Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P26562

- HEMA_I76A4

UniProt

P26562 - HEMA_I76A4

Protein

Hemagglutinin

Gene

HA

Organism
Influenza A virus (strain A/Duck/Alberta/35/1976 H1N1)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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/Duck/Alberta/35/1976 H1N1)
    Taxonomic identifieri352520 [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_0000038910Add
    BLAST
    Chaini345 – 566222Hemagglutinin HA2 chainPRO_0000038911Add
    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.

    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 strandi56 – 616
    Helixi74 – 796
    Helixi82 – 843
    Turni85 – 873
    Beta strandi96 – 983
    Helixi115 – 1217
    Beta strandi123 – 13412
    Helixi136 – 1394
    Beta strandi150 – 1556
    Beta strandi158 – 1603
    Beta strandi163 – 1675
    Beta strandi170 – 1734
    Beta strandi178 – 1836
    Beta strandi186 – 19813
    Helixi202 – 2098
    Beta strandi216 – 2205
    Beta strandi223 – 2275
    Beta strandi242 – 25110
    Beta strandi256 – 2638
    Beta strandi265 – 27612
    Beta strandi282 – 2843
    Beta strandi289 – 2935
    Beta strandi295 – 2973
    Beta strandi307 – 3104
    Beta strandi317 – 3193
    Beta strandi330 – 3323
    Turni351 – 3533
    Beta strandi365 – 3684
    Helixi382 – 40120
    Helixi419 – 47052
    Helixi471 – 4733
    Beta strandi474 – 4785
    Beta strandi481 – 4866
    Helixi490 – 4989

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WRHX-ray3.00H/J/L18-343[»]
    I/K/M345-566[»]
    ProteinModelPortaliP26562.
    SMRiP26562. Positions 18-519.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26562.

    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.

    P26562-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEAKLFVLFC TFTVLKADTI CVGYHANNST DTVDTVLEKN VTVTHSVNLL    50
    EDSHNGKLCS LNGIAPLQLG KCNVAGWLLG NPECDLLLTA NSWSYIIETS 100
    NSENGTCYPG EFIDYEELRE QLSSISSFEK FEIFPKASSW PNHETTKGVT 150
    AACSYSGASS FYRNLLWITK KGTSYPKLSK SYTNNKGKEV LVLWGVHHPP 200
    SVSEQQSLYQ NADAYVSVGS SKYNRRFAPE IAARPEVRGQ AGRMNYYWTL 250
    LDQGDTITFE ATGNLIAPWY AFALNKGSDS GIITSDAPVH NCDTRCQTPH 300
    GALNSSLPFQ NVHPITIGEC PKYVKSTKLR MATGLRNVPS IQSRGLFGAI 350
    AGFIEGGWTG MIDGWYGYHH QNEQGSGYAA DQKSTQNAID GITSKVNSVI 400
    EKMNTQFTAV GKEFNNLERR IENLNKKVDD GFLDVWTYNA ELLVLLENER 450
    TLDFHDSNVR NLYEKVKSQL RNNAKEIGNG CFEFYHKCDD ECMESVKNGT 500
    YDYPKYSEES KLNREEIDGV KLESMGVYQI LAIYSTVASS LVLLVSWGAI 550
    SFWMCSNGSL QCRICI 566
    Length:566
    Mass (Da):63,072
    Last modified:February 1, 1996 - v2
    Checksum:i9B7ADCA0E9BCA819
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651A → P in AAB52910. (PubMed:8892928)Curated
    Sequence conflicti125 – 1251I → V in AAB52910. (PubMed:8892928)Curated
    Sequence conflicti236 – 2361E → K in AAB52910. (PubMed:8892928)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10477 Genomic RNA. Translation: BAA01280.1.
    U47310 mRNA. Translation: AAB52910.1.
    PIRiA36257. HMIVD1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10477 Genomic RNA. Translation: BAA01280.1 .
    U47310 mRNA. Translation: AAB52910.1 .
    PIRi A36257. HMIVD1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WRH X-ray 3.00 H/J/L 18-343 [» ]
    I/K/M 345-566 [» ]
    ProteinModelPortali P26562.
    SMRi P26562. Positions 18-519.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P26562.

    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 analysis of the haemagglutinin gene of an avian H1N1 influenza virus."
      Austin F.J., Kawaoka Y., Webster R.G.
      J. Gen. Virol. 71:2471-2474(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Emergence of avian H1N1 influenza viruses in pigs in China."
      Guan Y., Shortridge K.F., Krauss S., Li P.H., Kawaoka Y., Webster R.G.
      J. Virol. 70:8041-8046(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-344.

    Entry informationi

    Entry nameiHEMA_I76A4
    AccessioniPrimary (citable) accession number: P26562
    Secondary accession number(s): O09652
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 95 of the entry and version 2 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