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P03205

- GP42_EBVB9

UniProt

P03205 - GP42_EBVB9

Protein

Glycoprotein 42

Gene

BZLF2

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Plays a role in virion attachment to host B-lymphocytes, through binding to leukocyte antigen (HLA) class II and subsequently participates in fusion of the virion with host membranes. May act as a tropism switch that directs fusion with B-lymphocytes and inhibits fusion with epithelial cells.1 Publication

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro

    GO - Biological processi

    1. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction

    Keywords - Ligandi

    Lectin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycoprotein 42
    Short name:
    gp42
    Gene namesi
    ORF Names:BZLF2
    OrganismiEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
    Taxonomic identifieri10377 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007640: Genome

    Subcellular locationi

    Virion membrane 1 Publication
    Note: virions synthesized in B-lymphocytes contain a lower amount of gp42 due to sequestration by cellular HLA class II protein, whereas virions made from epithelial cells has a higher amount of gp42. Membrane; Single-pass membrane protein Potential.Curated

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. virion membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Membrane, Virion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi107 – 1071Y → A: Loss of HLA class II binding and fusion competence. 1 Publication
    Mutagenesisi125 – 1251W → G: Loss of HLA class II binding and fusion competence. 1 Publication
    Mutagenesisi160 – 1601E → A: Loss of HLA class II binding and fusion competence. 1 Publication
    Mutagenesisi210 – 2101F → A: Binds to HLA class II but unable to mediate fusion. 1 Publication
    Mutagenesisi220 – 2201R → A: Loss of HLA class II binding and fusion competence. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 223223Glycoprotein 42PRO_0000116279Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi99 ↔ 138
    Disulfide bondi102 ↔ 115
    Disulfide bondi128 ↔ 214
    Disulfide bondi132 ↔ 216
    Disulfide bondi192 ↔ 208

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Forms a complex with gp25 and gp85 via its N-terminus; this complex is used for invasion of B-lymphocytes.

    Protein-protein interaction databases

    BioGridi971787. 1 interaction.
    MINTiMINT-6768327.

    Structurei

    Secondary structure

    1
    223
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni104 – 1063
    Beta strandi108 – 1114
    Beta strandi114 – 1185
    Helixi127 – 1359
    Beta strandi139 – 1413
    Turni146 – 1483
    Helixi149 – 1535
    Beta strandi161 – 1644
    Beta strandi174 – 1763
    Beta strandi179 – 1824
    Beta strandi187 – 1915
    Beta strandi193 – 1986
    Beta strandi214 – 2196

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KG0X-ray2.65C86-221[»]
    3FD4X-ray2.40A/B33-223[»]
    ProteinModelPortaliP03205.
    SMRiP03205. Positions 86-221.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03205.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 88IntravirionSequence Analysis
    Topological domaini30 – 223194Virion surfaceSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei9 – 2921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini111 – 217107C-type lectinAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi38 – 414Poly-Ala
    Compositional biasi57 – 604Poly-Pro

    Domaini

    The C-lectin type domain is essential for virion-induced membrane fusion.

    Sequence similaritiesi

    Belongs to the epstein barr virus gp42 family.Curated
    Contains 1 C-type lectin domain.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Family and domain databases

    Gene3Di3.10.100.10. 1 hit.
    InterProiIPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    [Graphical view]
    PfamiPF00059. Lectin_C. 1 hit.
    [Graphical view]
    SMARTiSM00034. CLECT. 1 hit.
    [Graphical view]
    SUPFAMiSSF56436. SSF56436. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P03205-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVSFKQVRVP LFTAIALVIV LLLAYFLPPR VRGGGRVAAA AITWVPKPNV    50
    EVWPVDPPPP VNFNKTAEQE YGDKEVKLPH WTPTLHTFQV PQNYTKANCT 100
    YCNTREYTFS YKGCCFYFTK KKHTWNGCFQ ACAELYPCTY FYGPTPDILP 150
    VVTRNLNAIE SLWVGVYRVG EGNWTSLDGG TFKVYQIFGS HCTYVSKFST 200
    VPVSHHECSF LKPCLCVSQR SNS 223
    Length:223
    Mass (Da):25,257
    Last modified:July 21, 1986 - v1
    Checksum:iF87541F6CEC26D74
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01555 Genomic DNA. Translation: CAA24860.1.
    AJ507799 Genomic DNA. Translation: CAD53422.1.
    PIRiF43042. QQBE26.
    RefSeqiYP_401672.1. NC_007605.1.

    Genome annotation databases

    GeneIDi3783745.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01555 Genomic DNA. Translation: CAA24860.1 .
    AJ507799 Genomic DNA. Translation: CAD53422.1 .
    PIRi F43042. QQBE26.
    RefSeqi YP_401672.1. NC_007605.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KG0 X-ray 2.65 C 86-221 [» ]
    3FD4 X-ray 2.40 A/B 33-223 [» ]
    ProteinModelPortali P03205.
    SMRi P03205. Positions 86-221.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 971787. 1 interaction.
    MINTi MINT-6768327.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3783745.

    Miscellaneous databases

    EvolutionaryTracei P03205.

    Family and domain databases

    Gene3Di 3.10.100.10. 1 hit.
    InterProi IPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    [Graphical view ]
    Pfami PF00059. Lectin_C. 1 hit.
    [Graphical view ]
    SMARTi SM00034. CLECT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56436. SSF56436. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Epstein-Barr virus uses different complexes of glycoproteins gH and gL to infect B lymphocytes and epithelial cells."
      Wang X., Kenyon W.J., Li Q., Mullberg J., Hutt-Fletcher L.M.
      J. Virol. 72:5552-5558(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GP25 AND GP85.
    3. "Alternate replication in B cells and epithelial cells switches tropism of Epstein-Barr virus."
      Borza C.M., Hutt-Fletcher L.M.
      Nat. Med. 8:594-599(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "Mutational analyses of Epstein-Barr virus glycoprotein 42 reveal functional domains not involved in receptor binding but required for membrane fusion."
      Silva A.L., Omerovic J., Jardetzky T.S., Longnecker R.
      J. Virol. 78:5946-5956(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-107; TRP-125; GLU-160; PHE-210 AND ARG-220.
    5. Cited for: SUBCELLULAR LOCATION.
    6. "Structure of the Epstein-Barr virus gp42 protein bound to the MHC class II receptor HLA-DR1."
      Mullen M.M., Haan K.M., Longnecker R., Jardetzky T.S.
      Mol. Cell 9:375-385(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 86-221.

    Entry informationi

    Entry nameiGP42_EBVB9
    AccessioniPrimary (citable) accession number: P03205
    Secondary accession number(s): Q777E6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 82 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