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Protein

Glycoprotein 42

Gene

BZLF2

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Additionally, hampers T-cell recognition via HLA class II molecules through steric hindrance of T-cell receptor-class II-peptide interaction.3 Publications
Soluble gp42 inhibits HLA class II-restricted antigen presentation to T-cells through binding to immature and mature HLA class II complexes.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei33 – 34Potential cleavageCurated2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Glycoprotein 42
Short name:
gp42
Cleaved into the following chain:
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]
Proteomesi
  • UP000007640 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 8IntravirionSequence analysis8
Transmembranei9 – 29HelicalSequence analysisAdd BLAST21
Topological domaini30 – 223Virion surfaceSequence analysisAdd BLAST194

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host membrane, Membrane, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi107Y → A: Loss of HLA class II binding and fusion competence. 1 Publication1
Mutagenesisi125W → G: Loss of HLA class II binding and fusion competence. 1 Publication1
Mutagenesisi160E → A: Loss of HLA class II binding and fusion competence. 1 Publication1
Mutagenesisi210F → A: Binds to HLA class II but unable to mediate fusion. 1 Publication1
Mutagenesisi220R → A: Loss of HLA class II binding and fusion competence. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001162791 – 223Glycoprotein 42Add BLAST223
ChainiPRO_000043322634 – 223Soluble gp42Add BLAST190

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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. Interacts with human HLA-DRA and HLA-DRB1.4 Publications

Protein-protein interaction databases

BioGridi971787. 1 interactor.
IntActiP03205. 1 interactor.
MINTiMINT-6768327.

Structurei

Secondary structure

1223
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni104 – 106Combined sources3
Beta strandi108 – 111Combined sources4
Beta strandi114 – 118Combined sources5
Helixi127 – 135Combined sources9
Beta strandi139 – 141Combined sources3
Turni146 – 148Combined sources3
Helixi149 – 153Combined sources5
Beta strandi161 – 164Combined sources4
Beta strandi174 – 176Combined sources3
Beta strandi179 – 182Combined sources4
Beta strandi187 – 191Combined sources5
Beta strandi193 – 198Combined sources6
Beta strandi214 – 219Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KG0X-ray2.65C86-221[»]
3FD4X-ray2.40A/B33-223[»]
ProteinModelPortaliP03205.
SMRiP03205.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03205.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini111 – 217C-type lectinAdd BLAST107

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi38 – 41Poly-Ala4
Compositional biasi57 – 60Poly-Pro4

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.
InterProiIPR016186. C-type_lectin-like/link.
IPR016187. CTDL_fold.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P03205-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSFKQVRVP LFTAIALVIV LLLAYFLPPR VRGGGRVAAA AITWVPKPNV
60 70 80 90 100
EVWPVDPPPP VNFNKTAEQE YGDKEVKLPH WTPTLHTFQV PQNYTKANCT
110 120 130 140 150
YCNTREYTFS YKGCCFYFTK KKHTWNGCFQ ACAELYPCTY FYGPTPDILP
160 170 180 190 200
VVTRNLNAIE SLWVGVYRVG EGNWTSLDGG TFKVYQIFGS HCTYVSKFST
210 220
VPVSHHECSF LKPCLCVSQR SNS
Length:223
Mass (Da):25,257
Last modified:July 21, 1986 - v1
Checksum:iF87541F6CEC26D74
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
KEGGivg:3783745.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24860.1.
AJ507799 Genomic DNA. Translation: CAD53422.1.
PIRiF43042. QQBE26.
RefSeqiYP_401672.1. NC_007605.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KG0X-ray2.65C86-221[»]
3FD4X-ray2.40A/B33-223[»]
ProteinModelPortaliP03205.
SMRiP03205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi971787. 1 interactor.
IntActiP03205. 1 interactor.
MINTiMINT-6768327.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3783745.
KEGGivg:3783745.

Miscellaneous databases

EvolutionaryTraceiP03205.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR016186. C-type_lectin-like/link.
IPR016187. CTDL_fold.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
ProtoNetiSearch...

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: November 30, 2016
This is version 95 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.