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Q9DR81 (HEMA_CVBON) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
ORF Names:2b
OrganismBovine coronavirus (strain Ontario) (BCoV) (BCV)
Taxonomic identifier231422 [NCBI]
Taxonomic lineageViruses › ssRNA positive-strand viruses, no DNA stage › Nidovirales › Coronaviridae › Coronavirinae › Betacoronavirus ›
Virus hostBos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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.

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.

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 – 1818 By similarity
Chain19 – 424406Hemagglutinin-esterase
PRO_0000037141

Regions

Topological domain19 – 392374Virion surface Potential
Transmembrane393 – 41321Helical; Potential
Topological domain414 – 42411Intravirion Potential
Region7 – 127121Esterase domain first part By similarity
Region128 – 266139Receptor binding By similarity
Region267 – 379113Esterase domain second part By similarity

Sites

Active site401Nucleophile By similarity
Active site2281Charge relay system By similarity
Active site3291Charge relay system By similarity

Amino acid modifications

Glycosylation541N-linked (GlcNAc...); by host Potential
Glycosylation891N-linked (GlcNAc...); by host Potential
Glycosylation1531N-linked (GlcNAc...); by host Potential
Glycosylation2361N-linked (GlcNAc...); by host Potential
Glycosylation3011N-linked (GlcNAc...); by host Potential
Glycosylation3161N-linked (GlcNAc...); by host Potential
Glycosylation3581N-linked (GlcNAc...); by host Potential
Disulfide bond44 ↔ 65 By similarity
Disulfide bond113 ↔ 162 By similarity
Disulfide bond197 ↔ 276 By similarity
Disulfide bond205 ↔ 249 By similarity
Disulfide bond307 ↔ 312 By similarity
Disulfide bond347 ↔ 371 By similarity

Natural variations

Natural variant3941F → L in strain: Isolate BCO.43277.

Sequences

Sequence LengthMass (Da)Tools
Q9DR81 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 999752B9FCA231BA

FASTA42447,652
        10         20         30         40         50         60 
MFLLPRFVLV SCIIGSLGFD NPPTNVVSHL NGDWFLFGDS RSDCNHVVTT NPRNYSYMDL 

        70         80         90        100        110        120 
NPALCGSGKI SSKAGNSIFR SFHFTDFYNY TGEGQQIIFY EGVNFTPYHA FKCTTSGSND 

       130        140        150        160        170        180 
IWMQNKGLFY TQVYKNMAVY RSLTFVNVPY VYNGSAQSTA LCKSGSLVLN NPAYIAREAN 

       190        200        210        220        230        240 
FGDYYYKVEA DFYLSGCDEY IVPLCIFNGK FLSNTKYYDD SQYYFNKDTG VIYGLNSTET 

       250        260        270        280        290        300 
ITTGFDFNCH YLVLPSGNYL AISNELLLTV PTKAICLNKR KDFTPVQVVD SRWNNARQSD 

       310        320        330        340        350        360 
NMTAVACQPP YCYFRNSTTN YVGVYDINHG DAGFTSILSG LLYDSPCFSQ QGVFRYDNVS 

       370        380        390        400        410        420 
SVWPLYPYGR CPTAADINTP DVPICVYDPL PIIFLGILLG VAVIIIVVLL LYFMVDNGTR 


LHDA

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References

[1]"Bovine coronaviruses associated with enteric and respiratory diseases in Canadian dairy cattle display different reactivities to anti-HE monoclonal antibodies and distinct amino acid changes in their HE, S and ns4.9 protein."
Gelinas A.-M., Boutin M., Sasseville A.M.-J., Dea S.
Virus Res. 76:43-57(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Isolate BCO.43277 and Isolate BCO.44175.
[2]"Identification of specific variations within the HE, S1, and ORF4 genes of bovine coronaviruses associated with enteric and respiratory diseases in dairy cattle."
Gelinas A.-M., Sasseville A.M.-J., Dea S.
Adv. Exp. Med. Biol. 494:63-67(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: Isolate BCO.43277 and Isolate BCO.44175.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF239308 Genomic RNA. Translation: AAG60544.1.
AF239309 Genomic RNA. Translation: AAG40622.1.

3D structure databases

ProteinModelPortalQ9DR81.
SMRQ9DR81. Positions 19-376.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. Capsid_hemag. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHEMA_CVBON
AccessionPrimary (citable) accession number: Q9DR81
Secondary accession number(s): Q98VL2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: March 1, 2001
Last modified: April 3, 2013
This is version 69 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

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