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Protein

Hemagglutinin-esterase

Gene

HE

Organism
Bovine coronavirus (strain Mebus) (BCoV) (BCV)
Status
Reviewed-Annotation score: Annotation score: 5 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.1 Publication

Catalytic activityi

N-acetyl-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei40Nucleophile1 Publication1
Active sitei326Charge relay system1 Publication1
Active sitei329Charge relay system1 Publication1

GO - Molecular functioni

  • host cell surface receptor binding Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB
  • sialate O-acetylesterase activity Source: UniProtKB

GO - Biological processi

  • fusion of virus membrane with host plasma membrane Source: InterPro
  • negative regulation of immune system process Source: UniProtKB
  • receptor-mediated virion attachment to host cell Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hemagglutinin, Hydrolase

Enzyme and pathway databases

BRENDAi3.1.1.53. 8724.

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
OrganismiBovine coronavirus (strain Mebus) (BCoV) (BCV)
Taxonomic identifieri11132 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
Proteomesi
  • UP000007554 Componenti: Genome

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.1 Publication

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 392Virion surfaceSequence analysisAdd BLAST374
Transmembranei393 – 413HelicalSequence analysisAdd BLAST21
Topological domaini414 – 424IntravirionSequence analysisAdd BLAST11

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi40S → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi184Y → A: Decreased receptor binding. 1 Publication1
Mutagenesisi211F → A: Loss of receptor binding. 1 Publication1
Mutagenesisi266L → A: Loss of receptor binding; when associated with A-267. 1 Publication1
Mutagenesisi267L → A: Loss of receptor binding; when associated with A-266. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 181 PublicationAdd BLAST18
ChainiPRO_000003713819 – 424Hemagglutinin-esteraseAdd BLAST406

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi44 ↔ 651 Publication
Glycosylationi54N-linked (GlcNAc...); by host1 Publication1
Glycosylationi89N-linked (GlcNAc...); by host1 Publication1
Disulfide bondi113 ↔ 1621 Publication
Glycosylationi153N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi197 ↔ 2761 Publication
Disulfide bondi205 ↔ 2491 Publication
Glycosylationi236N-linked (GlcNAc...); by host1 Publication1
Glycosylationi301N-linked (GlcNAc...); by host1 Publication1
Disulfide bondi307 ↔ 3121 Publication
Glycosylationi316N-linked (GlcNAc...); by host1 Publication1
Disulfide bondi347 ↔ 3711 Publication
Glycosylationi358N-linked (GlcNAc...); by host1 Publication1

Post-translational modificationi

N-glycosylated in the RER.1 Publication

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.1 Publication

GO - Molecular functioni

  • host cell surface receptor binding Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB

Structurei

Secondary structure

1424
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 25Combined sources3
Beta strandi29 – 32Combined sources4
Beta strandi34 – 39Combined sources6
Helixi40 – 42Combined sources3
Helixi44 – 49Combined sources6
Beta strandi50 – 52Combined sources3
Helixi55 – 57Combined sources3
Helixi62 – 64Combined sources3
Beta strandi70 – 73Combined sources4
Helixi78 – 83Combined sources6
Beta strandi84 – 86Combined sources3
Beta strandi95 – 100Combined sources6
Helixi107 – 109Combined sources3
Helixi119 – 137Combined sources19
Beta strandi140 – 147Combined sources8
Beta strandi150 – 152Combined sources3
Beta strandi162 – 164Combined sources3
Beta strandi167 – 169Combined sources3
Beta strandi171 – 175Combined sources5
Beta strandi182 – 184Combined sources3
Beta strandi188 – 207Combined sources20
Beta strandi211 – 213Combined sources3
Beta strandi216 – 218Combined sources3
Beta strandi221 – 226Combined sources6
Turni227 – 229Combined sources3
Beta strandi232 – 236Combined sources5
Beta strandi242 – 244Combined sources3
Beta strandi247 – 270Combined sources24
Beta strandi273 – 280Combined sources8
Beta strandi286 – 289Combined sources4
Helixi302 – 306Combined sources5
Turni309 – 311Combined sources3
Beta strandi312 – 315Combined sources4
Beta strandi323 – 326Combined sources4
Beta strandi329 – 331Combined sources3
Helixi332 – 338Combined sources7
Helixi339 – 342Combined sources4
Beta strandi346 – 349Combined sources4
Beta strandi352 – 355Combined sources4
Beta strandi357 – 359Combined sources3
Beta strandi368 – 370Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CL4X-ray2.10A19-388[»]
3CL5X-ray1.80A19-388[»]
ProteinModelPortaliP15776.
SMRiP15776.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15776.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni7 – 127Esterase domain first partBy similarityAdd BLAST121
Regioni128 – 266Receptor bindingBy similarityAdd BLAST139
Regioni267 – 379Esterase 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.

P15776-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLLLRFVLV SCIIGSLGFD NPPTNVVSHL NGDWFLFGDS RSDCNHVVNT
60 70 80 90 100
NPRNYSYMDL NPALCDSGKI SSKAGNSIFR SFHFTDFYNY TGEGQQIIFY
110 120 130 140 150
EGVNFTPYHA FKCTTSGSND IWMQNKGLFY TQVYKNMAVY RSLTFVNVPY
160 170 180 190 200
VYNGSAQSTA LCKSGSLVLN NPAYIAREAN FGDYYYKVEA DFYLSGCDEY
210 220 230 240 250
IVPLCIFNGK FLSNTKYYDD SQYYFNKDTG VIYGLNSTET ITTGFDFNCH
260 270 280 290 300
YLVLPSGNYL AISNELLLTV PTKAICLNKR KDFTPVQVVD SRWNNARQSD
310 320 330 340 350
NMTAVACQPP YCYFRNSTTN YVGVYDINHG DAGFTSILSG LLYDSPCFSQ
360 370 380 390 400
QGVFRYDNVS SVWPLYSYGR CPTAADINTP DVPICVYDPL PLILLGILLG
410 420
VAVIIIVVLL LYFMVDNGTR LHDA
Length:424
Mass (Da):47,695
Last modified:April 1, 1990 - v1
Checksum:iFDEF70542F91F305
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00735 Genomic RNA. Translation: AAA66393.1.
S50936 Genomic RNA. Translation: AAB19562.1.
PIRiA34666. HMIHBC.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00735 Genomic RNA. Translation: AAA66393.1.
S50936 Genomic RNA. Translation: AAB19562.1.
PIRiA34666. HMIHBC.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CL4X-ray2.10A19-388[»]
3CL5X-ray1.80A19-388[»]
ProteinModelPortaliP15776.
SMRiP15776.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.1.53. 8724.

Miscellaneous databases

EvolutionaryTraceiP15776.

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_CVBM
AccessioniPrimary (citable) accession number: P15776
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 2, 2016
This is version 112 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, Complete proteome, Direct protein sequencing

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.