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P03452

- HEMA_I34A1

UniProt

P03452 - HEMA_I34A1

Protein

Hemagglutinin

Gene

HA

Organism
Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (06 Mar 2007)
      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
    Sitei343 – 3442Cleavage; by hostBy similarity

    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: Reactome
    4. intracellular transport of viral protein in host cell Source: Reactome
    5. receptor-mediated endocytosis of virus by host cell Source: Reactome
    6. uncoating of virus Source: Reactome
    7. viral entry into host cell Source: Reactome
    8. viral genome packaging Source: Reactome
    9. viral life cycle Source: Reactome
    10. viral process Source: Reactome
    11. viral release from host cell Source: Reactome
    12. viral transcription Source: Reactome
    13. virion assembly Source: Reactome
    14. 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

    Enzyme and pathway databases

    ReactomeiREACT_6145. Influenza Life Cycle.
    REACT_6147. Entry of Influenza Virion into Host Cell via Endocytosis.
    REACT_6212. Budding.
    REACT_6215. Transport of HA trimer, NA tetramer and M2 tetramer from the endoplasmic reticulum to the Golgi Apparatus.
    REACT_6235. Packaging of Eight RNA Segments.
    REACT_6277. Assembly of Viral Components at the Budding Site.
    REACT_6321. Uncoating of the Influenza Virion.
    REACT_6326. Release.
    REACT_6351. Fusion of the Influenza Virion to the Host Cell Endosome.
    REACT_9491. Viral mRNA Translation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hemagglutinin
    Cleaved into the following 2 chains:
    Gene namesi
    Name:HA
    OrganismiInfluenza A virus (strain A/Puerto Rico/8/1934 H1N1)
    Taxonomic identifieri211044 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
    Virus hostiAves [TaxID: 8782]
    Homo sapiens (Human) [TaxID: 9606]
    Sus scrofa (Pig) [TaxID: 9823]
    ProteomesiUP000009255: Genome

    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. endocytic vesicle membrane Source: Reactome
    2. endoplasmic reticulum membrane Source: Reactome
    3. endosome lumen Source: Reactome
    4. extracellular region Source: Reactome
    5. Golgi membrane Source: Reactome
    6. host cell plasma membrane Source: UniProtKB-SubCell
    7. integral component of membrane Source: UniProtKB-KW
    8. plasma membrane Source: Reactome
    9. viral envelope Source: UniProtKB-KW
    10. 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 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 342325Hemagglutinin HA1 chainPRO_0000039034Add
    BLAST
    Chaini344 – 565222Hemagglutinin HA2 chainPRO_0000039035Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi21 ↔ 480Interchain (between HA1 and HA2 chains)By similarity
    Glycosylationi27 – 271N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi28 – 281N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi40 – 401N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi59 ↔ 291By similarity
    Disulfide bondi72 ↔ 84By similarity
    Disulfide bondi107 ↔ 152By similarity
    Glycosylationi285 – 2851N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi295 ↔ 319By similarity
    Glycosylationi303 – 3031N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi487 ↔ 491By similarity
    Glycosylationi497 – 4971N-linked (GlcNAc...); by hostSequence Analysis
    Lipidationi554 – 5541S-palmitoyl cysteine; by hostBy similarity
    Lipidationi561 – 5611S-palmitoyl cysteine; by hostBy similarity
    Lipidationi564 – 5641S-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 By similarity.By similarity
    Palmitoylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Interactioni

    Subunit structurei

    Homotrimer of disulfide-linked HA1-HA2.

    Protein-protein interaction databases

    IntActiP03452. 8 interactions.
    MINTiMINT-3375119.

    Structurei

    Secondary structure

    1
    565
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 257
    Beta strandi39 – 446
    Beta strandi46 – 483
    Beta strandi56 – 616
    Beta strandi67 – 704
    Helixi74 – 796
    Helixi82 – 876
    Beta strandi94 – 985
    Beta strandi107 – 1104
    Helixi115 – 1228
    Beta strandi125 – 13410
    Turni136 – 1383
    Beta strandi149 – 1546
    Beta strandi157 – 1593
    Beta strandi162 – 1665
    Beta strandi170 – 1723
    Beta strandi177 – 1826
    Beta strandi185 – 19713
    Helixi201 – 2088
    Beta strandi215 – 2184
    Beta strandi223 – 2264
    Beta strandi242 – 2509
    Beta strandi255 – 2628
    Beta strandi264 – 27512
    Beta strandi281 – 2833
    Beta strandi288 – 29710
    Beta strandi300 – 3023
    Beta strandi307 – 3093
    Beta strandi315 – 3195
    Beta strandi329 – 3313
    Turni350 – 3523
    Beta strandi364 – 3674
    Beta strandi376 – 3794
    Helixi381 – 40121
    Beta strandi405 – 4084
    Helixi418 – 46952
    Beta strandi472 – 4754
    Beta strandi477 – 4859
    Helixi491 – 4966

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RU7X-ray2.30A/C/E/G/I/K18-338[»]
    B/D/F/H/J/L344-503[»]
    1RVXX-ray2.20A/C/E/G/I/K14-338[»]
    B/D/F/H/J/L344-503[»]
    1RVZX-ray2.25A/C/E/G/I/K14-338[»]
    B/D/F/H/J/L344-503[»]
    ProteinModelPortaliP03452.
    SMRiP03452. Positions 18-339, 344-518.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03452.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini18 – 528511ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini550 – 56516CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei529 – 54921HelicalSequence 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.

