Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q5MQD1 (HEMA_CVHN1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 50. 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
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:2
OrganismHuman coronavirus HKU1 (isolate N1) (HCoV-HKU1) [Complete proteome]
Taxonomic identifier443239 [NCBI]
Taxonomic lineageViruses › ssRNA positive-strand viruses, no DNA stage › Nidovirales › Coronaviridae › Coronavirinae › Betacoronavirus ›
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length386 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 N1 belongs to genotype A.

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 – 386373Hemagglutinin-esterase
PRO_0000297761

Regions

Topological domain14 – 358345Virion surface Potential
Transmembrane359 – 37921Helical; Potential
Topological domain380 – 3867Intravirion Potential
Region1 – 121121Esterase domain first part By similarity
Region122 – 236115Receptor binding By similarity
Region237 – 349113Esterase domain second part By similarity

Sites

Active site341Nucleophile By similarity
Active site2021Charge relay system By similarity
Active site2991Charge 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
Glycosylation1681N-linked (GlcNAc...); by host Potential
Glycosylation1931N-linked (GlcNAc...); by host Potential
Glycosylation2861N-linked (GlcNAc...); by host Potential
Glycosylation3141N-linked (GlcNAc...); by host Potential
Glycosylation3281N-linked (GlcNAc...); by host Potential
Disulfide bond38 ↔ 59 By similarity
Disulfide bond107 ↔ 154 By similarity
Disulfide bond180 ↔ 246 By similarity
Disulfide bond188 ↔ 219 By similarity
Disulfide bond277 ↔ 282 By similarity
Disulfide bond317 ↔ 341 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5MQD1 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 8A880856BCDE8818

FASTA38644,679
        10         20         30         40         50         60 
MLIIFLFFYF CYGFNEPLNV VSHLNHDWFL FGDSRSDCNH INNLKIKNFD YLDIHPSLCN 

        70         80         90        100        110        120 
NGKISSSAGD SIFKSFHFTR FYNYTGEGDQ IIFYEGVNFN PYHRFKCFPN GSNDVWLLNK 

       130        140        150        160        170        180 
VRFYRALYSN MAFFRYLTFV DIPYNVSLSK FNSCKSDILS LNNPIFINYS KEVYFTLLGC 

       190        200        210        220        230        240 
SLYLVPLCLF KSNFSQYYYN IDTGSVYGFS NVVYPDLDCI YISLKPGSYK VSTTAPFLSL 

       250        260        270        280        290        300 
PTKALCFDKS KQFVPVQVVD SRWNNERASD ISLSVACQLP YCYFRNSSAN YVGKYDINHG 

       310        320        330        340        350        360 
DSGFISILSG LLYNVSCISY YGVFLYDNFT SIWPYYSFGR CPTSSIIKHP ICVYDFLPII 

       370        380 
LQGILLCLAL LFVVFLLFLL YNDKSH

« Hide

References

[1]"Characterization and complete genome sequence of a novel coronavirus, coronavirus HKU1, from patients with pneumonia."
Woo P.C.Y., Lau S.K.P., Chu C.-M., Chan K.-H., Tsoi H.-W., Huang Y., Wong B.H.L., Poon R.W.S., Cai J.J., Luk W.-K., Poon L.L.M., Wong S.S.Y., Guan Y., Peiris J.S.M., Yuen K.-Y.
J. Virol. 79:884-895(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY597011 Genomic RNA. Translation: AAT98579.1.
RefSeqYP_173237.1. NC_006577.2.

3D structure databases

ProteinModelPortalQ5MQD1.
SMRQ5MQD1. Positions 15-345.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3200425.

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_CVHN1
AccessionPrimary (citable) accession number: Q5MQD1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: February 1, 2005
Last modified: May 29, 2013
This is version 50 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents