Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Active sitei44NucleophileBy similarity1
Active sitei334Charge relay systemBy similarity1
Active sitei337Charge relay systemBy similarity1

GO - Molecular functioni

GO - Biological processi

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 virusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostiMus [TaxID: 10088]

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini24 – 399Virion surfaceSequence analysisAdd BLAST376
Transmembranei400 – 420HelicalSequence analysisAdd BLAST21
Topological domaini421 – 431IntravirionSequence analysisAdd BLAST11

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000003714624 – 431Hemagglutinin-esteraseAdd BLAST408

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi48 ↔ 69By similarity
Glycosylationi53N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi93N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi117 ↔ 166By similarity
Glycosylationi151N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi157N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi199N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi205 ↔ 284By similarity
Disulfide bondi213 ↔ 257By similarity
Glycosylationi244N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi248N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi309N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi315 ↔ 320By similarity
Glycosylationi324N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi352N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi355 ↔ 379By similarity
Glycosylationi366N-linked (GlcNAc...); by hostSequence analysis1

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

Secondary structure

1431
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi33 – 36Combined sources4
Beta strandi38 – 42Combined sources5
Helixi44 – 46Combined sources3
Helixi48 – 53Combined sources6
Helixi66 – 70Combined sources5
Beta strandi74 – 76Combined sources3
Helixi82 – 87Combined sources6
Beta strandi88 – 90Combined sources3
Beta strandi99 – 104Combined sources6
Turni111 – 113Combined sources3
Helixi123 – 140Combined sources18
Turni141 – 143Combined sources3
Beta strandi144 – 151Combined sources8
Beta strandi157 – 159Combined sources3
Beta strandi167 – 169Combined sources3
Beta strandi174 – 177Combined sources4
Beta strandi179 – 183Combined sources5
Helixi191 – 193Combined sources3
Beta strandi197 – 202Combined sources6
Beta strandi204 – 218Combined sources15
Beta strandi229 – 234Combined sources6
Turni235 – 237Combined sources3
Beta strandi239 – 244Combined sources6
Beta strandi254 – 262Combined sources9
Beta strandi264 – 270Combined sources7
Beta strandi276 – 278Combined sources3
Beta strandi281 – 288Combined sources8
Beta strandi294 – 297Combined sources4
Helixi310 – 314Combined sources5
Turni317 – 319Combined sources3
Beta strandi320 – 323Combined sources4
Beta strandi332 – 334Combined sources3
Helixi340 – 346Combined sources7
Helixi347 – 350Combined sources4
Beta strandi354 – 357Combined sources4
Beta strandi360 – 363Combined sources4
Beta strandi365 – 367Combined sources3
Beta strandi376 – 378Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5JIFX-ray2.00A/B24-395[»]
ProteinModelPortaliO92367.
SMRiO92367.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni11 – 131Esterase domain first partBy similarityAdd BLAST121
Regioni132 – 274Receptor bindingBy similarityAdd BLAST143
Regioni275 – 387Esterase domain second partBy similarityAdd BLAST113

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:November 1, 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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5JIFX-ray2.00A/B24-395[»]
ProteinModelPortaliO92367.
SMRiO92367.
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...

Entry informationi

Entry nameiHEMA_CVMDV
AccessioniPrimary (citable) accession number: O92367
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: November 1, 1998
Last modified: November 2, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.