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C7S226

- C7S226_I57A0

UniProt

C7S226 - C7S226_I57A0

Protein
Submitted name:

Hemagglutinin

Gene

HA

Organism
Influenza A virus (strain A/Japan/305/1957 H2N2)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (13 Oct 2009)
      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.UniRule annotationSAAS annotation

    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

    HemagglutininUniRule annotationSAAS annotation

    Keywords - Biological processi

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

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    HemagglutininImported
    Gene namesi
    Name:HAImported
    OrganismiInfluenza A virus (strain A/Japan/305/1957 H2N2)Imported
    Taxonomic identifieri387161 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
    Virus hostiAves [TaxID: 8782]
    Homo sapiens (Human) [TaxID: 9606]

    Subcellular locationi

    Virion membrane SAAS annotation; Single-pass type I membrane protein SAAS annotation. Host apical cell membrane SAAS annotation; Single-pass type I membrane protein SAAS annotation

    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 membraneSAAS annotation, Host membrane, Membrane, Viral envelope proteinUniRule annotationSAAS annotation, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1515 PotentialImportedAdd
    BLAST
    Chaini16 – 562547 PotentialImportedPRO_5000514962Add
    BLAST
    Chaini16 – 340325HA1ImportedPRO_5000514963Add
    BLAST
    Chaini341 – 562222HA2ImportedPRO_5000514964Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi26 – 261N-linked (GlcNAc...)Imported
    Glycosylationi38 – 381N-linked (GlcNAc...)Imported
    Glycosylationi179 – 1791N-linked (GlcNAc...)Imported
    Glycosylationi300 – 3001N-linked (GlcNAc...)Imported
    Glycosylationi494 – 4941N-linked (GlcNAc...)Imported

    Keywords - PTMi

    Disulfide bondSAAS annotation

    Interactioni

    Subunit structurei

    Homotrimer of disulfide-linked HA1-HA2.UniRule annotationSAAS annotation

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KU3X-ray1.60A15-340[»]
    B341-514[»]
    3KU5X-ray1.73A15-340[»]
    B341-514[»]
    3KU6X-ray1.75A15-340[»]
    B341-514[»]
    3QQBX-ray1.97A15-340[»]
    B341-514[»]
    3QQEX-ray2.10A15-340[»]
    B341-514[»]
    3QQIX-ray1.65A/B61-279[»]
    3QQOX-ray2.90A/C/E15-340[»]
    B/D/F341-514[»]
    4HF5X-ray3.00A15-340[»]
    B341-514[»]
    4HLZX-ray2.90A/C/E15-340[»]
    B/D/F341-514[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiC7S226.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the influenza viruses hemagglutinin family.UniRule annotation

    Keywords - Domaini

    SignalImported, Transmembrane, Transmembrane helixSAAS annotation

    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.

    C7S226-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAIIYLILLF TAVRGDQICI GYHANNSTEK VDTILERNVT VTHAKDILEK    50
    THNGKLCKLN GIPPLELGDC SIAGWLLGNP ECDRLLSVPE WSYIMEKENP 100
    RDGLCYPGSF NDYEELKHLL SSVKHFEKVK ILPKDRWTQH TTTGGSRACA 150
    VSGNPSFFRN MVWLTEKGSN YPVAKGSYNN TSGEQMLIIW GVHHPNDETE 200
    QRTLYQNVGT YVSVGTSTLN KRSTPEIATR PKVNGQGGRM EFSWTLLDMW 250
    DTINFESTGN LIAPEYGFKI SKRGSSGIMK TEGTLENCET KCQTPLGAIN 300
    TTLPFHNVHP LTIGECPKYV KSEKLVLATG LRNVPQIESR GLFGAIAGFI 350
    EGGWQGMVDG WYGYHHSNDQ GSGYAADKES TQKAFDGITN KVNSVIEKMN 400
    TQFEAVGKEF SNLERRLENL NKKMEDGFLD VWTYNAELLV LMENERTLDF 450
    HDSNVKNLYD KVRMQLRDNV KELGNGCFEF YHKCDDECMN SVKNGTYDYP 500
    KYEEESKLNR NEIKGVKLSS MGVYQILAIY ATVAGSLSLA IMMAGISFWM 550
    CSNGSLQCRI CI 562
    Length:562
    Mass (Da):63,120
    Last modified:October 13, 2009 - v1
    Checksum:iD4747A6A6733E733
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CY045804 Viral cRNA. Translation: ACV49600.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CY045804 Viral cRNA. Translation: ACV49600.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3KU3 X-ray 1.60 A 15-340 [» ]
    B 341-514 [» ]
    3KU5 X-ray 1.73 A 15-340 [» ]
    B 341-514 [» ]
    3KU6 X-ray 1.75 A 15-340 [» ]
    B 341-514 [» ]
    3QQB X-ray 1.97 A 15-340 [» ]
    B 341-514 [» ]
    3QQE X-ray 2.10 A 15-340 [» ]
    B 341-514 [» ]
    3QQI X-ray 1.65 A/B 61-279 [» ]
    3QQO X-ray 2.90 A/C/E 15-340 [» ]
    B/D/F 341-514 [» ]
    4HF5 X-ray 3.00 A 15-340 [» ]
    B 341-514 [» ]
    4HLZ X-ray 2.90 A/C/E 15-340 [» ]
    B/D/F 341-514 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei C7S226.

    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. "The NIAID Influenza Genome Sequencing Project."
      Spiro D., Halpin R., Boyne A., Bera J., Ghedin E., Hostetler J., Fedorova N., Kim M., Zaborsky J., Overton L., Djuric K., Sarmiento M., Sitz J., Katzel D., Brown E.G., Keleta L., Bao Y., Sanders R.
      , Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.
      Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: A/Japan/305/1957Imported.
    2. The NIAID Influenza Genome Sequencing Consortium
      Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: A/Japan/305/1957Imported.
    3. "Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic."
      Xu R., McBride R., Paulson J.C., Basler C.F., Wilson I.A.
      J. Virol. 84:1715-1721(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 15-340 AND 341-514, GLYCOSYLATION AT ASN-38; ASN-179 AND ASN-494.
    4. "Structural characterization of an early fusion intermediate of influenza virus hemagglutinin."
      Xu R., Wilson I.A.
      J. Virol. 85:5172-5182(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 61-279, GLYCOSYLATION AT ASN-26; ASN-38; ASN-179; ASN-300 AND ASN-494.
    5. "Structure of a classical broadly neutralizing stem antibody in complex with a pandemic H2 influenza virus hemagglutinin."
      Dreyfus C., Ekiert D.C., Wilson I.A.
      J. Virol. 87:7149-7154(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 15-340 AND 341-514, GLYCOSYLATION AT ASN-26; ASN-179; ASN-300 AND ASN-494.
    6. "A recurring motif for antibody recognition of the receptor-binding site of influenza hemagglutinin."
      Xu R., Krause J.C., McBride R., Paulson J.C., Crowe J.E., Wilson I.A.
      Nat. Struct. Mol. Biol. 20:363-370(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 15-340 AND 341-514, GLYCOSYLATION AT ASN-179 AND ASN-300.

    Entry informationi

    Entry nameiC7S226_I57A0
    AccessioniPrimary (citable) accession number: C7S226
    Entry historyi
    Integrated into UniProtKB/TrEMBL: October 13, 2009
    Last sequence update: October 13, 2009
    Last modified: October 1, 2014
    This is version 40 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported

    External Data

    Dasty 3