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P0C0V9

- HEMA_BRV1

UniProt

P0C0V9 - HEMA_BRV1

Protein

Hemagglutinin-esterase

Gene

HE

Organism
Breda virus 1 (BRV-1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 54 (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.1 Publication

    Catalytic activityi

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

    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

    GO - Biological processi

    1. fusion of virus membrane with host plasma membrane Source: InterPro
    2. metabolic process 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
    OrganismiBreda virus 1 (BRV-1)
    Taxonomic identifieri360393 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeTorovirinaeTorovirus
    Virus hostiBos taurus (Bovine) [TaxID: 9913]
    ProteomesiUP000000355: 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 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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi64 – 641S → T: Strongly reduced activity toward 7,9-di-O-acetylated sialic acids and strongly increased activity toward 9-mono-O-acetylated sialic acids. 1 Publication
    Mutagenesisi103 – 1031R → H: Strongly reduced activity toward both 7,9-di and 9-mono-O-acetylated sialic acids. Increased activity toward synthetic substrate (4-nitrophenyl)acetate. 1 Publication
    Mutagenesisi109 – 1091W → A: Reduced lectin activity. 1 Publication
    Mutagenesisi168 – 1681L → A: Reduced lectin activity. 1 Publication
    Mutagenesisi170 – 1701L → A: Reduced lectin activity. 1 Publication
    Mutagenesisi207 – 2071F → A: Loss of lectin activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1414Sequence AnalysisAdd
    BLAST
    Chaini15 – 416402Hemagglutinin-esterasePRO_0000045398Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi41 ↔ 571 Publication
    Glycosylationi76 – 761N-linked (GlcNAc...); by host1 Publication
    Disulfide bondi88 ↔ 1361 Publication
    Disulfide bondi200 ↔ 2461 Publication
    Disulfide bondi206 ↔ 2131 Publication
    Glycosylationi257 – 2571N-linked (GlcNAc...); by host1 Publication
    Glycosylationi278 – 2781N-linked (GlcNAc...); by host1 Publication
    Disulfide bondi304 ↔ 3091 Publication
    Glycosylationi313 – 3131N-linked (GlcNAc...); by host1 Publication
    Glycosylationi322 – 3221N-linked (GlcNAc...); by host1 Publication
    Glycosylationi343 – 3431N-linked (GlcNAc...); by host1 Publication
    Disulfide bondi346 ↔ 3711 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-48962N.

    Structurei

    Secondary structure

    1
    416
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi21 – 233
    Beta strandi27 – 293
    Beta strandi31 – 366
    Helixi37 – 393
    Turni44 – 496
    Helixi54 – 596
    Beta strandi60 – 623
    Helixi68 – 736
    Beta strandi86 – 883
    Beta strandi90 – 956
    Helixi102 – 1043
    Beta strandi108 – 1114
    Helixi112 – 13120
    Beta strandi135 – 1417
    Beta strandi151 – 1533
    Beta strandi164 – 17310
    Beta strandi177 – 1837
    Beta strandi185 – 1873
    Beta strandi193 – 20210
    Beta strandi207 – 2093
    Beta strandi212 – 2143
    Beta strandi216 – 2227
    Beta strandi225 – 2317
    Beta strandi244 – 2518
    Beta strandi253 – 26715
    Beta strandi269 – 2746
    Beta strandi283 – 2864
    Helixi299 – 3035
    Turni306 – 3083
    Beta strandi309 – 3124
    Beta strandi320 – 3256
    Beta strandi328 – 3303
    Helixi331 – 3377
    Helixi338 – 3414
    Beta strandi345 – 3484
    Beta strandi351 – 3533
    Beta strandi357 – 3615
    Beta strandi368 – 3703
    Helixi375 – 3784

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3I26X-ray1.80A/B/C/D15-392[»]
    3I27X-ray2.00A/B/C/D15-392[»]
    ProteinModelPortaliP0C0V9.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C0V9.

    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.

    P0C0V9-1 [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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti29 – 291F → S.
    Natural varianti114 – 1141D → G.
    Natural varianti133 – 1331T → I.
    Natural varianti152 – 1521Q → K.
    Natural varianti155 – 1551V → E.
    Natural varianti159 – 1591N → K.
    Natural varianti214 – 2141L → R.
    Natural varianti234 – 2341P → S.
    Natural varianti238 – 2381S → L.
    Natural varianti416 – 4161C → V.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF076621 Genomic RNA. Translation: AAD03842.1.
    AY427798 Genomic RNA. Translation: AAS17961.1.
    RefSeqiYP_337909.1. NC_007447.1.

    Genome annotation databases

    GeneIDi3707767.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF076621 Genomic RNA. Translation: AAD03842.1 .
    AY427798 Genomic RNA. Translation: AAS17961.1 .
    RefSeqi YP_337909.1. NC_007447.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3I26 X-ray 1.80 A/B/C/D 15-392 [» ]
    3I27 X-ray 2.00 A/B/C/D 15-392 [» ]
    ProteinModelPortali P0C0V9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48962N.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3707767.

    Miscellaneous databases

    EvolutionaryTracei P0C0V9.

    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. "Bovine torovirus: sequencing of the structural genes and expression of the nucleocapsid protein of Breda virus."
      Duckmanton L.M., Tellier R., Liu P., Petric M.
      Virus Res. 58:83-96(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "The complete sequence of the bovine torovirus genome."
      Draker R., Roper R.L., Petric M., Tellier R.
      Virus Res. 115:56-68(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "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.
    4. "Structural basis for ligand and substrate recognition by torovirus hemagglutinin esterases."
      Langereis M.A., Zeng Q., Gerwig G.J., Frey B., von Itzstein M., Kamerling J.P., de Groot R.J., Huizinga E.G.
      Proc. Natl. Acad. Sci. U.S.A. 106:15897-15902(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 15-392 OF APOPROTEIN AND IN COMPLEX WITH RECEPTOR ANALOG, FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-76; ASN-257; ASN-278; ASN-313; ASN-322 AND ASN-343, DISULFIDE BONDS, MUTAGENESIS OF SER-64; ARG-103; TRP-109; LEU-168; LEU-170 AND PHE-207.

    Entry informationi

    Entry nameiHEMA_BRV1
    AccessioniPrimary (citable) accession number: P0C0V9
    Secondary accession number(s): O39517, Q3T8I8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: January 10, 2006
    Last modified: October 1, 2014
    This is version 54 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, Reference proteome

    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