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Protein

Envelope glycoprotein B

Gene

gB

Organism
Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Envelope glycoprotein that forms spikes at the surface of the virion envelope. Participates in viral entry through an RGD motif that binds ITGAV-ITGB3. 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.3 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:
Envelope glycoprotein BUniRule annotation
Short name:
gBUniRule annotation
Gene namesi
Name:gBUniRule annotation
Synonyms:ORF8
OrganismiHuman herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Taxonomic identifieri868565 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeRhadinovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000000942 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)DescriptionActionsGraphical viewLength
Topological domaini27 – 732Virion surfaceUniRule annotationAdd BLAST706
Transmembranei733 – 753HelicalUniRule annotationAdd BLAST21
Topological domaini754 – 845IntravirionUniRule annotationAdd BLAST92

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26UniRule annotationAdd BLAST26
ChainiPRO_000042390527 – 845Envelope glycoprotein BUniRule annotationAdd BLAST819

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi68 ↔ 528UniRule annotation
Disulfide bondi85 ↔ 484UniRule annotation
Disulfide bondi157 ↔ 222UniRule annotation
Glycosylationi179N-linked (GlcNAc...); by hostUniRule annotation1
Glycosylationi254N-linked (GlcNAc...); by hostUniRule annotation1
Glycosylationi275N-linked (GlcNAc...); by hostUniRule annotation1
Disulfide bondi315 ↔ 362UniRule annotation
Glycosylationi355N-linked (GlcNAc...); by hostUniRule annotation1
Glycosylationi368N-linked (GlcNAc...); by hostUniRule annotation1
Glycosylationi372N-linked (GlcNAc...); by hostUniRule annotation1
Glycosylationi385N-linked (GlcNAc...); by hostUniRule annotation1
Glycosylationi408N-linked (GlcNAc...); by hostUniRule annotation1
Glycosylationi455N-linked (GlcNAc...); by hostUniRule annotation1
Disulfide bondi550 ↔ 587UniRule annotation
Glycosylationi562N-linked (GlcNAc...); by hostUniRule annotation1
Glycosylationi599N-linked (GlcNAc...); by hostUniRule annotation1
Glycosylationi614N-linked (GlcNAc...); by hostUniRule annotation1
Glycosylationi628N-linked (GlcNAc...); by hostUniRule annotation1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotrimer; disulfide-linked. Binds to heparan sulfate proteoglycans. Interacts with gH/gL heterodimer (By similarity). Interacts with host ITGAV-ITGB3; this interaction mediates viral entry.UniRule annotationBy similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ITGB3P051062EBI-9027696,EBI-702847From a different organism.

Protein-protein interaction databases

IntActiF5HB81. 1 interactor.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni124 – 130Involved in fusion and/or binding to host membraneUniRule annotation7
Regioni208 – 216Involved in fusion and/or binding to host membraneUniRule annotation9
Regioni678 – 730Hydrophobic membrane proximal regionUniRule annotationAdd BLAST53

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi830 – 833Internalization motifUniRule annotation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi448 – 451Poly-Gly4

Sequence similaritiesi

Belongs to the herpesviridae glycoprotein B family.UniRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK19255.

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.

F5HB81-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPRSRLATL GTVILLVCFC AGAAHSRGDT FQTSSSPTPP GSSSKAPTKP
60 70 80 90 100
GEEASGPKSV DFYQFRVCSA SITGELFRFN LEQTCPDTKD KYHQEGILLV
110 120 130 140 150
YKKNIVPHIF KVRRYRKIAT SVTVYRGLTE SAITNKYELP RPVPLYEISH
160 170 180 190 200
MDSTYQCFSS MKVNVNGVEN TFTDRDDVNT TVFLQPVEGL TDNIQRYFSQ
210 220 230 240 250
PVIYAEPGWF PGIYRVRTTV NCEIVDMIAR SAEPYNYFVT SLGDTVEVSP
260 270 280 290 300
FCYNESSCST TPSNKNGLSV QVVLNHTVVT YSDRGTSPTP QNRIFVETGA
310 320 330 340 350
YTLSWASESK TTAVCPLALW KTFPRSIQTT HEDSFHFVAN EITATFTAPL
360 370 380 390 400
TPVANFTDTY SCLTSDINTT LNASKAKLAS THVPNGTVQY FHTTGGLYLV
410 420 430 440 450
WQPMSAINLT HAQGDSGNPT SSPPPSASPM TTSASRRKRR SASTAAAGGG
460 470 480 490 500
GSTDNLSYTQ LQFAYDKLRD GINQVLEELS RAWCREQVRD NLMWYELSKI
510 520 530 540 550
NPTSVMTAIY GRPVSAKFVG DAISVTECIN VDQSSVNIHK SLRTNSKDVC
560 570 580 590 600
YARPLVTFKF LNSSNLFTGQ LGARNEIILT NNQVETCKDT CEHYFITRNE
610 620 630 640 650
TLVYKDYAYL RTINTTDIST LNTFIALNLS FIQNIDFKAI ELYSSAEKRL
660 670 680 690 700
ASSVFDLETM FREYNYYTHR LAGLREDLDN TIDMNKERFV RDLSEIVADL
710 720 730 740 750
GGIGKTVVNV ASSVVTLCGS LVTGFINFIK HPLGGMLMII IVIAIILIIF
760 770 780 790 800
MLSRRTNTIA QAPVKMIYPD VDRRAPPSGG APTREEIKNI LLGMHQLQQE
810 820 830 840
ERQKADDLKK STPSVFQRTA NGLRQRLRGY KPLTQSLDIS PETGE
Length:845
Mass (Da):93,985
Last modified:June 28, 2011 - v1
Checksum:iC44A5F2FF29B1E41
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF148805 Genomic DNA. Translation: ABD28851.1.
RefSeqiYP_001129354.1. NC_009333.1.

Genome annotation databases

GeneIDi4961501.
KEGGivg:4961501.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF148805 Genomic DNA. Translation: ABD28851.1.
RefSeqiYP_001129354.1. NC_009333.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiF5HB81. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi4961501.
KEGGivg:4961501.

Phylogenomic databases

KOiK19255.

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_HHV8P
AccessioniPrimary (citable) accession number: F5HB81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: June 28, 2011
Last modified: September 7, 2016
This is version 18 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.