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Protein

Envelope glycoprotein B

Gene

gB

Organism
Epstein-Barr virus (strain GD1) (HHV-4) (Human herpesvirus 4)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moities of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress.UniRule annotation

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:
Envelope glycoprotein BUniRule annotation
Short name:
gBUniRule annotation
Gene namesi
Name:gBUniRule annotation
ORF Names:BALF4
OrganismiEpstein-Barr virus (strain GD1) (HHV-4) (Human herpesvirus 4)
Taxonomic identifieri10376 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007641 Componenti: Genome

Subcellular locationi

  • Virion membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • Host cell membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • Host endosome membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • Host Golgi apparatus membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation

  • Note: During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN).UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 732711Virion surfaceUniRule annotationAdd
BLAST
Transmembranei733 – 75321HelicalUniRule annotationAdd
BLAST
Topological domaini754 – 857104IntravirionUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host endosome, Host Golgi apparatus, Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121UniRule annotationAdd
BLAST
Chaini22 – 857836Envelope glycoprotein BUniRule annotationPRO_0000385468Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 528UniRule annotation
Disulfide bondi68 ↔ 484UniRule annotation
Glycosylationi76 – 761N-linked (GlcNAc...); by hostUniRule annotation
Disulfide bondi141 ↔ 206UniRule annotation
Glycosylationi163 – 1631N-linked (GlcNAc...); by hostUniRule annotation
Glycosylationi290 – 2901N-linked (GlcNAc...); by hostUniRule annotation
Disulfide bondi295 ↔ 342UniRule annotation
Glycosylationi329 – 3291N-linked (GlcNAc...); by hostUniRule annotation
Glycosylationi348 – 3481N-linked (GlcNAc...); by hostUniRule annotation
Glycosylationi395 – 3951N-linked (GlcNAc...); by hostUniRule annotation
Glycosylationi436 – 4361N-linked (GlcNAc...); by hostUniRule annotation
Disulfide bondi551 ↔ 588UniRule annotation
Glycosylationi563 – 5631N-linked (GlcNAc...); by hostUniRule annotation
Glycosylationi629 – 6291N-linked (GlcNAc...); by hostUniRule annotation

Post-translational modificationi

A proteolytic cleavage by host furin generates two subunits that remain linked by disulfide bonds.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei432 – 4332Cleavage; by host furinSequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotrimer; disulfide-linked. Binds to heparan sulfate proteoglycans. Interacts with gH/gL heterodimer.UniRule annotation

Protein-protein interaction databases

IntActiP0C762. 15 interactions.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni108 – 1147Involved in fusion and/or binding to host membraneUniRule annotation
Regioni192 – 2009Involved in fusion and/or binding to host membraneUniRule annotation
Regioni678 – 73053Hydrophobic membrane proximal regionUniRule annotationAdd
BLAST
Regioni709 – 72921Hydrophobic membrane proximal regionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi402 – 41615Pro-richAdd
BLAST
Compositional biasi428 – 4325Poly-Arg
Compositional biasi836 – 8394Poly-Arg

Sequence similaritiesi

Belongs to the herpesviridae glycoprotein B family.UniRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Family and domain databases

HAMAPiMF_04032. HSV_GB. 1 hit.
InterProiIPR000234. Herpes_Glycoprot_B.
[Graphical view]
PfamiPF00606. Glycoprotein_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0C762-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRRRVLSVV VLLAALACRL GAQTPEQPAP PATTVQPTAT RQQTSFPFRV
60 70 80 90 100
CELSSHGDLF RFSSDIQCPS FGTRENHTEG LLMVFKDNII PYSFKVRSYT
110 120 130 140 150
KIVTNILIYN GWYADSVTNR HEEKFSVDSY ETDQMDTIYQ CYNAVKMTKD
160 170 180 190 200
GLTRVYVDRD GVNITVNLKP TGGLANGVRR YASQTELYDA PGWLIWTYRT
210 220 230 240 250
RTTVNCLITD MMAKSNSPFD FFVTTTGQTV EMSPFYDGKN KETFHERADS
260 270 280 290 300
FHVRTNYKIV DYDNRGTNPQ GERRAFLDKG TYTLSWKLEN RTAYCPLQHW
310 320 330 340 350
QTFDSTIATE TGKSIHFVTD EGTSSFVTNT TVGIELPDAF KCIEEQVNKT
360 370 380 390 400
MHEKYEAVQD RYTKGQEAIT YFITSGGLLL AWLPLTPRSL ATVKNLTELT
410 420 430 440 450
TPTSSPPSSP SPPAPPAARG STSAAVLRRR RRDAGNATTP VPPAAPGKSL
460 470 480 490 500
GTLNNPATVQ IQFAYDSLRR QINRMLGDLA RAWCLEQKRQ NMVLRELTKI
510 520 530 540 550
NPTTVMSSIY GKAVAAKRLG DVISVSQCVP VNQATVTLRK SMRVPGSETM
560 570 580 590 600
CYSRPLVSFS FINDTKTYEG QLGTDNEIFL TKKMTEVCQA TSQYYFQSGN
610 620 630 640 650
EIHVYNDYHH FKTIELDGIA TLQTFISLNT SLIENIDFAS LELYSRDEQR
660 670 680 690 700
ASNVFDLEGI FREYNFQAQN IAGLRKDLDN AVSNGRNQFV DGLGELMDSL
710 720 730 740 750
GSVGQSITNL VSTVGGLFSS LVSGFISFFK NPFGGMLILV LVAGVVILVI
760 770 780 790 800
SLTRRTRQMS QQPVQMLYPG IDELAQQHAS GEGPGINPIS KTELQAIMLA
810 820 830 840 850
LHEQNQEQKR AAQRAAGPSV ASRALQAARD RFPGLRRRRY HDPETAAALL

GEAETEF
Length:857
Mass (Da):95,609
Last modified:September 22, 2009 - v1
Checksum:i928490D0B9EB8488
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY961628 Genomic DNA. Translation: AAY41155.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY961628 Genomic DNA. Translation: AAY41155.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0C762. 15 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

HAMAPiMF_04032. HSV_GB. 1 hit.
InterProiIPR000234. Herpes_Glycoprot_B.
[Graphical view]
PfamiPF00606. Glycoprotein_B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGB_EBVG
AccessioniPrimary (citable) accession number: P0C762
Secondary accession number(s): Q3KSP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 22, 2009
Last modified: September 7, 2016
This is version 21 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

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.