoyl cysteine; by hostBy similarity
    Lipidationi562 – 5621S-palmitoyl cysteine; by hostBy similarity
    Lipidationi565 – 5651S-palmitoyl cysteine; by hostBy similarity

    Post-translational modificationi

    In natural infection, inactive HA is matured into HA1 and HA2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in this process is secreted in lungs by Clara cells.1 Publication
    Palmitoylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Interactioni

    Subunit structurei

    Homotrimer of disulfide-linked HA1-HA2.

    Protein-protein interaction databases

    DIPiDIP-45342N.
    IntActiP03437. 1 interaction.

    Structurei

    Secondary structure

    1
    566
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi27 – 359
    Beta strandi40 – 423
    Beta strandi50 – 534
    Beta strandi55 – 573
    Beta strandi65 – 728
    Beta strandi74 – 763
    Helixi82 – 876
    Helixi90 – 956
    Beta strandi101 – 1055
    Helixi121 – 13111
    Beta strandi136 – 1383
    Turni144 – 1463
    Beta strandi152 – 1576
    Beta strandi160 – 1623
    Beta strandi167 – 1693
    Beta strandi171 – 1733
    Beta strandi180 – 1856
    Beta strandi188 – 1903
    Beta strandi192 – 2009
    Helixi204 – 2118
    Beta strandi212 – 2154
    Beta strandi217 – 2215
    Beta strandi226 – 2294
    Beta strandi245 – 2539
    Beta strandi258 – 2658
    Beta strandi267 – 2704
    Beta strandi272 – 2754
    Beta strandi282 – 2854
    Beta strandi290 – 2945
    Beta strandi296 – 2994
    Beta strandi302 – 3043
    Beta strandi307 – 3115
    Beta strandi318 – 3203
    Beta strandi331 – 3333
    Beta strandi337 – 3393
    Turni352 – 3543
    Beta strandi366 – 3738
    Beta strandi376 – 3827
    Helixi383 – 44967
    Beta strandi455 – 4573
    Helixi458 – 47013
    Helixi472 – 4743
    Beta strandi475 – 4773
    Beta strandi479 – 4846
    Helixi491 – 4999
    Helixi504 – 51512
    Turni516 – 5194

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EO8X-ray2.80A17-344[»]
    B346-520[»]
    1FYTX-ray2.60C322-334[»]
    1HA0X-ray2.80A25-518[»]
    1HGGX-ray2.90A/C/E17-344[»]
    B/D/F346-520[»]
    1HTMX-ray2.50A/C/E17-43[»]
    B/D/F383-520[»]
    1J8HX-ray2.40C322-334[»]
    1QU1X-ray1.90A/B/C/D/E/F376-530[»]
    2HMGX-ray3.00A/C/E17-344[»]
    B/D/F346-520[»]
    2VIRX-ray3.25C44-325[»]
    2VISX-ray3.25C44-325[»]
    2VITX-ray3.25C44-325[»]
    2VIUX-ray2.50A17-344[»]
    B346-520[»]
    2YPGX-ray2.85A/C/E17-344[»]
    B/D/F346-520[»]
    3EYMX-ray2.80A/C/E25-345[»]
    B/D/F346-517[»]
    3HMGX-ray2.90A/C/E17-344[»]
    B/D/F346-520[»]
    3S4SX-ray2.40C/F322-334[»]
    3S5LX-ray2.10C/F322-334[»]
    3VUNX-ray3.00A/C/E17-345[»]
    B/D/F346-520[»]
    4HMGX-ray3.00A/C/E17-344[»]
    B/D/F346-520[»]
    5HMGX-ray3.20A/C/E17-344[»]
    B/D/F346-520[»]
    ProteinModelPortaliP03437.
    SMRiP03437. Positions 17-520.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03437.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini17 – 530514ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini552 – 56615CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei531 – 55121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Family and domain databases

