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P03451

- HEMA_I57A0

UniProt

P03451 - HEMA_I57A0

Protein

Hemagglutinin

Gene

HA

Organism
Influenza A virus (strain A/Japan/305/1957 H2N2)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei340 – 3412Cleavage; 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/Japan/305/1957 H2N2)
    Taxonomic identifieri387161 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
    Virus hostiAves [TaxID: 8782]
    Homo sapiens (Human) [TaxID: 9606]

    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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi519 – 5191S → A: No effect on palmitoylation. 1 Publication
    Mutagenesisi520 – 5201S → A: No effect on palmitoylation. 1 Publication
    Mutagenesisi551 – 5511C → A: Loss of palmitoylation. 1 Publication
    Mutagenesisi558 – 5581C → A: Loss of palmitoylation. 1 Publication
    Mutagenesisi561 – 5611C → A: Loss of palmitoylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1515Sequence AnalysisAdd
    BLAST
    Chaini16 – 339324Hemagglutinin HA1 chainPRO_0000039010Add
    BLAST
    Chaini341 – 562222Hemagglutinin HA2 chainPRO_0000039011Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi19 ↔ 477Interchain (between HA1 and HA2 chains)By similarity
    Glycosylationi25 – 251N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi26 – 261N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi38 – 381N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi57 ↔ 288By similarity
    Disulfide bondi70 ↔ 82By similarity
    Disulfide bondi105 ↔ 149By similarity
    Glycosylationi179 – 1791N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi180 – 1801N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi292 ↔ 316By similarity
    Glycosylationi300 – 3001N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi484 ↔ 488By similarity
    Glycosylationi494 – 4941N-linked (GlcNAc...); by hostSequence Analysis
    Lipidationi551 – 5511S-palmitoyl cysteine; by host1 Publication
    Lipidationi558 – 5581S-palmitoyl cysteine; by host1 Publication
    Lipidationi561 – 5611S-palmitoyl cysteine; by host1 Publication

    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.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Interactioni

    Subunit structurei

    Homotrimer of disulfide-linked HA1-HA2.

    Protein-protein interaction databases

    DIPiDIP-60235N.

    Structurei

    Secondary structure

    1
    562
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 238
    Beta strandi37 – 426
    Beta strandi44 – 463
    Beta strandi65 – 684
    Helixi72 – 776
    Helixi80 – 867
    Beta strandi94 – 963
    Beta strandi101 – 1033
    Beta strandi108 – 1103
    Helixi113 – 1197
    Beta strandi122 – 13211
    Helixi134 – 1363
    Beta strandi138 – 1414
    Beta strandi146 – 1516
    Beta strandi154 – 1563
    Beta strandi161 – 1633
    Beta strandi167 – 1693
    Beta strandi174 – 1796
    Beta strandi182 – 19413
    Helixi198 – 2058
    Beta strandi206 – 2094
    Beta strandi212 – 2154
    Beta strandi220 – 2234
    Beta strandi239 – 2479
    Beta strandi252 – 2598
    Beta strandi261 – 27111
    Beta strandi278 – 2803
    Beta strandi289 – 2946
    Beta strandi297 – 2993
    Beta strandi303 – 3064
    Beta strandi313 – 3153
    Beta strandi326 – 3283
    Turni347 – 3493
    Beta strandi361 – 3677
    Beta strandi373 – 3764
    Helixi378 – 39720
    Beta strandi403 – 4053
    Helixi415 – 46652
    Helixi467 – 4693
    Beta strandi470 – 4723
    Beta strandi474 – 4829
    Helixi486 – 4938
    Helixi499 – 51012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FHUmodel-A/C/E16-335[»]
    B/D/F341-500[»]
    4HFUX-ray3.11A15-340[»]
    B341-514[»]
    4HG4X-ray3.20A/B/C/D/E/F/G/H/I15-340[»]
    a/b/c/d/e/f/g/h/i341-514[»]
    ProteinModelPortaliP03451.
    SMRiP03451. Positions 16-335, 341-513.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini16 – 525510ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini547 – 56216CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei526 – 54621HelicalSequence 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.

    P03451-1 [UniParc]FASTAAdd to Basket

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    MAIIYLILLF TAVRGDQICI GYHANNSTEK VDTNLERNVT VTHAKDILEK    50
    THNGKLCKLN GIPPLELGDC SIAGWLLGNP ECDRLLSVPE WSYIMEKENP 100
    RDGLCYPGSF NDYEELKHLL SSVKHFEKVK ILPKDRWTQH TTTGGSRACA 150
    VSGNPSFFRN MVWLTKEGSD YPVAKGSYNN TSGEQMLIIW GVHHPIDETE 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 GNLERRLENL NKRMEDGFLD VWTYNAELLV LMENERTLDF 450
    HDSNVKNLYD KVRMQLRDNV KELGNGCFEF YHKCDDECMN SVKNGTYDYP 500
    KYEEESKLNR NEIKGVKLSS MGVYQILAIY ATVAGSLSLA IMMAGISFWM 550
    CSNGSLQCRI CI 562
    Length:562
    Mass (Da):63,119
    Last modified:July 21, 1986 - v1
    Checksum:i6B7FD0C038993630
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02127 Genomic RNA. Translation: AAA43185.1.
    PIRiA04062. HMIV2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02127 Genomic RNA. Translation: AAA43185.1 .
    PIRi A04062. HMIV2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FHU model - A/C/E 16-335 [» ]
    B/D/F 341-500 [» ]
    4HFU X-ray 3.11 A 15-340 [» ]
    B 341-514 [» ]
    4HG4 X-ray 3.20 A/B/C/D/E/F/G/H/I 15-340 [» ]
    a/b/c/d/e/f/g/h/i 341-514 [» ]
    ProteinModelPortali P03451.
    SMRi P03451. Positions 16-335, 341-513.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60235N.

    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. "Cloning and DNA sequence of double-stranded copies of haemagglutinin genes from H2 and H3 strains elucidates antigenic shift and drift in human influenza virus."
      Gething M.-J., Bye J., Skehel J.J., Waterfield M.
      Nature 287:301-306(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion."
      Naeve C.W., Williams D.
      EMBO J. 9:3857-3866(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-551; CYS-558 AND CYS-561, MUTAGENESIS OF SER-519; SER-520; CYS-551; CYS-558 AND CYS-561.
    3. "Fusion of influenza hemagglutinin-expressing fibroblasts with glycophorin-bearing liposomes: role of hemagglutinin surface density."
      Ellens H., Bentz J., Mason D., Zhang F., White J.M.
      Biochemistry 29:9697-9707(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiHEMA_I57A0
    AccessioniPrimary (citable) accession number: P03451
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 101 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