Reviewed,
UniProtKB/Swiss-Prot Q0ZME8 (HEMA_CVHN5)
Last modified
June 16, 2009.
Version 16.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Hemagglutinin-esterase Short name=HE protein EC=3.1.1.53 Alternative name(s): E3 glycoprotein | ||||
| Gene names |
| ||||
| Organism | Human coronavirus HKU1 (isolate N5) (HCoV-HKU1) [Complete proteome] | ||||
| Taxonomic identifier | 443241 [NCBI] | ||||
| Taxonomic lineage | Viruses › ssRNA positive-strand viruses, no DNA stage › Nidovirales › Coronaviridae › Coronavirus › Coronavirus group 2 › Coronavirus group 2a | ||||
| Virus host | Homo sapiens (Human) [TaxID: 9606] |
Protein attributes
| Sequence length | 385 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Mediates de-O-acetylation of N-acetyl-9-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. This receptor-destroying activity is important for virus release as it probably helps preventing self-aggregation and ensures the efficient spread of the progeny virus from cell to cell. May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. Seems to be a 'luxury' protein that is not absolutely necessary for virus infection in culture. However, its presence in the virus may alter its pathogenicity. May become a target for both the humoral and the cellular branches of the immune system By similarity. |
| Catalytic activity | N-acetyl-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate. |
| Subunit structure | Homodimer; disulfide-linked. Forms a complex with the M protein in the pre-Golgi. Associates then with S-M complex to form a ternary complex S-M-HE By similarity. |
| Subcellular location | Virion membrane; Single-pass type I membrane protein Potential. Host cell membrane; Single-pass type I membrane protein Potential. Note: In infected cells becomes incorporated into the envelope of virions during virus assembly at the endoplasmic reticulum and cis Golgi. However, some may escape incorporation into virions and subsequently migrate to the cell surface By similarity. |
| Post-translational modification | N-glycosylated in the RER By similarity. |
| Miscellaneous | Isolate N5 belongs to genotype C. Genotype C probably arose from recombination between genotypes A and B. |
| Sequence similarities | Belongs to the influenza type C/coronaviruses hemagglutinin-esterase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Envelope protein Membrane Virion |
| Domain | Signal Transmembrane |
| Molecular function | Hemagglutinin Hydrolase |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | viral envelope fusion with host membrane Inferred from electronic annotation. Source: InterPro |
| Cellular component | host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-KW viral envelopeInferred from electronic annotation. Source: UniProtKB-KW virion membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | host cell surface receptor binding Inferred from electronic annotation. Source: InterPro sialate O-acetylesterase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 13 | 13 | Potential | ||||||
| Chain | 14 – 385 | 372 | Hemagglutinin-esterase | PRO_0000297763 | |||||
Regions | |||||||||
| Topological domain | 14 – 360 | 347 | Extracellular Potential | ||||||
| Transmembrane | 361 – 381 | 21 | Potential | ||||||
| Topological domain | 382 – 385 | 4 | Cytoplasmic Potential | ||||||
| Region | 1 – 121 | 121 | Esterase domain first part By similarity | ||||||
| Region | 122 – 239 | 118 | Receptor binding By similarity | ||||||
| Region | 240 – 352 | 113 | Esterase domain second part By similarity | ||||||
Sites | |||||||||
| Active site | 34 | 1 | Nucleophile By similarity | ||||||
| Active site | 205 | 1 | Charge relay system By similarity | ||||||
| Active site | 302 | 1 | Charge relay system By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 83 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 110 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 145 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 171 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 196 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 251 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 289 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 317 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
| Glycosylation | 331 | 1 | N-linked (GlcNAc...); by host Potential | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Comparative analysis of 22 coronavirus HKU1 genomes reveals a novel genotype and evidence of natural recombination in coronavirus HKU1." Woo P.C.Y., Lau S.K.P., Yip C.C.Y., Huang Y., Tsoi H.-W., Chan K.-H., Yuen K.-Y. J. Virol. 80:7136-7145(2006) [PubMed: 16809319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
Cross-references
Sequence databases | |
|---|---|
| DQ339101 Genomic RNA. Translation: ABC70718.1. | |
3D structure databases | |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR007142. Hemagglutn-estrase_core. IPR003860. Hemagglutn-estrase_hemagglutn. [Graphical view] |
| Pfam | PF03996. Hema_esterase. 1 hit. PF02710. Hema_HEFG. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HEMA_CVHN5 | ||||||||
| Accession | Primary (citable) accession number: Q0ZME8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Virus (Virus annotation project) | ||||||||

Clusters with


