P31615 (HEMA_CVMA5) Reviewed, UniProtKB/Swiss-Prot
Last modified February 19, 2014. Version 89. History...
Names and origin
|Protein names||Recommended name:|
Short name=HE protein
|Organism||Murine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus) [Reference proteome]|
|Taxonomic identifier||11142 [NCBI]|
|Taxonomic lineage||Viruses › ssRNA positive-strand viruses, no DNA stage › Nidovirales › Coronaviridae › Coronavirinae › Betacoronavirus ›|
|Virus host||Mus musculus (Mouse) [TaxID: 10090]|
|Sequence length||428 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Inferred from homology|
General annotation (Comments)
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-4-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.
N-acetyl-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate.
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.
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.
N-glycosylated in the RER.
Readthrough of the terminator UGA may occur between the codons for Ile-14 and Cys-16.
Belongs to the influenza type C/coronaviruses hemagglutinin-esterase family.
|Cellular component||Host cell membrane|
Viral envelope protein
|Technical term||Complete proteome|
|Gene Ontology (GO)|
|Biological_process||fusion of virus membrane with host plasma membrane|
Inferred from electronic annotation. Source: InterPrometabolic process
Inferred from electronic annotation. Source: GOC
|Cellular_component||host cell plasma membrane|
Inferred from electronic annotation. Source: UniProtKB-SubCellintegral component of membrane
Inferred from electronic annotation. Source: UniProtKB-KWviral envelope
Inferred from electronic annotation. Source: UniProtKB-KWvirion membrane
Inferred from electronic annotation. Source: UniProtKB-SubCell
|Molecular_function||sialate O-acetylesterase activity|
Inferred from electronic annotation. Source: UniProtKB-EC
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Signal peptide||1 – 20||20||Potential|
|Chain||21 – 428||408||Hemagglutinin-esterase||PRO_0000037145|
|Topological domain||21 – 404||384||Virion surface Potential|
|Transmembrane||405 – 425||21||Helical; Potential|
|Topological domain||426 – 428||3||Intravirion Potential|
|Region||9 – 129||121||Esterase domain first part By similarity|
|Region||130 – 278||149||Receptor binding By similarity|
|Region||279 – 392||114||Esterase domain second part By similarity|
|Active site||42||1||Nucleophile By similarity|
|Active site||235||1||Charge relay system By similarity|
|Active site||342||1||Charge relay system By similarity|
Amino acid modifications
|Glycosylation||91||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||149||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||193||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||243||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||313||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||328||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||332||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||357||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||371||1||N-linked (GlcNAc...); by host Potential|
|Disulfide bond||46 ↔ 67||By similarity|
|Disulfide bond||115 ↔ 164||By similarity|
|Disulfide bond||199 ↔ 288||By similarity|
|Disulfide bond||207 ↔ 261||By similarity|
|Disulfide bond||319 ↔ 324||By similarity|
|Disulfide bond||360 ↔ 384||By similarity|
|||"Sequence of mouse hepatitis virus A59 mRNA 2: indications for RNA recombination between coronaviruses and influenza C virus."|
Luytjes W., Bredenbeek P.J., Noten A.F.H., Horzinek M.C., Spaan W.J.M.
Virology 166:415-422(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|||"Altered pathogenesis of a mutant of the murine coronavirus MHV-A59 is associated with a Q159L amino acid substitution in the spike protein."|
Leparc-Goffart I., Hingley S.T., Chua M.M., Jiang X., Lavi E., Weiss S.R.
Virology 239:1-10(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Isolate C12 mutant.
|M23256 Genomic RNA. Translation: AAA46449.1. Sequence problems.|
AF029248 Genomic RNA. No translation available.
|PIR||HMIHMH. B31165. |
3D structure databases
|SMR||P31615. Positions 23-389. |
Protocols and materials databases
Family and domain databases
|InterPro||IPR008980. Capsid_hemagglutn. |
|Pfam||PF03996. Hema_esterase. 1 hit. |
PF02710. Hema_HEFG. 1 hit.
|SUPFAM||SSF49818. SSF49818. 1 hit. |
|Accession||Primary (citable) accession number: P31615|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families