    P03452-1 [UniParc]FASTAAdd to Basket

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    MKANLLVLLC ALAAADADTI CIGYHANNST DTVDTVLEKN VTVTHSVNLL    50
    EDSHNGKLCR LKGIAPLQLG KCNIAGWLLG NPECDPLLPV RSWSYIVETP 100
    NSENGICYPG DFIDYEELRE QLSSVSSFER FEIFPKESSW PNHNTNGVTA 150
    ACSHEGKSSF YRNLLWLTEK EGSYPKLKNS YVNKKGKEVL VLWGIHHPPN 200
    SKEQQNLYQN ENAYVSVVTS NYNRRFTPEI AERPKVRDQA GRMNYYWTLL 250
    KPGDTIIFEA NGNLIAPMYA FALSRGFGSG IITSNASMHE CNTKCQTPLG 300
    AINSSLPYQN IHPVTIGECP KYVRSAKLRM VTGLRNIPSI QSRGLFGAIA 350
    GFIEGGWTGM IDGWYGYHHQ NEQGSGYAAD QKSTQNAING ITNKVNTVIE 400
    KMNIQFTAVG KEFNKLEKRM ENLNKKVDDG FLDIWTYNAE LLVLLENERT 450
    LDFHDSNVKN LYEKVKSQLK NNAKEIGNGC FEFYHKCDNE CMESVRNGTY 500
    DYPKYSEESK LNREKVDGVK LESMGIYQIL AIYSTVASSL VLLVSLGAIS 550
    FWMCSNGSLQ CRICI 565
    Length:565
    Mass (Da):63,353
    Last modified:March 6, 2007 - v2
    Checksum:i47F34821748F494E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101C → S in AAM75158. (PubMed:11779399)Curated
    Sequence conflicti146 – 1461N → TK in CAA24272. (PubMed:7278968)Curated
    Sequence conflicti155 – 1551E → A in CAA24272. (PubMed:7278968)Curated
    Sequence conflicti199 – 1991P → S in CAA24272. (PubMed:7278968)Curated
    Sequence conflicti203 – 2031E → D in CAA24272. (PubMed:7278968)Curated
    Sequence conflicti207 – 2071L → I in CAA24272. (PubMed:7278968)Curated
    Sequence conflicti207 – 2071L → I in AAM75158. (PubMed:11779399)Curated
    Sequence conflicti268 – 2681M → R in CAA24272. (PubMed:7278968)Curated
    Sequence conflicti308 – 3081Y → F in CAA24272. (PubMed:7278968)Curated
    Sequence conflicti337 – 3371I → N in ABO21709. (PubMed:15163504)Curated
    Sequence conflicti397 – 3971T → S in CAA24272. (PubMed:7278968)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01088 Genomic RNA. Translation: CAA24272.1.
    AF389118 Genomic RNA. Translation: AAM75158.1.
    EF467821 Genomic RNA. Translation: ABO21709.1.
    CY009444 Genomic RNA. Translation: ABD77675.1.
    J02144 Genomic RNA. Translation: AAA43194.1.
    RefSeqiNP_040980.1. NC_002017.1.

    Genome annotation databases

    GeneIDi956529.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01088 Genomic RNA. Translation: CAA24272.1 .
    AF389118 Genomic RNA. Translation: AAM75158.1 .
    EF467821 Genomic RNA. Translation: ABO21709.1 .
    CY009444 Genomic RNA. Translation: ABD77675.1 .
    J02144 Genomic RNA. Translation: AAA43194.1 .
    RefSeqi NP_040980.1. NC_002017.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RU7 X-ray 2.30 A/C/E/G/I/K 18-338 [» ]
    B/D/F/H/J/L 344-503 [» ]
    1RVX X-ray 2.20 A/C/E/G/I/K 14-338 [» ]
    B/D/F/H/J/L 344-503 [» ]
    1RVZ X-ray 2.25 A/C/E/G/I/K 14-338 [» ]
    B/D/F/H/J/L 344-503 [» ]
    ProteinModelPortali P03452.
    SMRi P03452. Positions 18-339, 344-518.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P03452. 8 interactions.
    MINTi MINT-3375119.

    Chemistry

    BindingDBi P03452.
    ChEMBLi CHEMBL1075313.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 956529.

    Enzyme and pathway databases

    Reactomei REACT_6145. Influenza Life Cycle.
    REACT_6147. Entry of Influenza Virion into Host Cell via Endocytosis.
    REACT_6212. Budding.
    REACT_6215. Transport of HA trimer, NA tetramer and M2 tetramer from the endoplasmic reticulum to the Golgi Apparatus.
    REACT_6235. Packaging of Eight RNA Segments.
    REACT_6277. Assembly of Viral Components at the Budding Site.
    REACT_6321. Uncoating of the Influenza Virion.
    REACT_6326. Release.
    REACT_6351. Fusion of the Influenza Virion to the Host Cell Endosome.
    REACT_9491. Viral mRNA Translation.

    Miscellaneous databases

    EvolutionaryTracei P03452.

    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. "Nucleotide sequence of the haemagglutinin gene of a human influenza virus H1 subtype."
      Winter G., Fields S., Brownlee G.G.
      Nature 292:72-75(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Efficient generation and growth of influenza virus A/PR/8/34 from eight cDNA fragments."
      de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F., Osterhaus A.D.M.E., Fouchier R.A.M.
      Virus Res. 103:155-161(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], REVERSE GENETICS.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate EE12/E1.
    5. "The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype)."
      Caton A.J., Brownlee G.G., Yewdell J.W., Gerhard W.
      Cell 31:417-427(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 18-343.

    Entry informationi

    Entry nameiHEMA_I34A1
    AccessioniPrimary (citable) accession number: P03452
    Secondary accession number(s): A4GXH4
    , Q20N38, Q83964, Q8JUU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 119 of the entry and version 2 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, Complete proteome, Reference proteome

    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