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Q9WCD9

- HEMA_I30A0

UniProt

Q9WCD9 - HEMA_I30A0

Protein

Hemagglutinin

Gene

HA

Organism
Influenza A virus (strain A/Swine/Iowa/15/1930 H1N1)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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 By similarity.By similarity

    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/Swine/Iowa/15/1930 H1N1)
    Taxonomic identifieri380342 [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 By similarity.By similarity

    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_5000055153Add
    BLAST
    Chaini345 – 566222Hemagglutinin HA2 chainPRO_5000055154Add
    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
    Disulfide bondi107 ↔ 153By similarity
    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.By similarity

    Structurei

    Secondary structure

    1
    566
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 257
    Beta strandi39 – 446
    Beta strandi46 – 483
    Beta strandi58 – 614
    Beta strandi67 – 704
    Helixi74 – 796
    Helixi82 – 898
    Beta strandi96 – 983
    Helixi115 – 1228
    Beta strandi125 – 1317
    Turni136 – 1383
    Beta strandi150 – 1556
    Beta strandi158 – 1603
    Beta strandi163 – 1675
    Beta strandi178 – 1836
    Beta strandi186 – 1883
    Beta strandi190 – 1989
    Helixi202 – 2098
    Beta strandi216 – 2194
    Beta strandi224 – 2274
    Beta strandi240 – 25112
    Beta strandi256 – 2638
    Beta strandi265 – 2684
    Beta strandi271 – 2766
    Beta strandi282 – 2843
    Beta strandi289 – 2935
    Beta strandi295 – 2984
    Beta strandi301 – 3033
    Beta strandi308 – 3103
    Beta strandi316 – 3205
    Beta strandi330 – 3323

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RUYX-ray2.70H/J/L18-339[»]
    ProteinModelPortaliQ9WCD9.
    SMRiQ9WCD9. Positions 345-519.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9WCD9.

    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.

    Q9WCD9-1 [UniParc]FASTAAdd to Basket

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    MKAILLVLLC AFAATNADTL CIGYHANNST DTVDTVLEKN VTVTHSVNLL    50
    EDSHNGKLCR LGGIAPLQLG KCNIAGXXLG NPECDLLLTV SSWSYIVETS 100
    NSDNGTCYPG DFIDYEELRE QLSSVSSFEK FEIFPKTSSW PNHETTRGVT 150
    AACPYAGASS FYRNLLWLVK KENSYPKLSK SYVNNKGKEV LVLWGVHHPP 200
    TSTDQQSLYQ NADAYVSVGS SKYDRRFTPE IAARPKVRGQ AGRMNYYWTL 250
    LEPGDTITFE ATGNLVAPRY AFALNRGSES GIITSDAPVH DCDTKCQTPH 300
    GAINSSLPFQ NIHPVTIGEC PKYVKSTKLR MVTGLRNIPS IQSRGLFGAI 350
    AGFIEGGWTG LIDGWYGYHH QNGQGSGYAA DQKSTQNAID GITNKVNSVI 400
    EKMNTQFTVV GKEFNNLERR IKNLNKKVDD GFLDVWTYNA EMLVLLENER 450
    TLDFHDSNVK NLYEKARSQL RNNAKEIGNG CFEFYHKCDD ACMESVRNGT 500
    YDYPKYSEES KLNREEIDGV KLESMMVYQI LAIYSTVASS LVLLVSLGAI 550
    SFWMCSNGSL QCRICI 566
    Length:566
    Mass (Da):62,868
    Last modified:November 1, 1999 - v1
    Checksum:iDF84450D8446B949
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF091308 mRNA. Translation: AAD25303.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF091308 mRNA. Translation: AAD25303.1 .

    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 H/J/L 18-339 [» ]
    ProteinModelPortali Q9WCD9.
    SMRi Q9WCD9. Positions 345-519.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q9WCD9.

    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. "Molecular basis for the generation in pigs of influenza A viruses with pandemic potential."
      Ito T., Couceiro J.N., Kelm S., Baum L.G., Krauss S., Castrucci M.R., Donatelli I., Kida H., Paulson J.C., Webster R.G., Kawaoka Y.
      J. Virol. 72:7367-7373(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiHEMA_I30A0
    AccessioniPrimary (citable) accession number: Q9WCD9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2007
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 79 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