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The annotation and conditions in this rule are derived from the following entries: P03452 (HEMA_I34A1), P03465 (HEMA_INCCA)

If a protein meets these conditions... i

Common conditions

Special conditions

    • taxon = Gammainfluenzavirus
    • Subsequence at position 229 - 316 aligns to "C-x*-C" in entry P03465 (individually applies "")
    • Subsequence at position 150 - 310 aligns to entry P03465 (individually applies "N-acetyl-9-O-acetylneuraminic acid binding")
    • Subsequence at position 210 - 252 aligns to "C-x*-C" in entry P03465 (individually applies "")
    • Subsequence at position 310 - 364 aligns to entry P03465 (individually applies "Esterase domain-2")
    • Subsequence at position 447 - 655 aligns to entry P03465 (individually applies "Hemagglutinin-esterase-fusion glycoprotein chain 2")
    • Subsequence at position 237 - 289 aligns to "C-x*-C" in entry P03465 (individually applies "")
    • Subsequence at position 41 - 150 aligns to entry P03465 (individually applies "Esterase domain-1")
    • Subsequence at position 20 - 583 aligns to "C-x*-C" in entry P03465 (individually applies "Interchain (between HEF1 and HEF2 chains)")
    • Subsequence at position 140 - 188 aligns to "C-x*-C" in entry P03465 (individually applies "")
    • Subsequence at position 15 - 40 aligns to entry P03465 (individually applies "Fusion domain-1")
    • Subsequence at position 369 - 369 aligns to entry P03465 (individually applies "Charge relay system")
    • Subsequence at position 71 - 71 aligns to entry P03465 (individually applies "Nucleophile")
    • Subsequence at position 365 - 650 aligns to entry P03465 (individually applies "Fusion domain-2")
    • Subsequence at position 120 - 165 aligns to "C-x*-C" in entry P03465 (individually applies "")
    • Subsequence at position 345 - 351 aligns to "C-x*-C" in entry P03465 (individually applies "")
    • Subsequence at position 15 - 446 aligns to entry P03465 (individually applies "Hemagglutinin-esterase-fusion glycoprotein chain 1")
    • Subsequence at position 366 - 366 aligns to entry P03465 (individually applies "Charge relay system")
    • taxon = Betainfluenzavirus, Alphainfluenzavirus
    • Subsequence at position 18 - 343 aligns to entry P03452 (individually applies "Hemagglutinin HA1 chain")
    • Subsequence at position 59 - 291 aligns to "C-x*-C" in entry P03452 (individually applies "")
    • Subsequence at position 561 - 561 aligns to "C" in entry P03452 (individually applies "S-palmitoyl cysteine; by host")
    • Subsequence at position 554 - 554 aligns to "C" in entry P03452 (individually applies "S-palmitoyl cysteine; by host")
    • Subsequence at position 343 - 344 aligns to "R-G" in entry P03452 (individually applies "Cleavage; by host")
    • Subsequence at position 295 - 319 aligns to "C-x*-C" in entry P03452 (individually applies "")
    • Subsequence at position 21 - 480 aligns to "C-x*-C" in entry P03452 (individually applies "Interchain (between HA1 and HA2 chains)")
    • Subsequence at position 564 - 564 aligns to "C" in entry P03452 (individually applies "S-palmitoyl cysteine; by host")
    • Subsequence at position 107 - 152 aligns to "C-x*-C" in entry P03452 (individually applies "")
    • Subsequence at position 344 - 565 aligns to entry P03452 (individually applies "Hemagglutinin HA2 chain")
    • Subsequence at position 487 - 491 aligns to "C-x*-C" in entry P03452 (individually applies "")
    • Subsequence at position 72 - 84 aligns to "C-x*-C" in entry P03452 (individually applies "")
    • Predicted signal
    • Predicted transmembrane

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi

  • Recommended name:
    Hemagglutinin
  • Recommended name:
    Hemagglutinin-esterase-fusion glycoprotein (EC:3.1.1.53)
    Short name:
    HEF

