P03205 (GP42_EBVB9) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycoprotein 42
Short name=gp42

Gene names

ORF Names:

BZLF2

Organism

Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) [Reference proteome]

Taxonomic identifier

10377 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Gammaherpesvirinae › Lymphocryptovirus › Epstein-Barr virus (strain GD1)

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	223 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Host-virus interaction
Cellular component	Membrane Virion
Domain	Transmembrane Transmembrane helix
Ligand	Lectin
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW virion membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 223

223

Glycoprotein 42

PRO_0000116279

Regions

Topological domain

1 – 8

8

Intravirion Potential

Transmembrane

9 – 29

21

Helical; Potential

Topological domain

30 – 223

194

Virion surface Potential

Domain

111 – 217

107

C-type lectin

Compositional bias

38 – 41

4

Poly-Ala

Compositional bias

57 – 60

4

Poly-Pro

Amino acid modifications

Disulfide bond

99 ↔ 138

Disulfide bond

102 ↔ 115

Disulfide bond

128 ↔ 214

Disulfide bond

132 ↔ 216

Disulfide bond

192 ↔ 208

Experimental info

Mutagenesis

107

1

Y → A: Loss of HLA class II binding and fusion competence. Ref.4

Mutagenesis

125

1

W → G: Loss of HLA class II binding and fusion competence. Ref.4

Mutagenesis

160

1

E → A: Loss of HLA class II binding and fusion competence. Ref.4

Mutagenesis

210

1

F → A: Binds to HLA class II but unable to mediate fusion. Ref.4

Mutagenesis

220

1

R → A: Loss of HLA class II binding and fusion competence. Ref.4

Secondary structure

1

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223

Helix Strand Turn

Details...

Turn

104 – 106

3

Beta strand

108 – 111

4

Beta strand

114 – 118

5

Helix

127 – 135

9

Beta strand

139 – 141

3

Turn

146 – 148

3

Helix

149 – 153

5

Beta strand

161 – 164

4

Beta strand

174 – 176

3

Beta strand

179 – 182

4

Beta strand

187 – 191

5

Beta strand

193 – 198

6

Beta strand

214 – 219

6

Sequences

	Sequence		Length	Mass (Da)
	P03205 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: F87541F6CEC26D74	FASTA	223	25,257
	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

References

	« Hide 'large scale' referencesShow '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.

PIR

QQBE26. F43042.

RefSeq

YP_401672.1. NC_007605.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KG0	X-ray	2.65	C	86-221	[»]
3FD4	X-ray	2.40	A/B	33-223	[»]

ProteinModelPortal

P03205.

SMR

P03205. Positions 86-221.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-6768327.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3783745.

Phylogenomic databases

ProtClustDB

CLSP2512076.

Family and domain databases

Gene3D

3.10.100.10. 1 hit.

InterPro

IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]

SMART

SM00034. CLECT. 1 hit.
[Graphical view]

SUPFAM

SSF56436. C-type_lectin_fold. 1 hit.

PROSITE

PS00615. C_TYPE_LECTIN_1. False negative.
PS50041. C_TYPE_LECTIN_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P03205.

Entry information

Entry name

GP42_EBVB9

Accession

Primary (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:	April 3, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program