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P03205 (GP42_EBVB9) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycoprotein 42

Short name=gp42
Gene names
ORF Names:BZLF2
OrganismEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) [Reference proteome]
Taxonomic identifier10377 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length223 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3

Subunit structure

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

Subcellular location

Virion membrane. 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. Ref.5

Domain

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

Sequence similarities

Belongs to the epstein barr virus gp42 family.

Contains 1 C-type lectin domain.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentMembrane
Virion
   DomainTransmembrane
Transmembrane helix
   LigandLectin
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processviral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

virion membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 223223Glycoprotein 42
PRO_0000116279

Regions

Topological domain1 – 88Intravirion Potential
Transmembrane9 – 2921Helical; Potential
Topological domain30 – 223194Virion surface Potential
Domain111 – 217107C-type lectin
Compositional bias38 – 414Poly-Ala
Compositional bias57 – 604Poly-Pro

Amino acid modifications

Disulfide bond99 ↔ 138
Disulfide bond102 ↔ 115
Disulfide bond128 ↔ 214
Disulfide bond132 ↔ 216
Disulfide bond192 ↔ 208

Experimental info

Mutagenesis1071Y → A: Loss of HLA class II binding and fusion competence. Ref.4
Mutagenesis1251W → G: Loss of HLA class II binding and fusion competence. Ref.4
Mutagenesis1601E → A: Loss of HLA class II binding and fusion competence. Ref.4
Mutagenesis2101F → A: Binds to HLA class II but unable to mediate fusion. Ref.4
Mutagenesis2201R → A: Loss of HLA class II binding and fusion competence. Ref.4

Secondary structure

.......................... 223
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03205 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: F87541F6CEC26D74

FASTA22325,257
        10         20         30         40         50         60 
MVSFKQVRVP LFTAIALVIV LLLAYFLPPR VRGGGRVAAA AITWVPKPNV EVWPVDPPPP 

        70         80         90        100        110        120 
VNFNKTAEQE YGDKEVKLPH WTPTLHTFQV PQNYTKANCT YCNTREYTFS YKGCCFYFTK 

       130        140        150        160        170        180 
KKHTWNGCFQ ACAELYPCTY FYGPTPDILP VVTRNLNAIE SLWVGVYRVG EGNWTSLDGG 

       190        200        210        220 
TFKVYQIFGS HCTYVSKFST VPVSHHECSF LKPCLCVSQR SNS 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence and expression of the B95-8 Epstein-Barr virus genome."
Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J., Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C., Tuffnell P.S., Barrell B.G.
Nature 310:207-211(1984) [PubMed] [Europe PMC] [Abstract]
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]"Proteins of purified Epstein-Barr virus."
Johannsen E., Luftig M., Chase M.R., Weicksel S., Cahir-McFarland E., Illanes D., Sarracino D., Kieff E.
Proc. Natl. Acad. Sci. U.S.A. 101:16286-16291(2004) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01555 Genomic DNA. Translation: CAA24860.1.
AJ507799 Genomic DNA. Translation: CAD53422.1.
PIRQQBE26. F43042.
RefSeqYP_401672.1. NC_007605.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KG0X-ray2.65C86-221[»]
3FD4X-ray2.40A/B33-223[»]
ProteinModelPortalP03205.
SMRP03205. Positions 86-221.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid971787. 1 interaction.
MINTMINT-6768327.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3783745.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP03205.

Entry information

Entry nameGP42_EBVB9
AccessionPrimary (citable) accession number: P03205
Secondary accession number(s): Q777E6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references