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P03205

- GP42_EBVB9

UniProt

P03205 - GP42_EBVB9

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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: 4 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.1 Publication

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. viral process Source: UniProtKB-KW
Complete GO annotation...

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
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 Reviewed prediction.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88Intravirion Reviewed prediction
Transmembranei9 – 2921Helical; Reviewed prediction
Add
BLAST
Topological domaini30 – 223194Virion surface Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

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 42
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP03205.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini111 – 217107C-type lectin
Add
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

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...

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

« Hide 'large scale' publications
  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: May 14, 2014
This is version 81 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

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