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P15776

- HEMA_CVBM

UniProt

P15776 - HEMA_CVBM

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Protein

Hemagglutinin-esterase

Gene

HE

Organism
Bovine coronavirus (strain Mebus) (BCoV) (BCV)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei40 – 401Nucleophile1 Publication
Active sitei326 – 3261Charge relay system1 Publication
Active sitei329 – 3291Charge relay system1 Publication

GO - Molecular functioni

  1. host cell surface receptor binding Source: UniProtKB
  2. protein homodimerization activity Source: UniProtKB
  3. sialate O-acetylesterase activity Source: UniProtKB

GO - Biological processi

  1. fusion of virus membrane with host plasma membrane Source: InterPro
  2. metabolic process Source: UniProtKB
  3. receptor-mediated virion attachment to host cell Source: UniProtKB
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
OrganismiBovine coronavirus (strain Mebus) (BCoV) (BCV)
Taxonomic identifieri11132 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
ProteomesiUP000007554: 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

GO - Cellular componenti

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

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401S → A: Loss of enzyme activity. 1 Publication
Mutagenesisi184 – 1841Y → A: Decreased receptor binding. 1 Publication
Mutagenesisi211 – 2111F → A: Loss of receptor binding. 1 Publication
Mutagenesisi266 – 2661L → A: Loss of receptor binding; when associated with A-267. 1 Publication
Mutagenesisi267 – 2671L → A: Loss of receptor binding; when associated with A-266. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 424406Hemagglutinin-esterasePRO_0000037138Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 651 Publication
Glycosylationi54 – 541N-linked (GlcNAc...); by host1 Publication
Glycosylationi89 – 891N-linked (GlcNAc...); by host1 Publication
Disulfide bondi113 ↔ 1621 Publication
Glycosylationi153 – 1531N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi197 ↔ 2761 Publication
Disulfide bondi205 ↔ 2491 Publication
Glycosylationi236 – 2361N-linked (GlcNAc...); by host1 Publication
Glycosylationi301 – 3011N-linked (GlcNAc...); by host1 Publication
Disulfide bondi307 ↔ 3121 Publication
Glycosylationi316 – 3161N-linked (GlcNAc...); by host1 Publication
Disulfide bondi347 ↔ 3711 Publication
Glycosylationi358 – 3581N-linked (GlcNAc...); by host1 Publication

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

Structurei

Secondary structure

1
424
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 253
Beta strandi29 – 324
Beta strandi34 – 396
Helixi40 – 423
Helixi44 – 496
Beta strandi50 – 523
Helixi55 – 573
Helixi62 – 643
Beta strandi70 – 734
Helixi78 – 836
Beta strandi84 – 863
Beta strandi95 – 1006
Helixi107 – 1093
Helixi119 – 13719
Beta strandi140 – 1478
Beta strandi150 – 1523
Beta strandi162 – 1643
Beta strandi167 – 1693
Beta strandi171 – 1755
Beta strandi182 – 1843
Beta strandi188 – 20720
Beta strandi211 – 2133
Beta strandi216 – 2183
Beta strandi221 – 2266
Turni227 – 2293
Beta strandi232 – 2365
Beta strandi242 – 2443
Beta strandi247 – 27024
Beta strandi273 – 2808
Beta strandi286 – 2894
Helixi302 – 3065
Turni309 – 3113
Beta strandi312 – 3154
Beta strandi323 – 3264
Beta strandi329 – 3313
Helixi332 – 3387
Helixi339 – 3424
Beta strandi346 – 3494
Beta strandi352 – 3554
Beta strandi357 – 3593
Beta strandi368 – 3703

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CL4X-ray2.10A19-388[»]
3CL5X-ray1.80A19-388[»]
ProteinModelPortaliP15776.
SMRiP15776. Positions 19-376.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15776.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 392374Virion surfaceSequence AnalysisAdd
BLAST
Topological domaini414 – 42411IntravirionSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei393 – 41321HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 127121Esterase domain first partBy similarityAdd
BLAST
Regioni128 – 266139Receptor bindingBy similarityAdd
BLAST
Regioni267 – 379113Esterase 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.
[Graphical view]
PfamiPF03996. Hema_esterase. 1 hit.
PF02710. Hema_HEFG. 1 hit.
[Graphical view]
SUPFAMiSSF49818. SSF49818. 1 hit.

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:
EMBL
GenBank
DDBJ
Links Updated
U00735 Genomic RNA. Translation: AAA66393.1.
S50936 Genomic RNA. Translation: AAB19562.1.
PIRiA34666. HMIHBC.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00735 Genomic RNA. Translation: AAA66393.1 .
S50936 Genomic RNA. Translation: AAB19562.1 .
PIRi A34666. HMIHBC.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3CL4 X-ray 2.10 A 19-388 [» ]
3CL5 X-ray 1.80 A 19-388 [» ]
ProteinModelPortali P15776.
SMRi P15776. Positions 19-376.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P15776.

Family and domain databases

InterProi IPR008980. Capsid_hemagglutn.
IPR007142. Hemagglutn-estrase_core.
IPR003860. Hemagglutn-estrase_hemagglutn.
[Graphical view ]
Pfami PF03996. Hema_esterase. 1 hit.
PF02710. Hema_HEFG. 1 hit.
[Graphical view ]
SUPFAMi SSF49818. SSF49818. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Structure and orientation of expressed bovine coronavirus hemagglutinin-esterase protein."
    Kienzle T.E., Abraham S., Hogue B.G., Brian D.A.
    J. Virol. 64:1834-1838(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], SUBCELLULAR LOCATION.
  2. "Structure and expression of the bovine coronavirus hemagglutinin protein."
    Kienzle T.E., Abraham S., Hogue B.G., Brian D.A.
    Adv. Exp. Med. Biol. 276:95-102(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "Synthesis and processing of the bovine enteric coronavirus haemagglutinin protein."
    Hogue B.G., Kienzle T.E., Brian D.A.
    J. Gen. Virol. 70:345-352(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-27.
  4. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "Structure of coronavirus hemagglutinin-esterase offers insight into corona and influenza virus evolution."
    Zeng Q., Langereis M.A., van Vliet A.L., Huizinga E.G., de Groot R.J.
    Proc. Natl. Acad. Sci. U.S.A. 105:9065-9069(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-388 OF APOPROTEIN AND MUTANT ALA-40 IN COMPLEX WITH RECEPTOR, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITES, GLYCOSYLATION AT ASN-54; ASN-89; ASN-236; ASN-301; ASN-316 AND ASN-358, DISULFIDE BONDS, MUTAGENESIS OF SER-40; TYR-184; PHE-211; LEU-266 AND LEU-267.

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: October 29, 2014
This is version 103 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

External Data

Dasty 3