    Gene3Di2.10.77.10. 1 hit.
    3.90.20.10. 1 hit.
    3.90.209.20. 1 hit.
    InterProiIPR008980. Capsid_hemagglutn.
    IPR013828. Hemagglutn_HA1_a/b_dom.
    IPR013827. Hemagglutn_HA1_b-rbn_dom.
    IPR000149. Hemagglutn_influenz_A.
    IPR001364. Hemagglutn_influenz_A/B.
    IPR013829. Hemagglutn_stalk.
    [Graphical view]
    PfamiPF00509. Hemagglutinin. 1 hit.
    [Graphical view]
    PRINTSiPR00330. HEMAGGLUTN1.
    PR00329. HEMAGGLUTN12.
    SUPFAMiSSF49818. SSF49818. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P03437-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTIIALSYI FCLALGQDLP GNDNSTATLC LGHHAVPNGT LVKTITDDQI    50
    EVTNATELVQ SSSTGKICNN PHRILDGIDC TLIDALLGDP HCDVFQNETW 100
    DLFVERSKAF SNCYPYDVPD YASLRSLVAS SGTLEFITEG FTWTGVTQNG 150
    GSNACKRGPG SGFFSRLNWL TKSGSTYPVL NVTMPNNDNF DKLYIWGIHH 200
    PSTNQEQTSL YVQASGRVTV STRRSQQTII PNIGSRPWVR GLSSRISIYW 250
    TIVKPGDVLV INSNGNLIAP RGYFKMRTGK SSIMRSDAPI DTCISECITP 300
    NGSIPNDKPF QNVNKITYGA CPKYVKQNTL KLATGMRNVP EKQTRGLFGA 350
    IAGFIENGWE GMIDGWYGFR HQNSEGTGQA ADLKSTQAAI DQINGKLNRV 400
    IEKTNEKFHQ IEKEFSEVEG RIQDLEKYVE DTKIDLWSYN AELLVALENQ 450
    HTIDLTDSEM NKLFEKTRRQ LRENAEEMGN GCFKIYHKCD NACIESIRNG 500
    TYDHDVYRDE ALNNRFQIKG VELKSGYKDW ILWISFAISC FLLCVVLLGF 550
    IMWACQRGNI RCNICI 566
    Length:566
    Mass (Da):63,416
    Last modified:July 21, 1986 - v1
    Checksum:iE395659C23CAFECA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141A → P in AAA43239. 1 PublicationCurated
    Sequence conflicti15 – 151L → I in BAF37221. (PubMed:15331693)Curated
    Sequence conflicti160 – 1601G → S in BAF37221. (PubMed:15331693)Curated
    Sequence conflicti198 – 1981I → V in BAF37221. (PubMed:15331693)Curated
    Sequence conflicti240 – 2401R → G in BAF37221. (PubMed:15331693)Curated
    Sequence conflicti477 – 4771E → D in BAF37221. (PubMed:15331693)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02090 Genomic RNA. Translation: AAA43178.1.
    V01085 Genomic RNA. Translation: CAA24269.1.
    M55059 Genomic RNA. Translation: AAA43239.1.
    AB284320 Genomic RNA. Translation: BAF37221.1.
    PIRiA93231. HMIVHA.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02090 Genomic RNA. Translation: AAA43178.1 .
    V01085 Genomic RNA. Translation: CAA24269.1 .
    M55059 Genomic RNA. Translation: AAA43239.1 .
    AB284320 Genomic RNA. Translation: BAF37221.1 .
    PIRi A93231. HMIVHA.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EO8 X-ray 2.80 A 17-344 [» ]
    B 346-520 [» ]
    1FYT X-ray 2.60 C 322-334 [» ]
    1HA0 X-ray 2.80 A 25-518 [» ]
    1HGG X-ray 2.90 A/C/E 17-344 [» ]
    B/D/F 346-520 [» ]
    1HTM X-ray 2.50 A/C/E 17-43 [» ]
    B/D/F 383-520 [» ]
    1J8H X-ray 2.40 C 322-334 [» ]
    1QU1 X-ray 1.90 A/B/C/D/E/F 376-530 [» ]
    2HMG X-ray 3.00 A/C/E 17-344 [» ]
    B/D/F 346-520 [» ]
    2VIR X-ray 3.25 C 44-325 [» ]
    2VIS X-ray 3.25 C 44-325 [» ]
    2VIT X-ray 3.25 C 44-325 [» ]
    2VIU X-ray 2.50 A 17-344 [» ]
    B 346-520 [» ]
    2YPG X-ray 2.85 A/C/E 17-344 [» ]
    B/D/F 346-520 [» ]
    3EYM X-ray 2.80 A/C/E 25-345 [» ]
    B/D/F 346-517 [» ]
    3HMG X-ray 2.90 A/C/E 17-344 [» ]
    B/D/F 346-520 [» ]
    3S4S X-ray 2.40 C/F 322-334 [» ]
    3S5L X-ray 2.10 C/F 322-334 [» ]
    3VUN X-ray 3.00 A/C/E 17-345 [» ]
    B/D/F 346-520 [» ]
    4HMG X-ray 3.00 A/C/E 17-344 [» ]
    B/D/F 346-520 [» ]
    5HMG X-ray 3.20 A/C/E 17-344 [» ]
    B/D/F 346-520 [» ]
    ProteinModelPortali P03437.
    SMRi P03437. Positions 17-520.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-45342N.
    IntActi P03437. 1 interaction.

