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P0C0W0

- HEMA_BRV2

UniProt

P0C0W0 - HEMA_BRV2

Protein

Hemagglutinin-esterase

Gene

HE

Organism
Breda virus 2 (BRV-2)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (10 Jan 2006)
      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-di-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. Also hydrolyzes 5-N-acetyl-4-O-acetylneuraminic acid and N-acetyl-9-O-acetylneuraminic acid, but displays a substrate preference for N-acetyl-9-di-O-acetylneuraminic acid. 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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei37 – 371NucleophileBy similarity
    Active sitei325 – 3251Charge relay systemBy similarity
    Active sitei328 – 3281Charge relay systemBy similarity

    GO - Molecular functioni

    1. sialate O-acetylesterase activity Source: UniProtKB-EC

    GO - Biological processi

    1. fusion of virus membrane with host plasma membrane Source: InterPro

    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
    OrganismiBreda virus 2 (BRV-2)
    Taxonomic identifieri360394 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeTorovirinaeTorovirus
    Virus hostiBos taurus (Bovine) [TaxID: 9913]

    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 By similarity.By similarity

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1414Sequence AnalysisAdd
    BLAST
    Chaini15 – 416402Hemagglutinin-esterasePRO_0000045399Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi41 ↔ 57By similarity
    Glycosylationi76 – 761N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi108 ↔ 156By similarity
    Disulfide bondi192 ↔ 273By similarity
    Disulfide bondi200 ↔ 246By similarity
    Glycosylationi257 – 2571N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi278 – 2781N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi304 ↔ 309By similarity
    Glycosylationi313 – 3131N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi322 – 3221N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi343 – 3431N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi346 ↔ 371By similarity

    Post-translational modificationi

    N-glycosylated.Curated

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliP0C0W0.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini15 – 393379Virion surfaceSequence AnalysisAdd
    BLAST
    Topological domaini415 – 4162IntravirionSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei394 – 41421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni4 – 121118Esterase domain first partBy similarityAdd
    BLAST
    Regioni122 – 263142Receptor bindingBy similarityAdd
    BLAST
    Regioni264 – 379116Esterase domain second partBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi61 – 677Poly-Ser
    Compositional biasi402 – 4054Poly-Val

    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.

    P0C0W0-1 [UniParc]FASTAAdd to Basket

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    MLSLILFFPS FAFAATPVTP YYGPGHITFD WCGFGDSRSD CTNPQSPMSL    50
    DIPQQLCPKF SSKSSSSMFL SLHWNNHSSF VSYDYFNCGV EKVFYEGVNF 100
    SPRKQYSCWD EGVDGWIELK TRFYTKLYQM ATTSRCIKLI QLQAPSSLPT 150
    LQAGVCRTNK QLPDNPRLAL LSDTVPTSVQ FVLPGSSGTT ICTKHLVPFC 200
    YLNHGCFTTG GSCLPFGVSY VSDSFYYGYY DATPQIGSTE SHDYVCDYLF 250
    MEPGTYNAST VGKFLVYPTK SYCMDTMNIT VPVQAVQSIW SEQYASDDAI 300
    GQACKAPYCI FYNKTTPYTV TNGSDANHGD DEVRMMMQGL LRNSSCISPQ 350
    GSTPLALYST EMIYEPNYGS CPQFYKLFDT SGNENIDVIS SSYFVATWVL 400
    LVVVVILIFV IISFFC 416
    Length:416
    Mass (Da):46,440
    Last modified:January 10, 2006 - v1
    Checksum:i384C406385439054
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10866 Genomic RNA. Translation: CAA71819.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10866 Genomic RNA. Translation: CAA71819.1 .

    3D structure databases

    ProteinModelPortali P0C0W0.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Hemagglutinin-esterase, a novel structural protein of torovirus."
      Cornelissen L.A.H.M., Wierda C.M.H., van der Meer F.J., Herrewegh A.A.P.M., Horzinek M.C., Egberink H.F., de Groot R.J.
      Virology 71:5277-5286(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], CHARACTERIZATION, SUBCELLULAR LOCATION.
    2. "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.

    Entry informationi

    Entry nameiHEMA_BRV2
    AccessioniPrimary (citable) accession number: P0C0W0
    Secondary accession number(s): O39517
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: January 10, 2006
    Last modified: October 1, 2014
    This is version 48 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3