HAMAP rule MF_04072
General rule information
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| Accession | MF_04072 |
| Dates | 20-APR-2017 (Created)
2-SEP-2024 (Last updated, Version 8) |
| Name | INFV_HEMA |
| Scope(s) |
Viruses Orthomyxoviridae |
| Template(s) | P03452 (HEMA_I34A1); P03465 (HEMA_INCCA); [ Recover all ] |
| Triggered by |
HAMAP; MF_04072 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | HEMA |
| case <OC:Alphainfluenzavirus> or <OC:Betainfluenzavirus> | |
| Protein name | RecName: Full=Hemagglutinin; Contains: RecName: Full=Hemagglutinin HA1 chain; Contains: RecName: Full=Hemagglutinin HA2 chain; Flags: Precursor; |
| Gene name | Name=HA; |
| else | |
| Protein name | RecName: Full=Hemagglutinin-esterase-fusion glycoprotein; Short=HEF; EC=3.1.1.53; Contains: RecName: Full=Hemagglutinin-esterase-fusion glycoprotein chain 1; Short=HEF1; Contains: RecName: Full=Hemagglutinin-esterase-fusion glycoprotein chain 2; Short=HEF2; Flags: Precursor; |
| Gene name | Name=HE; |
| end case | |
Comments
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| case <OC:Alphainfluenzavirus> | |
| FUNCTION | 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. |
| SUBUNIT | Homotrimer of disulfide-linked HA1-HA2. |
| SUBCELLULAR LOCATION | Virion membrane; Single-pass type I membrane protein. 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. |
| PTM | 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 club cells. |
| PTM | Palmitoylated. |
| else case <OC:Betainfluenzavirus> | |
| FUNCTION | 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. |
| SUBUNIT | Homotrimer of disulfide-linked HA1-HA2. |
| SUBCELLULAR LOCATION | Virion membrane; Single-pass type I membrane protein. 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. |
| PTM | 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 club cells. |
| PTM | Palmitoylated. |
| else case <OC:Gammainfluenzavirus> | |
| FUNCTION | 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. |
| CATALYTIC ACTIVITY | Reaction=N-acetyl-9-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate + H(+); Xref=Rhea:RHEA:22600, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28999, ChEBI:CHEBI:30089, ChEBI:CHEBI:35418; EC=3.1.1.53; |
| CATALYTIC ACTIVITY | Reaction=N-acetyl-4-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate + H(+); Xref=Rhea:RHEA:25564, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29006, ChEBI:CHEBI:30089, ChEBI:CHEBI:35418; EC=3.1.1.53; |
| SUBUNIT | Homotrimer of disulfide-linked HEF1-HEF2. |
| SUBCELLULAR LOCATION | Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass type I membrane protein. |
| PTM | In natural infection, inactive HEF is matured into HEF1 and HEF2 outside the cell by one or more trypsin-like, arginine-specific endoprotease. |
| end case | |
| SIMILARITY | Belongs to the influenza viruses hemagglutinin family. |
Keywords
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| case <OC:Alphainfluenzavirus> | |
| Clathrin- and caveolin-independent endocytosis of virus by host | |
| Clathrin-mediated endocytosis of virus by host | |
| end case | |
| case <OC:Alphainfluenzavirus> or <OC:Betainfluenzavirus> | |
| Lipoprotein | |
| Palmitate | |
| end case | |
| case <OC:Gammainfluenzavirus> | |
| Hydrolase | |
| end case | |
| Disulfide bond | |
| Fusion of virus membrane with host endosomal membrane | |
| Fusion of virus membrane with host membrane | |
| Glycoprotein | |
| Hemagglutinin | |
| Host cell membrane | |
| Host membrane | |
| Host-virus interaction | |
| Membrane | |
| Signal | |
| Transmembrane | |
| Transmembrane helix | |
| Viral attachment to host cell | |
