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P15776

- HEMA_CVBM

UniProt

P15776 - HEMA_CVBM

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
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    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

    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-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. viral envelope Source: UniProtKB-KW
    4. virion membrane Source: UniProtKB-SubCell

    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

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    MFLLLRFVLV SCIIGSLGFD NPPTNVVSHL NGDWFLFGDS RSDCNHVVNT    50
    NPRNYSYMDL NPALCDSGKI SSKAGNSIFR SFHFTDFYNY TGEGQQIIFY 100
    EGVNFTPYHA FKCTTSGSND IWMQNKGLFY TQVYKNMAVY RSLTFVNVPY 150
    VYNGSAQSTA LCKSGSLVLN NPAYIAREAN FGDYYYKVEA DFYLSGCDEY 200
    IVPLCIFNGK FLSNTKYYDD SQYYFNKDTG VIYGLNSTET ITTGFDFNCH 250
    YLVLPSGNYL AISNELLLTV PTKAICLNKR KDFTPVQVVD SRWNNARQSD 300
    NMTAVACQPP YCYFRNSTTN YVGVYDINHG DAGFTSILSG LLYDSPCFSQ 350
    QGVFRYDNVS SVWPLYSYGR CPTAADINTP DVPICVYDPL PLILLGILLG 400
    VAVIIIVVLL LYFMVDNGTR LHDA 424
    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 1, 2014
    This is version 102 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