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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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111Virion surfaceSequence analysisAdd
BLAST
Transmembranei12 – 3221Sequence analysisAdd
BLAST
Topological domaini33 – 4614Virion surfaceSequence analysisAdd
BLAST
Transmembranei47 – 6721Sequence analysisAdd
BLAST
Topological domaini68 – 703Virion surfaceSequence analysis
Transmembranei71 – 9121Sequence analysisAdd
BLAST
Topological domaini92 – 987Virion surfaceSequence analysis
Transmembranei99 – 12123Sequence analysisAdd
BLAST
Topological domaini122 – 13312Virion surfaceSequence analysisAdd
BLAST
Transmembranei134 – 15421Sequence analysisAdd
BLAST
Topological domaini155 – 1584Virion surfaceSequence analysis
Transmembranei159 – 17921Sequence analysisAdd
BLAST
Topological domaini180 – 21738Virion surfaceAdd
BLAST
Transmembranei218 – 23821Sequence analysisAdd
BLAST
Topological domaini239 – 2402Virion surfaceSequence analysis
Transmembranei241 – 26121Sequence analysisAdd
BLAST
Topological domaini262 – 2676Virion surfaceSequence analysis
Transmembranei268 – 28821Sequence analysisAdd
BLAST
Topological domaini289 – 29810Virion surfaceSequence analysis
Transmembranei299 – 31921Sequence analysisAdd
BLAST
Topological domaini320 – 33516Virion surfaceSequence analysisAdd
BLAST
Transmembranei336 – 35621Sequence analysisAdd
BLAST
Topological domaini357 – 3571Virion surfaceSequence analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 357357Protein BMRF2PRO_0000116254Add
BLAST

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 interactions.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi199 – 2013Integrin binding siteSequence analysis

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 interactions.

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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Characterization of a cDNA clone corresponding to a transcript from the Epstein-Barr virus BamHI M fragment: evidence for overlapping mRNAs."
    Pfitzner A.J., Strominger J.L., Speck S.H.
    J. Virol. 61:2943-2946(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Identification of a protein encoded in the EB-viral open reading frame BMRF2."
    Modrow S., Hoflacher B., Wolf H.
    Arch. Virol. 127:379-386(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, SUBCELLULAR LOCATION.
  4. "Epstein-Barr virus infection of polarized tongue and nasopharyngeal epithelial cells."
    Tugizov S.M., Berline J.W., Palefsky J.M.
    Nat. Med. 9:307-314(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST BETA1 INTEGRIN FAMILY.
  5. Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION.
  6. "A gamma-herpesvirus glycoprotein complex manipulates actin to promote viral spread."
    Gill M.B., Edgar R., May J.S., Stevenson P.G.
    PLoS ONE 3:E1808-E1808(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Characterization of the Epstein-Barr virus glycoprotein BMRF-2."
    Xiao J., Palefsky J.M., Herrera R., Tugizov S.M.
    Virology 359:382-396(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, GLYCOSYLATION.
  8. "The Epstein-Barr virus BMRF-2 protein facilitates virus attachment to oral epithelial cells."
    Xiao J., Palefsky J.M., Herrera R., Berline J., Tugizov S.M.
    Virology 370:430-442(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "The BDLF2 protein of Epstein-Barr virus is a type II glycosylated envelope protein whose processing is dependent on coexpression with the BMRF2 protein."
    Gore M., Hutt-Fletcher L.M.
    Virology 383:162-167(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BDLF2.

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.