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O92367 (HEMA_CVMDV) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
ORF Names:2b
OrganismMurine coronavirus (strain DVIM) (MHV-DVIM) (Murine hepatitis virus)
Taxonomic identifier231423 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostMus [TaxID: 10088]

Protein attributes

Sequence length431 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-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.

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 – 2323 Potential
Chain24 – 431408Hemagglutinin-esterase
PRO_0000037146

Regions

Topological domain24 – 399376Virion surface Potential
Transmembrane400 – 42021Helical; Potential
Topological domain421 – 43111Intravirion Potential
Region11 – 131121Esterase domain first part By similarity
Region132 – 274143Receptor binding By similarity
Region275 – 387113Esterase domain second part By similarity

Sites

Active site441Nucleophile By similarity
Active site2361Charge relay system By similarity
Active site3371Charge relay system By similarity

Amino acid modifications

Glycosylation531N-linked (GlcNAc...); by host Potential
Glycosylation931N-linked (GlcNAc...); by host Potential
Glycosylation1511N-linked (GlcNAc...); by host Potential
Glycosylation1571N-linked (GlcNAc...); by host Potential
Glycosylation1991N-linked (GlcNAc...); by host Potential
Glycosylation2441N-linked (GlcNAc...); by host Potential
Glycosylation2481N-linked (GlcNAc...); by host Potential
Glycosylation3091N-linked (GlcNAc...); by host Potential
Glycosylation3241N-linked (GlcNAc...); by host Potential
Glycosylation3521N-linked (GlcNAc...); by host Potential
Glycosylation3661N-linked (GlcNAc...); by host Potential
Disulfide bond48 ↔ 69 By similarity
Disulfide bond117 ↔ 166 By similarity
Disulfide bond205 ↔ 284 By similarity
Disulfide bond213 ↔ 257 By similarity
Disulfide bond315 ↔ 320 By similarity
Disulfide bond355 ↔ 379 By similarity

Sequences

Sequence LengthMass (Da)Tools
O92367 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: DF4BE9EE0AE7301B

FASTA43148,440
        10         20         30         40         50         60 
MARTDAMAPR TLLLVLSLGY AFGFNEPLNV VSHLNDDWFL FGDSRSDCNH INNLSQQNYN 

        70         80         90        100        110        120 
YMDINPELCK SGKISAKAGN SLFKSFHFTD FYNYTGEGSQ IIFYEGVNFT PYVGFKCLNN 

       130        140        150        160        170        180 
GDNNRWMGNK ARFYTQLYQK MAHYRSLSVI NITYTYNGSA GPVSMCKHIA NGVTLTLNNP 

       190        200        210        220        230        240 
TFIGKEVSKP DYYYESEANF TLQGCDEFIV PLCVFNGQYL SSKLYYDDSQ YYYNVDTGVL 

       250        260        270        280        290        300 
YGFNSTLNIT SGLDLTCIYL ALTPGNYISI SNELLLTVPS KAICLRKPKA FTPVQVVDSR 

       310        320        330        340        350        360 
WHSNRQSDNM TAIACQLPYC YFRNTTSDYN GVYDSHHGDA GFTSILAGLM YNVSCLAQQG 

       370        380        390        400        410        420 
AFVYNNVSSS WPQYPYGHCP TAANIVFMAP VCMYDPLPVI LLGVLLGIAV LIIVFLMFYF 

       430 
MTDSGVRLHE A 

« Hide

References

[1]"Sequence of the hemagglutinin-esterase (HE) genes of two enterotropic MHV strains."
Compton S.R., Moore K.M.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF091734 mRNA. Translation: AAC63044.1.

3D structure databases

ProteinModelPortalO92367.
SMRO92367. Positions 25-384.
ModBaseSearch...
MobiDBSearch...

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. SSF49818. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHEMA_CVMDV
AccessionPrimary (citable) accession number: O92367
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 75 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