Cleaved chain(s) or included domain(s)i

  • Cleaved chain:
    Recommended name:
    Hemagglutinin HA1 chain
  • Cleaved chain:
    Recommended name:
    Hemagglutinin HA2 chain
  • Cleaved chain:
    Recommended name:
    Hemagglutinin-esterase-fusion glycoprotein chain 1
    Short name:
    HEF1
  • Cleaved chain:
    Recommended name:
    Hemagglutinin-esterase-fusion glycoprotein chain 2
    Short name:
    HEF2

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi

  • Name:HA
  • Name:HE

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

  • Homotrimer of disulfide-linked HA1-HA2.
  • Homotrimer of disulfide-linked HEF1-HEF2.
  • Homotrimer of disulfide-linked HA1-HA2.

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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.
  • Palmitoylated.
  • In natural infection, inactive HEF is matured into HEF1 and HEF2 outside the cell by one or more trypsin-like, arginine-specific endoprotease.
  • 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.
  • Palmitoylated.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. 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 induce an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.
  • Binds to the N-acetyl-9-O-acetylneuraminic acid residues on the cell surface, bringing about the attachment of the virus particle to the cell. 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 induce an irreversible conformational change in HEF2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. Displays a receptor-destroying activity which is a neuraminidate-O-acetyl esterase. This activity cleaves off any receptor on the cell surface, which would otherwise prevent virions release. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell.
  • 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 either through clathrin-dependent endocytosis or through 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.

<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei

  • (to residues corresponding to positions @NTER@i - @TO@i)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei

  • Charge relay system (to residues corresponding to position 369)
  • Nucleophile (to residues corresponding to position 71)
  • Charge relay system (to residues corresponding to position 366)

<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei

  • Cleavage; by host (to residues corresponding to positions 343 - 344)

<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni

  • N-acetyl-9-O-acetylneuraminic acid binding (to residues corresponding to positions 150 - 310)
  • Esterase domain-2 (to residues corresponding to positions 310 - 364)
  • Esterase domain-1 (to residues corresponding to positions 41 - 150)
  • Fusion domain-1 (to residues corresponding to positions 15 - 40)
  • Fusion domain-2 (to residues corresponding to positions 365 - 650)

<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>Chaini

  • Hemagglutinin-esterase-fusion glycoprotein chain 2 (to residues corresponding to positions 447 - 655)
  • Hemagglutinin-esterase-fusion glycoprotein chain 1 (to residues corresponding to positions 15 - 446)
  • Hemagglutinin HA1 chain (to residues corresponding to positions 18 - 343)
  • Hemagglutinin HA2 chain (to residues corresponding to positions 344 - 565)
  • @CHAIN_NAME@i (to residues corresponding to positions @TO|+1@i - @CTER@i)

<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei

  • Helical (to residues corresponding to positions @FROM@i - @TO@i)

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi

  • S-palmitoyl cysteine; by host (to residues corresponding to position 561)
  • S-palmitoyl cysteine; by host (to residues corresponding to position 554)
  • S-palmitoyl cysteine; by host (to residues corresponding to position 564)

<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi

  • (to residues corresponding to positions 229 - 316)
  • (to residues corresponding to positions 210 - 252)
  • (to residues corresponding to positions 237 - 289)
  • Interchain (between HEF1 and HEF2 chains) (to residues corresponding to positions 20 - 583)
  • (to residues corresponding to positions 140 - 188)
  • (to residues corresponding to positions 120 - 165)
  • (to residues corresponding to positions 345 - 351)
  • (to residues corresponding to positions 59 - 291)
  • (to residues corresponding to positions 295 - 319)
  • Interchain (between HA1 and HA2 chains) (to residues corresponding to positions 21 - 480)
  • (to residues corresponding to positions 107 - 152)
  • (to residues corresponding to positions 487 - 491)
  • (to residues corresponding to positions 72 - 84)

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO (Gene Ontology) termsi

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