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P18875

- HEMA_I79A4

UniProt

P18875 - HEMA_I79A4

Protein

Hemagglutinin

Gene

HA

Organism
Influenza A virus (strain A/Kiev/59/1979 H1N1)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      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
    Sitei344 – 3452Cleavage; 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: 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/Kiev/59/1979 H1N1)
    Taxonomic identifieri384495 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
    Virus hostiAves [TaxID: 8782]
    Homo sapiens (Human) [TaxID: 9606]
    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 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 343326Hemagglutinin HA1 chainPRO_0000039012Add
    BLAST
    Chaini345 – 566222Hemagglutinin HA2 chainPRO_0000039013Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi21 ↔ 481Interchain (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 ↔ 292By similarity
    Disulfide bondi72 ↔ 84By similarity
    Glycosylationi104 – 1041N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi144 – 1441N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi172 – 1721N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi177 – 1771N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi286 – 2861N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi296 ↔ 320By similarity
    Glycosylationi304 – 3041N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi488 ↔ 492By similarity
    Glycosylationi498 – 4981N-linked (GlcNAc...); by hostSequence Analysis
    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 By similarity.By similarity
    Palmitoylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Interactioni

    Subunit structurei

    Homotrimer of disulfide-linked HA1-HA2.

    Structurei

    Secondary structure

    1
    566
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni351 – 3533
    Beta strandi365 – 3684
    Helixi382 – 40221
    Helixi419 – 47052
    Beta strandi473 – 4786
    Beta strandi481 – 4866
    Helixi490 – 4978

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RUYX-ray2.70I/K/M345-504[»]
    ProteinModelPortaliP18875.
    SMRiP18875. Positions 18-340, 345-519.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP18875.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini18 – 529512ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini551 – 56616CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei530 – 55021HelicalSequence 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.

    P18875-1 [UniParc]FASTAAdd to Basket

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    MKAKLLVLLC ALSATDADTI CIGYHANNST DTVDTVLEKN VTVTHSVNLL    50
    EDSHNGKLCR LKGIAPLQLG KCSIAGWILG NPECESLFSK KSWSYIAETP 100
    NSENGTCYPG YFADYEELRE QLSSVSSFER FEIFPKERSW PKHNVTRGVT 150
    ASCSHKGKSS FYRNLLWLTE KNGSYPNLSK SYVNNKEKEV LVLWGVHHPS 200
    NIEDQKTIYR KENAYVSVVS SNYNRRFTPE IAKRPKVRGQ EGRINYYWTL 250
    LEPGDTIIFE ANGNLIAPWY AFALSRGFGS GIITSNASMD ECDTKCQTPQ 300
    GAINSSLPFQ NVHPVTIGEC PKYVRSTKLR MVTGLRNIPS IQSRGLFGAI 350
    AGFIEGGWTG MIDGWYGYHH QNEQGSGYAA DQKSTQNAIN GITNKVNSVI 400
    EKMNTQFTAV GKEFNKLEKR MENLNKKVDD GFLDIWTYNA ELLVLLENER 450
    TLDFHDSNVK NLYEKVKSQL KNNAKEIGNG CFEFYHKCNN ECMESVKNGT 500
    YDYPKYSEES KLNREKIDGV KLESMGVYQI LAIYSTVASS LCLLVSLGAI 550
    SFWMCSNGSL QCRICI 566
    Length:566
    Mass (Da):63,606
    Last modified:November 1, 1990 - v1
    Checksum:iA78A51A4F84D9E74
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M38353 Genomic RNA. Translation: AAA43172.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M38353 Genomic RNA. Translation: AAA43172.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RUY X-ray 2.70 I/K/M 345-504 [» ]
    ProteinModelPortali P18875.
    SMRi P18875. Positions 18-340, 345-519.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P18875.

    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. "Primary structure of the full-size DNA copy of the hemagglutinin gene of influenza virus A/Kiev/59/79 (H1N1)."
      Beklemishev A.B., Blinov V.M., Vasilenko S.K., Golovin S.Y., Karginov V.A., Mamayev L.V.
      Bioorg. Khim. 12:375-381(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiHEMA_I79A4
    AccessioniPrimary (citable) accession number: P18875
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 96 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