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Protein

Hemagglutinin-esterase

Gene

HE

Organism
Murine coronavirus (strain DVIM) (MHV-DVIM) (Murine hepatitis virus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

N-acetyl-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei44 – 441NucleophileBy similarity
Active sitei334 – 3341Charge relay systemBy similarity
Active sitei337 – 3371Charge relay systemBy similarity

GO - Molecular functioni

  1. sialate O-acetylesterase activity Source: UniProtKB-EC

GO - Biological processi

  1. fusion of virus membrane with host plasma membrane Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hemagglutinin, Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Hemagglutinin-esterase (EC:3.1.1.53)
Short name:
HE protein
Alternative name(s):
E3 glycoprotein
Gene namesi
Name:HE
ORF Names:2b
OrganismiMurine coronavirus (strain DVIM) (MHV-DVIM) (Murine hepatitis virus)
Taxonomic identifieri231423 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostiMus [TaxID: 10088]

Subcellular locationi

Virion membrane Curated; Single-pass type I membrane protein Curated. Host cell membrane Curated; Single-pass type I membrane protein Curated
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).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 399376Virion surfaceSequence AnalysisAdd
BLAST
Transmembranei400 – 42021HelicalSequence AnalysisAdd
BLAST
Topological domaini421 – 43111IntravirionSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. viral envelope Source: UniProtKB-KW
  4. virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 431408Hemagglutinin-esterasePRO_0000037146Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi48 ↔ 69By similarity
Glycosylationi53 – 531N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi93 – 931N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi117 ↔ 166By similarity
Glycosylationi151 – 1511N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi157 – 1571N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi199 – 1991N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi205 ↔ 284By similarity
Disulfide bondi213 ↔ 257By similarity
Glycosylationi244 – 2441N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi248 – 2481N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi309 – 3091N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi315 ↔ 320By similarity
Glycosylationi324 – 3241N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi352 – 3521N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi355 ↔ 379By similarity
Glycosylationi366 – 3661N-linked (GlcNAc...); by hostSequence Analysis

Post-translational modificationi

N-glycosylated in the RER.

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

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.

Structurei

3D structure databases

ProteinModelPortaliO92367.
SMRiO92367. Positions 25-384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 131121Esterase domain first partBy similarityAdd
BLAST
Regioni132 – 274143Receptor bindingBy similarityAdd
BLAST
Regioni275 – 387113Esterase domain second partBy similarityAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR008980. Capsid_hemagglutn.
IPR007142. Hemagglutn-estrase_core.
IPR003860. Hemagglutn-estrase_hemagglutn.
IPR013830. SGNH_hydro.
[Graphical view]
PfamiPF03996. Hema_esterase. 1 hit.
PF02710. Hema_HEFG. 1 hit.
[Graphical view]
SUPFAMiSSF49818. SSF49818. 1 hit.
SSF52266. SSF52266. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O92367-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARTDAMAPR TLLLVLSLGY AFGFNEPLNV VSHLNDDWFL FGDSRSDCNH
60 70 80 90 100
INNLSQQNYN YMDINPELCK SGKISAKAGN SLFKSFHFTD FYNYTGEGSQ
110 120 130 140 150
IIFYEGVNFT PYVGFKCLNN GDNNRWMGNK ARFYTQLYQK MAHYRSLSVI
160 170 180 190 200
NITYTYNGSA GPVSMCKHIA NGVTLTLNNP TFIGKEVSKP DYYYESEANF
210 220 230 240 250
TLQGCDEFIV PLCVFNGQYL SSKLYYDDSQ YYYNVDTGVL YGFNSTLNIT
260 270 280 290 300
SGLDLTCIYL ALTPGNYISI SNELLLTVPS KAICLRKPKA FTPVQVVDSR
310 320 330 340 350
WHSNRQSDNM TAIACQLPYC YFRNTTSDYN GVYDSHHGDA GFTSILAGLM
360 370 380 390 400
YNVSCLAQQG AFVYNNVSSS WPQYPYGHCP TAANIVFMAP VCMYDPLPVI
410 420 430
LLGVLLGIAV LIIVFLMFYF MTDSGVRLHE A
Length:431
Mass (Da):48,440
Last modified:October 31, 1998 - v1
Checksum:iDF4BE9EE0AE7301B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF091734 mRNA. Translation: AAC63044.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF091734 mRNA. Translation: AAC63044.1.

3D structure databases

ProteinModelPortaliO92367.
SMRiO92367. Positions 25-384.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR008980. Capsid_hemagglutn.
IPR007142. Hemagglutn-estrase_core.
IPR003860. Hemagglutn-estrase_hemagglutn.
IPR013830. SGNH_hydro.
[Graphical view]
PfamiPF03996. Hema_esterase. 1 hit.
PF02710. Hema_HEFG. 1 hit.
[Graphical view]
SUPFAMiSSF49818. SSF49818. 1 hit.
SSF52266. SSF52266. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "Sequence of the hemagglutinin-esterase (HE) genes of two enterotropic MHV strains."
    Compton S.R., Moore K.M.
    Submitted (AUG-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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiHEMA_CVMDV
AccessioniPrimary (citable) accession number: O92367
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2003
Last sequence update: October 31, 1998
Last modified: March 31, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.