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P0C0V9 (HEMA_BRV1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hemagglutinin-esterase

Short name=HE protein
EC=3.1.1.53
Alternative name(s):
E3 glycoprotein
Gene names
Name:HE
OrganismBreda virus 1 (BRV-1) [Reference proteome]
Taxonomic identifier360393 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeTorovirinaeTorovirus
Virus hostBos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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-di-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. Also hydrolyzes 5-N-acetyl-4-O-acetylneuraminic acid and N-acetyl-9-O-acetylneuraminic acid, but displays a substrate preference for N-acetyl-9-di-O-acetylneuraminic acid. 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.

Catalytic activity

N-acetyl-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate.

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 By similarity.

Sequence similarities

Belongs to the influenza type C/coronaviruses hemagglutinin-esterase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1414 Potential
Chain15 – 416402Hemagglutinin-esterase
PRO_0000045398

Regions

Topological domain15 – 393379Virion surface Potential
Transmembrane394 – 41421Helical; Potential
Topological domain415 – 4162Intravirion Potential
Region4 – 121118Esterase domain first part By similarity
Region122 – 263142Receptor binding By similarity
Region264 – 379116Esterase domain second part By similarity
Compositional bias61 – 677Poly-Ser
Compositional bias402 – 4054Poly-Val

Sites

Active site371Nucleophile By similarity
Active site2231Charge relay system By similarity
Active site3281Charge relay system By similarity

Amino acid modifications

Glycosylation761N-linked (GlcNAc...); by host Potential
Glycosylation2571N-linked (GlcNAc...); by host Potential
Glycosylation2781N-linked (GlcNAc...); by host Potential
Glycosylation3131N-linked (GlcNAc...); by host Potential
Glycosylation3221N-linked (GlcNAc...); by host Potential
Glycosylation3431N-linked (GlcNAc...); by host Potential

Natural variations

Natural variant291F → S.
Natural variant1141D → G.
Natural variant1331T → I.
Natural variant1521Q → K.
Natural variant1551V → E.
Natural variant1591N → K.
Natural variant2141L → R.
Natural variant2341P → S.
Natural variant2381S → L.
Natural variant4161C → V.

Secondary structure

......................................................................... 416
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C0V9 [UniParc].

Last modified January 10, 2006. Version 1.
Checksum: 384C406385439054

FASTA41646,440
        10         20         30         40         50         60 
MLSLILFFPS FAFAATPVTP YYGPGHITFD WCGFGDSRSD CTNPQSPMSL DIPQQLCPKF 

        70         80         90        100        110        120 
SSKSSSSMFL SLHWNNHSSF VSYDYFNCGV EKVFYEGVNF SPRKQYSCWD EGVDGWIELK 

       130        140        150        160        170        180 
TRFYTKLYQM ATTSRCIKLI QLQAPSSLPT LQAGVCRTNK QLPDNPRLAL LSDTVPTSVQ 

       190        200        210        220        230        240 
FVLPGSSGTT ICTKHLVPFC YLNHGCFTTG GSCLPFGVSY VSDSFYYGYY DATPQIGSTE 

       250        260        270        280        290        300 
SHDYVCDYLF MEPGTYNAST VGKFLVYPTK SYCMDTMNIT VPVQAVQSIW SEQYASDDAI 

       310        320        330        340        350        360 
GQACKAPYCI FYNKTTPYTV TNGSDANHGD DEVRMMMQGL LRNSSCISPQ GSTPLALYST 

       370        380        390        400        410 
EMIYEPNYGS CPQFYKLFDT SGNENIDVIS SSYFVATWVL LVVVVILIFV IISFFC 

« Hide

References

[1]"Bovine torovirus: sequencing of the structural genes and expression of the nucleocapsid protein of Breda virus."
Duckmanton L.M., Tellier R., Liu P., Petric M.
Virus Res. 58:83-96(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"The complete sequence of the bovine torovirus genome."
Draker R., Roper R.L., Petric M., Tellier R.
Virus Res. 115:56-68(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]"Nidovirus sialate-O-acetylesterases: evolution and substrate specificity of coronaviral and toroviral receptor-destroying enzymes."
Smits S.L., Gerwig G.J., van Vliet A.L., Lissenberg A., Briza P., Kamerling J.P., Vlasak R., de Groot R.J.
J. Biol. Chem. 280:6933-6941(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF076621 Genomic RNA. Translation: AAD03842.1.
AY427798 Genomic RNA. Translation: AAS17961.1.
RefSeqYP_337909.1. NC_007447.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3I26X-ray1.80A/B/C/D15-392[»]
3I27X-ray2.00A/B/C/D15-392[»]
ProteinModelPortalP0C0V9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48962N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3707767.

Family and domain databases

InterProIPR008980. Capsid_hemagglutn.
IPR007142. Hemagglutn-estrase_core.
IPR003860. Hemagglutn-estrase_hemagglutn.
[Graphical view]
PfamPF03996. Hema_esterase. 1 hit.
PF02710. Hema_HEFG. 1 hit.
[Graphical view]
SUPFAMSSF49818. SSF49818. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0C0V9.

Entry information

Entry nameHEMA_BRV1
AccessionPrimary (citable) accession number: P0C0V9
Secondary accession number(s): O39517, Q3T8I8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 10, 2006
Last modified: April 16, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references