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Protein

Protein BMRF2

Gene

BMRF2

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

Functioni

Facilitates virus attachment to oral epithelial cells by binding to host beta1 integrin family. Participates in rearrangement of cellular actin to increase intercellular contacts by binding BDLF2 and thereby promote virus cell-to-cell spreading.2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Viral attachment to host cell, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Protein BMRF2
Gene namesi
ORF Names:BMRF2
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 – 11Virion surfaceSequence analysisAdd BLAST11
Transmembranei12 – 32Sequence analysisAdd BLAST21
Topological domaini33 – 46Virion surfaceSequence analysisAdd BLAST14
Transmembranei47 – 67Sequence analysisAdd BLAST21
Topological domaini68 – 70Virion surfaceSequence analysis3
Transmembranei71 – 91Sequence analysisAdd BLAST21
Topological domaini92 – 98Virion surfaceSequence analysis7
Transmembranei99 – 121Sequence analysisAdd BLAST23
Topological domaini122 – 133Virion surfaceSequence analysisAdd BLAST12
Transmembranei134 – 154Sequence analysisAdd BLAST21
Topological domaini155 – 158Virion surfaceSequence analysis4
Transmembranei159 – 179Sequence analysisAdd BLAST21
Topological domaini180 – 217Virion surfaceAdd BLAST38
Transmembranei218 – 238Sequence analysisAdd BLAST21
Topological domaini239 – 240Virion surfaceSequence analysis2
Transmembranei241 – 261Sequence analysisAdd BLAST21
Topological domaini262 – 267Virion surfaceSequence analysis6
Transmembranei268 – 288Sequence analysisAdd BLAST21
Topological domaini289 – 298Virion surfaceSequence analysis10
Transmembranei299 – 319Sequence analysisAdd BLAST21
Topological domaini320 – 335Virion surfaceSequence analysisAdd BLAST16
Transmembranei336 – 356Sequence analysisAdd BLAST21
Topological domaini357Virion surfaceSequence analysis1

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001162541 – 357Protein BMRF2Add BLAST357

Post-translational modificationi

Extensively glycosylated by O-linked oligosaccharides.1 Publication

Keywords - PTMi

Glycoprotein

Expressioni

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Interacts with BDLF2. Interacts with host beta1 integrin family.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ITGB1P055562EBI-9348955,EBI-703066From a different organism.

Protein-protein interaction databases

IntActiP03192. 4 interactors.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi199 – 201Integrin binding siteSequence analysis3

Domaini

The RGD motif presumably is the main binding site to host beta1 integrins.

Sequence similaritiesi

Belongs to the herpesviridae BMRF2 family.Curated

Keywords - Domaini

Transmembrane

Family and domain databases

InterProiIPR006727. Herpes_BMRF2.
[Graphical view]
PfamiPF04633. Herpes_BMRF2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P03192-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSCKQHLSL GACVFCLGLL ASTPFIWCFV FANLLSLEIF SPWQTHVYRL
60 70 80 90 100
GFPTACLMAV LWTLVPAKHA VRAVTPAIML NIASALIFFS LRVYSTSTWV
110 120 130 140 150
SAPCLFLANL PLLCLWPRLA IEIVYICPAI HQRFFELGLL LACTIFALSV
160 170 180 190 200
VSRALEVSAV FMSPFFIFLA LGSGSLAGAR RNQIYTSGLE RRRSIFCARG
210 220 230 240 250
DHSVASLKET LHKCPWDLLA ISALTVLVVC VMIVLHVHAE VFFGLSRYLP
260 270 280 290 300
LFLCGAMASG GLYLGHSSII ACVMATLCTL TSVVVYFLHE TLGPLGKTVL
310 320 330 340 350
FISIFVYYFS GVAALSAAMR YKLKKFVNGP LVHLRVVYMC CFVFTFCEYL

LVTFIKS
Length:357
Mass (Da):39,516
Last modified:July 21, 1986 - v1
Checksum:iBDB101894C5980F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24845.1.
M17322 Genomic DNA. Translation: AAA45878.1.
AJ507799 Genomic DNA. Translation: CAD53408.1.
PIRiC43041. QQBE14.
RefSeqiYP_401658.1. NC_007605.1.

Genome annotation databases

GeneIDi3783719.
KEGGivg:3783719.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24845.1.
M17322 Genomic DNA. Translation: AAA45878.1.
AJ507799 Genomic DNA. Translation: CAD53408.1.
PIRiC43041. QQBE14.
RefSeqiYP_401658.1. NC_007605.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP03192. 4 interactors.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3783719.
KEGGivg:3783719.

Family and domain databases

InterProiIPR006727. Herpes_BMRF2.
[Graphical view]
PfamiPF04633. Herpes_BMRF2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBMRF2_EBVB9
AccessioniPrimary (citable) accession number: P03192
Secondary accession number(s): Q777F8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 13, 2016
This is version 75 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

Complete proteome, Reference proteome

Documents

  1. 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.