UniProtKB - P15776 (HEMA_CVBM)
Protein
Hemagglutinin-esterase
Gene
HE
Organism
Bovine coronavirus (strain Mebus) (BCoV) (BCV)
Status
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-4-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. May become a target for both the humoral and the cellular branches of the immune system.UniRule annotation1 Publication
Catalytic activityi
- H2O + N-acetyl-9-O-acetylneuraminate = acetate + H+ + N-acetylneuraminateUniRule annotation1 PublicationEC:3.1.1.53UniRule annotation1 Publication
- H2O + N-acetyl-4-O-acetylneuraminate = acetate + H+ + N-acetylneuraminateUniRule annotation1 PublicationEC:3.1.1.53UniRule annotation1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 40 | NucleophileUniRule annotation1 Publication | 1 | |
Active sitei | 326 | Charge relay systemUniRule annotation | 1 | |
Active sitei | 329 | Charge relay systemUniRule annotation | 1 |
GO - Molecular functioni
- host cell surface receptor binding Source: UniProtKB
- identical protein binding Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
- sialate O-acetylesterase activity Source: UniProtKB
- signaling receptor binding Source: UniProtKB
GO - Biological processi
- fusion of virus membrane with host plasma membrane Source: UniProtKB-UniRule
- negative regulation of immune system process Source: UniProtKB
- receptor-mediated virion attachment to host cell Source: UniProtKB
Keywordsi
Molecular function | Hemagglutinin, Hydrolase |
Enzyme and pathway databases
BRENDAi | 3.1.1.53, 8724 |
Names & Taxonomyi
Protein namesi | Recommended name: Hemagglutinin-esteraseUniRule annotation (EC:3.1.1.53UniRule annotation)Short name: HE proteinUniRule annotation Alternative name(s): E3 glycoproteinUniRule annotation |
Gene namesi | Name:HEUniRule annotation ORF Names:2b |
Organismi | Bovine coronavirus (strain Mebus) (BCoV) (BCV) |
Taxonomic identifieri | 11132 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Nidovirales › Cornidovirineae › Coronaviridae › Orthocoronavirinae › Betacoronavirus › Embecovirus › |
Virus hosti | Bos taurus (Bovine) [TaxID: 9913] |
Proteomesi |
|
Subcellular locationi
- Virion membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
- Host cell membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation 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.UniRule annotation1 Publication
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 17 – 392 | Virion surfaceUniRule annotationAdd BLAST | 376 | |
Transmembranei | 393 – 413 | HelicalUniRule annotationAdd BLAST | 21 | |
Topological domaini | 414 – 424 | IntravirionUniRule annotationAdd BLAST | 11 |
GO - Cellular componenti
- host cell plasma membrane Source: UniProtKB-SubCell
- integral component of membrane Source: UniProtKB-UniRule
- viral envelope Source: UniProtKB-UniRule
- virion membrane Source: UniProtKB-SubCell
Keywords - Cellular componenti
Host cell membrane, Host membrane, Membrane, Viral envelope protein, VirionPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 40 | S → A: Loss of enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 184 | Y → A: Decreased receptor binding. 1 Publication | 1 | |
Mutagenesisi | 211 | F → A: Loss of receptor binding. 1 Publication | 1 | |
Mutagenesisi | 266 | L → A: Loss of receptor binding; when associated with A-267. 1 Publication | 1 | |
Mutagenesisi | 267 | L → A: Loss of receptor binding; when associated with A-266. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 18 | 1 PublicationAdd BLAST | 18 | |
Signal peptidei | 1 – 16 | UniRule annotationAdd BLAST | 16 | |
ChainiPRO_0000037138 | 17 – 424 | Hemagglutinin-esteraseUniRule annotationAdd BLAST | 408 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 44 ↔ 65 | UniRule annotation1 Publication | ||
Glycosylationi | 54 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication | 1 | |
Glycosylationi | 89 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication | 1 | |
Disulfide bondi | 113 ↔ 162 | UniRule annotation1 Publication | ||
Glycosylationi | 153 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Disulfide bondi | 197 ↔ 276 | UniRule annotation1 Publication | ||
Disulfide bondi | 205 ↔ 249 | UniRule annotation1 Publication | ||
Glycosylationi | 236 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication | 1 | |
Glycosylationi | 301 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication | 1 | |
Disulfide bondi | 307 ↔ 312 | UniRule annotation1 Publication | ||
Glycosylationi | 316 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication | 1 | |
Disulfide bondi | 347 ↔ 371 | UniRule annotation1 Publication | ||
Glycosylationi | 358 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication | 1 | |
Glycosylationi | 417 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 |
Post-translational modificationi
N-glycosylated in the host RER.UniRule annotation1 Publication
Keywords - PTMi
Disulfide bond, GlycoproteinPTM databases
iPTMneti | P15776 |
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.
UniRule annotation1 PublicationGO - Molecular functioni
- identical protein binding Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
- signaling receptor binding Source: UniProtKB
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P15776 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P15776 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 7 – 127 | Esterase domain 1UniRule annotationAdd BLAST | 121 | |
Regioni | 128 – 266 | Receptor bindingUniRule annotationAdd BLAST | 139 | |
Regioni | 267 – 379 | Esterase domain 2UniRule annotationAdd BLAST | 113 |
Sequence similaritiesi
Belongs to the influenza type C/coronaviruses hemagglutinin-esterase family.UniRule annotation
Keywords - Domaini
Signal, Transmembrane, Transmembrane helixFamily and domain databases
HAMAPi | MF_04207, BETA_CORONA_HE, 1 hit |
InterProi | View protein in InterPro IPR008980, Capsid_hemagglutn IPR042545, HEMA IPR007142, Hemagglutn-estrase_core IPR003860, Hemagglutn-estrase_hemagglutn |
Pfami | View protein in Pfam PF03996, Hema_esterase, 1 hit PF02710, Hema_HEFG, 1 hit |
SUPFAMi | SSF49818, SSF49818, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P15776-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00735 Genomic RNA Translation: AAA66393.1 S50936 Genomic RNA Translation: AAB19562.1 |
PIRi | A34666, HMIHBC |
Similar proteinsi
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 |
PIRi | A34666, HMIHBC |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3CL4 | X-ray | 2.10 | A | 19-388 | [»] | |
3CL5 | X-ray | 1.80 | A | 19-388 | [»] | |
SMRi | P15776 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
PTM databases
iPTMneti | P15776 |
Enzyme and pathway databases
BRENDAi | 3.1.1.53, 8724 |
Miscellaneous databases
EvolutionaryTracei | P15776 |
Family and domain databases
HAMAPi | MF_04207, BETA_CORONA_HE, 1 hit |
InterProi | View protein in InterPro IPR008980, Capsid_hemagglutn IPR042545, HEMA IPR007142, Hemagglutn-estrase_core IPR003860, Hemagglutn-estrase_hemagglutn |
Pfami | View protein in Pfam PF03996, Hema_esterase, 1 hit PF02710, Hema_HEFG, 1 hit |
SUPFAMi | SSF49818, SSF49818, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | HEMA_CVBM | |
Accessioni | P15776Primary (citable) accession number: P15776 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1990 |
Last sequence update: | April 1, 1990 | |
Last modified: | December 2, 2020 | |
This is version 127 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families