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P31614 (HEMA_CVMS) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMurine coronavirus (strain S) (MHV-S) (Murine hepatitis virus)
Taxonomic identifier11145 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostMus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length430 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-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.

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 caution

The sequence AAA46460.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 430411Hemagglutinin-esterase
PRO_0000037148

Regions

Topological domain20 – 404385Virion surface Potential
Transmembrane405 – 42521Helical; Potential
Topological domain426 – 4305Intravirion Potential
Region9 – 129121Esterase domain first part By similarity
Region130 – 278149Receptor binding By similarity
Region279 – 392114Esterase domain second part By similarity
Compositional bias213 – 2186Poly-Ser

Sites

Active site421Nucleophile By similarity
Active site2351Charge relay system By similarity
Active site3421Charge relay system By similarity

Amino acid modifications

Glycosylation911N-linked (GlcNAc...); by host Potential
Glycosylation1491N-linked (GlcNAc...); by host Potential
Glycosylation1931N-linked (GlcNAc...); by host Potential
Glycosylation2431N-linked (GlcNAc...); by host Potential
Glycosylation3061N-linked (GlcNAc...); by host Potential
Glycosylation3131N-linked (GlcNAc...); by host Potential
Glycosylation3281N-linked (GlcNAc...); by host Potential
Glycosylation3571N-linked (GlcNAc...); by host Potential
Glycosylation3711N-linked (GlcNAc...); by host Potential
Disulfide bond46 ↔ 67 By similarity
Disulfide bond115 ↔ 164 By similarity
Disulfide bond199 ↔ 288 By similarity
Disulfide bond207 ↔ 261 By similarity
Disulfide bond319 ↔ 324 By similarity
Disulfide bond360 ↔ 384 By similarity

Secondary structure

.................................................................. 430
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31614 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: D0401D7D5E2B8C38

FASTA43048,256
        10         20         30         40         50         60 
MCIAMAPRTL LLLIGCQLVF GFNEPLNIVS HLNDDWFLFG DSRSDCTYVE NNGHPKLDWL 

        70         80         90        100        110        120 
DLDPKLCNSG RIYAKSGNSL FRSFHFIDFY NYSGEGDQVI FYEGVNFSPS HGFKCLAYGD 

       130        140        150        160        170        180 
NKRWMGNKAR FYARVYEKMA QYRSLSFVNV SYAYGGNAKP TSICKDKTLT LNNPTFISKE 

       190        200        210        220        230        240 
SNYVDYYYES EANFTLQGCD EFIVTLCVSN GHSKSSSSDP ANKYYTDAQS YYNMDTGVLY 

       250        260        270        280        290        300 
GFNSTLDVGN TVQNPGLDLT CRYLALTPGN YKAVSLEYLL SLPSKAICLR KPKSFMPVQV 

       310        320        330        340        350        360 
VDSRWNSTRQ SDNMTAVACQ LPYCFFRNTS ADYSGGTHDV HHGDFHFRQL LSGLLYNVSC 

       370        380        390        400        410        420 
IAQQGAFVYN NVSSSWPAYG YGHCPTAANI GYMAPVCIYE PLPVILLGVL LGIAVLIIVF 

       430 
LMFYFMTDSG 

« Hide

References

[1]"Heterogeneity of gene expression of the hemagglutinin-esterase (HE) protein of murine coronaviruses."
Yokomori K., Banner L.R., Lai M.M.C.
Virology 183:647-657(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"The sialate-4-O-acetylesterases of coronaviruses related to mouse hepatitis virus: a proposal to reorganize group 2 Coronaviridae."
Wurzer W.J., Obojes K., Vlasak R.
J. Gen. Virol. 83:395-402(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[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
M64316 Genomic RNA. Translation: AAA46460.1. Different initiation.
PIRHMIHMS. A40476.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4C7LX-ray2.10A/B22-400[»]
4C7WX-ray2.50A/B22-400[»]
ProteinModelPortalP31614.
SMRP31614. Positions 23-389.
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_CVMS
AccessionPrimary (citable) accession number: P31614
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 89 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