| Viral envelope protein | |
| Viral penetration into host cytoplasm | |
| Virion | |
| Virus endocytosis by host | |
| Virus entry into host cell | |
Gene Ontology
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| GO:0020002; Cellular component:host cell plasma membrane | |
| GO:0016020; Cellular component:membrane | |
| GO:0019031; Cellular component:viral envelope | |
| GO:0046789; Molecular function:host cell surface receptor binding | |
| case <OCellular component:Alphainfluenzavirus> | |
| GO:0075512; Biological process:clathrin-dependent endocytosis of virus by host cell | |
| end case | |
| GO:0039654; Biological process:fusion of virus membrane with host endosome membrane | |
| GO:0046761; Biological process:viral budding from plasma membrane | |
Cross-references
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| PROSITE | PS00001; ASN_GLYCOSYLATION; 0-unlimited; |
| Pfam | PF00509; Hemagglutinin; 1; |
| Pfam | PF03996; Hema_esterase; 1; |
| Pfam | PF02710; Hema_HEFG; 1; |
| Pfam | PF08720; Hema_stalk; 1; |
| PRINTS | PR00330; HEMAGGLUTN1; 1; |
| PRINTS | PR00329; HEMAGGLUTN12; 1; |
| PRINTS | PR00331; HEMAGGLUTN2; 1; |
| General | Signal; -; 1; |
| General | Transmembrane; -; 1; |
| ADD_TOPO_DOMAIN | Extracellular; -; 1; |
| ADD_TOPO_DOMAIN | Cytoplasmic; -; 1; |
Features
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| From: HEMA_I34A1 (P03452) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| case <OC:Alphainfluenzavirus> or <OC:Betainfluenzavirus> | ||||||||||||
| CHAIN | 18 | 343 | /note="Hemagglutinin HA1 chain" | |||||||||
| CHAIN | 344 | 565 | /note="Hemagglutinin HA2 chain" | |||||||||
| SITE | 343 | 344 | /note="Cleavage; by host" | R-G | ||||||||
| LIPID | 554 | 554 | /note="S-palmitoyl cysteine; by host" | C | ||||||||
| LIPID | 561 | 561 | /note="S-palmitoyl cysteine; by host" | C | ||||||||
| LIPID | 564 | 564 | /note="S-palmitoyl cysteine; by host" | C | ||||||||
| DISULFID | 21 | 480 | /note="Interchain (between HA1 and HA2 chains)" | C-x*-C | ||||||||
| DISULFID | 59 | 291 | C-x*-C | |||||||||
| DISULFID | 72 | 84 | C-x*-C | |||||||||
| DISULFID | 107 | 152 | C-x*-C | |||||||||
| DISULFID | 295 | 319 | C-x*-C | |||||||||
| DISULFID | 487 | 491 | C-x*-C | |||||||||
| end case | ||||||||||||
| From: HEMA_INCAA (P03465) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| case <OC:Gammainfluenzavirus> | ||||||||||||
| CHAIN | 15 | 446 | /note="Hemagglutinin-esterase-fusion glycoprotein chain 1" | |||||||||
| CHAIN | 447 | 655 | /note="Hemagglutinin-esterase-fusion glycoprotein chain 2" | |||||||||
| REGION | 15 | 40 | /note="Fusion domain-1" | |||||||||
| REGION | 41 | 150 | /note="Esterase domain-1" | |||||||||
| REGION | 150 | 310 | /note="N-acetyl-9-O-acetylneuraminic acid binding" | |||||||||
| REGION | 310 | 364 | /note="Esterase domain-2" | |||||||||
| REGION | 365 | 650 | /note="Fusion domain-2" | |||||||||
| ACT_SITE | 71 | 71 | /note="Nucleophile" | |||||||||
| ACT_SITE | 366 | 366 | /note="Charge relay system" | |||||||||
| ACT_SITE | 369 | 369 | /note="Charge relay system" | |||||||||
| DISULFID | 20 | 583 | /note="Interchain (between HEF1 and HEF2 chains)" | C-x*-C | ||||||||
| DISULFID | 120 | 165 | C-x*-C | |||||||||
| DISULFID | 140 | 188 | C-x*-C | |||||||||
| DISULFID | 210 | 252 | C-x*-C | |||||||||
| DISULFID | 229 | 316 | C-x*-C | |||||||||
| DISULFID | 237 | 289 | C-x*-C | |||||||||
| DISULFID | 345 | 351 | C-x*-C | |||||||||
| end case | ||||||||||||
Additional information
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| Size range | 560-655 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |