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P03454

- HEMA_I33A0

UniProt

P03454 - HEMA_I33A0

Protein

Hemagglutinin

Gene

HA

Organism
Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1))
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (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
    Sitei343 – 3442Cleavage; 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/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1))
    Taxonomic identifieri381518 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
    Virus hostiAves [TaxID: 8782]
    Homo sapiens (Human) [TaxID: 9606]
    Sus scrofa (Pig) [TaxID: 9823]
    ProteomesiUP000000834: Genome

    Subcellular locationi

    Virion membrane Curated; Single-pass type I membrane protein Curated. Host apical cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication
    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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi561 – 5611C → Y: 60% of proteins are targeted to the basolateral membrane in polarized epithelial cells. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 342325Hemagglutinin HA1 chainPRO_0000039069Add
    BLAST
    Chaini344 – 565222Hemagglutinin HA2 chainPRO_0000039070Add
    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
    Disulfide bondi59 ↔ 291By similarity
    Disulfide bondi72 ↔ 84By similarity
    Glycosylationi73 – 731N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi107 ↔ 152By similarity
    Glycosylationi142 – 1421N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi285 – 2851N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi295 ↔ 319By similarity
    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.

    Structurei

    3D structure databases

    ProteinModelPortaliP03454.
    SMRiP03454. Positions 18-339, 344-518.
    ModBaseiSearch...
    MobiDBiSearch...

    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.

    P03454-1 [UniParc]FASTAAdd to Basket

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    MKAKLLVLLY AFVATDADTI CIGYHANNST DTVDTIFEKN VAVTHSVNLL    50
    EDRHNGKLCK LKGIAPLQLG KCNITGWLLG NPECDSLLPA RSWSYIVETP 100
    NSENGACYPG DFIDYEELRE QLSSVSSLER FEIFPKESSW PNHTFNGVTV 150
    SCSHRGKSSF YRNLLWLTKK GDSYPKLTNS YVNNKGKEVL VLWGVHHPSS 200
    SDEQQSLYSN GNAYVSVASS NYNRRFTPEI AARPKVKDQH GRMNYYWTLL 250
    EPGDTIIFEA TGNLIAPWYA FALSRGFESG IITSNASMHE CNTKCQTPQG 300
    SINSNLPFQN IHPVTIGECP KYVRSTKLRM VTGLRNIPSI QYRGLFGAIA 350
    GFIEGGWTGM IDGWYGYHHQ NEQGSGYAAD QKSTQNAING ITNKVNSVIE 400
    KMNTQFTAVG KEFNNLEKRM ENLNKKVDDG FLDIWTYNAE LLVLLENERT 450
    LDFHDLNVKN LYEKVKSQLK NNAKEIGNGC FEFYHKCDNE CMESVRNGTY 500
    DYPKYSEESK LNREKIDGVK LESMGVYQIL AIYSTVASSL VLLVSLGAIS 550
    FWMCSNGSLQ CRICI 565
    Length:565
    Mass (Da):63,525
    Last modified:July 21, 1986 - v1
    Checksum:i1BFF292E4A709299
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02176 Genomic RNA. Translation: AAA43209.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02176 Genomic RNA. Translation: AAA43209.1 .

    3D structure databases

    ProteinModelPortali P03454.
    SMRi P03454. Positions 18-339, 344-518.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Complete sequence analysis shows that the hemagglutinins of the H0 and H2 subtypes of human influenza virus are closely related."
      Hiti A.L., Davis A.R., Nayak D.P.
      Virology 111:113-124(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Analysis of the transmembrane domain of influenza virus neuraminidase, a type II transmembrane glycoprotein, for apical sorting and raft association."
      Barman S., Nayak D.P.
      J. Virol. 74:6538-6545(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    3. "Influenza A virus hemagglutinin containing basolateral localization signal does not alter the apical budding of a recombinant influenza A virus in polarized MDCK cells."
      Barman S., Adhikary L., Kawaoka Y., Nayak D.P.
      Virology 305:138-152(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-561.

    Entry informationi

    Entry nameiHEMA_I33A0
    AccessioniPrimary (citable) accession number: P03454
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 98 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

    Complete proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3