    Chemistry

    BindingDBi P03437.
    ChEMBLi CHEMBL1932897.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P03437.

    Family and domain databases

    Gene3Di 2.10.77.10. 1 hit.
    3.90.20.10. 1 hit.
    3.90.209.20. 1 hit.
    InterProi IPR008980. Capsid_hemagglutn.
    IPR013828. Hemagglutn_HA1_a/b_dom.
    IPR013827. Hemagglutn_HA1_b-rbn_dom.
    IPR000149. Hemagglutn_influenz_A.
    IPR001364. Hemagglutn_influenz_A/B.
    IPR013829. Hemagglutn_stalk.
    [Graphical view ]
    Pfami PF00509. Hemagglutinin. 1 hit.
    [Graphical view ]
    PRINTSi PR00330. HEMAGGLUTN1.
    PR00329. HEMAGGLUTN12.
    SUPFAMi SSF49818. SSF49818. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Antigenic drift between the haemagglutinin of the Hong Kong influenza strains A/Aichi/2/68 and A/Victoria/3/75."
      Verhoeyen M., Fang R., Jou W.M., Devos R., Huylebroeck D., Saman E., Fiers W.
      Nature 286:771-776(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Shift and drift in influenza viruses."
      Min J.W., Verhoeyen M., Fang R.-X., Devos R., Huylebroeck D., Fiers W.
      (In) Carlile M.J., Collins J.F., Moseley B.E.B. (eds.); Symposium of the Society for General Microbiology, pp.285-311, Cambridge University Press, New York (1981)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Effect of the addition of oligosaccharides on the biological activities and antigenicity of influenza A/H3N2 virus hemagglutinin."
      Abe Y., Takashita E., Sugawara K., Matsuzaki Y., Muraki Y., Hongo S.
      J. Virol. 78:9605-9611(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    4. "Human mucus protease inhibitor in airway fluids is a potential defensive compound against infection with influenza A and Sendai viruses."
      Beppu Y., Imamura Y., Tashiro M., Towatari T., Ariga H., Kido H.
      J. Biochem. 121:309-316(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE.
    5. "Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3-A resolution."
      Wilson I.A., Skehel J.J., Wiley D.C.
      Nature 289:366-373(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    6. "Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid."
      Weis W.I., Brown J.H., Cusack S.C., Paulson J.C., Skehel J.J., Wiley D.C.
      Nature 333:426-431(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
    7. "The structure of a membrane fusion mutant of the influenza virus haemagglutinin."
      Weis W.I., Cusack S.C., Brown J.H., Daniels R.S., Skehel J.J., Wiley D.C.
      EMBO J. 9:17-24(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF A MUTANT WITH GLY-457.
    8. "Refinement of the influenza virus hemagglutinin by simulated annealing."
      Weis W.I., Bruenger A.T., Skehel J.J., Wiley D.C.
      J. Mol. Biol. 212:737-761(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
    9. "Structure of influenza haemagglutinin at the pH of membrane fusion."
      Bullough P.A., Hughson F.M., Skehel J.J., Wiley D.C.
      Nature 371:37-43(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    10. "Antigen distortion allows influenza virus to escape neutralization."
      Fleury D., Wharton S.A., Skehel J.J., Knossow M., Bizebard T.
      Nat. Struct. Biol. 5:119-123(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS).

    Entry informationi

    Entry nameiHEMA_I68A0
    AccessioniPrimary (citable) accession number: P03437
    Secondary accession number(s): A0PC85, Q67132
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Major glycoprotein, comprises over 80% of the envelope proteins present in virus particle.
    The extent of infection into host organism is determined by HA. Influenza viruses bud from the apical surface of polarized epithelial cells (e.g. bronchial epithelial cells) into lumen of lungs and are therefore usually pneumotropic. The reason is that HA is cleaved by tryptase clara which is restricted to lungs. However, HAs of H5 and H7 pantropic avian viruses subtypes can be cleaved by furin and subtilisin-type enzymes, allowing the virus to grow in other organs than lungs.
    The influenza A genome consist of 8 RNA segments. Genetic variation of hemagglutinin and/or neuraminidase genes results in the emergence of new influenza strains. The mechanism of variation can be the result of point mutations or the result of genetic reassortment between segments of two different strains.

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3