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Q0ZME8 (HEMA_CVHN5) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 36. 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:2
OrganismHuman coronavirus HKU1 (isolate N5) (HCoV-HKU1) [Complete proteome]
Taxonomic identifier443241 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length385 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 By similarity.

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 By similarity.

Miscellaneous

Isolate N5 belongs to genotype C. Genotype C probably arose from recombination between genotypes A and B.

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 – 1313 Potential
Chain14 – 385372Hemagglutinin-esterase
PRO_0000297763

Regions

Topological domain14 – 360347Virion surface Potential
Transmembrane361 – 38121Helical; Potential
Topological domain382 – 3854Intravirion Potential
Region1 – 121121Esterase domain first part By similarity
Region122 – 239118Receptor binding By similarity
Region240 – 352113Esterase domain second part By similarity

Sites

Active site341Nucleophile By similarity
Active site2051Charge relay system By similarity
Active site3021Charge relay system By similarity

Amino acid modifications

Glycosylation831N-linked (GlcNAc...); by host Potential
Glycosylation1101N-linked (GlcNAc...); by host Potential
Glycosylation1451N-linked (GlcNAc...); by host Potential
Glycosylation1711N-linked (GlcNAc...); by host Potential
Glycosylation1961N-linked (GlcNAc...); by host Potential
Glycosylation2511N-linked (GlcNAc...); by host Potential
Glycosylation2891N-linked (GlcNAc...); by host Potential
Glycosylation3171N-linked (GlcNAc...); by host Potential
Glycosylation3311N-linked (GlcNAc...); by host Potential
Disulfide bond38 ↔ 59 By similarity
Disulfide bond107 ↔ 155 By similarity
Disulfide bond183 ↔ 249 By similarity
Disulfide bond191 ↔ 222 By similarity
Disulfide bond280 ↔ 285 By similarity
Disulfide bond320 ↔ 344 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0ZME8 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 06FEAAB6C6F3B2B4

FASTA38544,429
        10         20         30         40         50         60 
MLIIFLFFNF CYGFNEPLNV VSHLNHDWFL FGDSRSDCNH INNLKIKNYG YLDIHPSLCN 

        70         80         90        100        110        120 
NGKISSSAGD SIFKSYHFTR FYNYTGEGDQ IIFYEGVNFS PHHRFKCFFN GSNDVWIFNK 

       130        140        150        160        170        180 
VRFYRALYSN MALFRYLTFV DILYNFSFSI KANICNSNIL SLNNPIFIST NYSKDVYFTL 

       190        200        210        220        230        240 
SGCSLYLVPL CLFKSNFSQY YYNMDTGFAY GYSNFVSSDL DCTYISLKSG SYKIFSTGFV 

       250        260        270        280        290        300 
LSIPTKALCF NKSKQFVPVQ VVDSRWNNLR ASDTSLSDAC QLPYCYFRNS SGNYVGKYDI 

       310        320        330        340        350        360 
NHGDNGFTSI LSGLLYNVSC ISYYGSFLYD NFTSIWPRFS FGNCPTSAYI KLNCFYDPLP 

       370        380 
IILQGILLFL ALLFIVFLLF LVYHG 

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References

[1]"Comparative analysis of 22 coronavirus HKU1 genomes reveals a novel genotype and evidence of natural recombination in coronavirus HKU1."
Woo P.C.Y., Lau S.K.P., Yip C.C.Y., Huang Y., Tsoi H.-W., Chan K.-H., Yuen K.-Y.
J. Virol. 80:7136-7145(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ339101 Genomic RNA. Translation: ABC70718.1.

3D structure databases

ProteinModelPortalQ0ZME8.
SMRQ0ZME8. Positions 15-348.
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_CVHN5
AccessionPrimary (citable) accession number: Q0ZME8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: July 24, 2007
Last modified: April 16, 2014
This is version 36 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