Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Envelope glycoprotein B

Gene

gB

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 (By similarity). Also plays a role, together with gK, in virus-induced cell-to-cell fusion (syncytia formation).UniRule annotation1 Publication

GO - Biological processi

Keywordsi

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

Protein family/group databases

TCDBi1.G.10.1.1 the herpes simplex virus membrane fusion complex (hsv-mfc) family

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein BUniRule annotation
Short name:
gBUniRule annotation
Gene namesi
Name:gBUniRule annotation
ORF Names:UL27
OrganismiHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifieri10299 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000009294 Componenti: Genome
  • UP000180652 Componenti: Genome

Subcellular locationi

  • Virion membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • Host cell membrane UniRule annotation1 Publication; 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 domaini31 – 774Virion surfaceUniRule annotationAdd BLAST744
Transmembranei775 – 795HelicalUniRule annotationAdd BLAST21
Topological domaini796 – 904IntravirionUniRule annotationAdd BLAST109

GO - Cellular componenti

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2364696

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30UniRule annotationAdd BLAST30
ChainiPRO_000003816031 – 904Envelope glycoprotein BUniRule annotationAdd BLAST874

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi87N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi116 ↔ 573UniRule annotation
Disulfide bondi133 ↔ 529UniRule annotation
Glycosylationi141N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi207 ↔ 271UniRule annotation
Disulfide bondi364 ↔ 412UniRule annotation
Glycosylationi398N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi430N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi489N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi596 ↔ 633UniRule annotation
Glycosylationi674N-linked (GlcNAc...) asparagine; by hostUniRule annotation1

Post-translational modificationi

The cytoplasmic tail is phosphorylated by the viral kinase US3. Phosphorylation may be linked to a down-regulation of gB expression on cell surface (By similarity).By similarity
ubiquitinated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Ubl conjugation

Proteomic databases

PRIDEiP10211

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi971469, 1 interactor

Structurei

3D structure databases

ProteinModelPortaliP10211
SMRiP10211
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni173 – 179Involved in fusion and/or binding to host membraneUniRule annotation7
Regioni258 – 265Involved in fusion and/or binding to host membraneUniRule annotation8
Regioni719 – 772Hydrophobic membrane proximal regionUniRule annotationAdd BLAST54

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi849 – 852Golgi targetingUniRule annotation4
Motifi889 – 892Internalization motifUniRule annotation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi51 – 83Pro-richAdd BLAST33
Compositional biasi476 – 484Poly-Pro9

Sequence similaritiesi

Belongs to the herpesviridae glycoprotein B family.UniRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

OrthoDBiVOG0900002K

Family and domain databases

Gene3Di2.30.29.100, 1 hit
HAMAPiMF_04032 HSV_GB, 1 hit
InterProiView protein in InterPro
IPR035377 Glycoprot_B_PH1
IPR035381 Glycoprot_B_PH2
IPR038631 Glycoprot_B_PH2_sf
IPR000234 Herpes_Glycoprot_B
PfamiView protein in Pfam
PF17416 Glycoprot_B_PH1, 1 hit
PF17417 Glycoprot_B_PH2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P10211-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRQGAPARGR RWFVVWALLG LTLGVLVASA APSSPGTPGV AAATQAANGG
60 70 80 90 100
PATPAPPAPG APPTGDPKPK KNRKPKPPKP PRPAGDNATV AAGHATLREH
110 120 130 140 150
LRDIKAENTD ANFYVCPPPT GATVVQFEQP RRCPTRPEGQ NYTEGIAVVF
160 170 180 190 200
KENIAPYKFK ATMYYKDVTV SQVWFGHRYS QFMGIFEDRA PVPFEEVIDK
210 220 230 240 250
INAKGVCRST AKYVRNNLET TAFHRDDHET DMELKPANAA TRTSRGWHTT
260 270 280 290 300
DLKYNPSRVE AFHRYGTTVN CIVEEVDARS VYPYDEFVLA TGDFVYMSPF
310 320 330 340 350
YGYREGSHTE HTSYAADRFK QVDGFYARDL TTKARATAPT TRNLLTTPKF
360 370 380 390 400
TVAWDWVPKR PSVCTMTKWQ EVDEMLRSEY GGSFRFSSDA ISTTFTTNLT
410 420 430 440 450
EYPLSRVDLG DCIGKDARDA MDRIFARRYN ATHIKVGQPQ YYLANGGFLI
460 470 480 490 500
AYQPLLSNTL AELYVREHLR EQSRKPPNPT PPPPGASANA SVERIKTTSS
510 520 530 540 550
IEFARLQFTY NHIQRHVNDM LGRVAIAWCE LQNHELTLWN EARKLNPNAI
560 570 580 590 600
ASATVGRRVS ARMLGDVMAV STCVPVAADN VIVQNSMRIS SRPGACYSRP
610 620 630 640 650
LVSFRYEDQG PLVEGQLGEN NELRLTRDAI EPCTVGHRRY FTFGGGYVYF
660 670 680 690 700
EEYAYSHQLS RADITTVSTF IDLNITMLED HEFVPLEVYT RHEIKDSGLL
710 720 730 740 750
DYTEVQRRNQ LHDLRFADID TVIHADANAA MFAGLGAFFE GMGDLGRAVG
760 770 780 790 800
KVVMGIVGGV VSAVSGVSSF MSNPFGALAV GLLVLAGLAA AFFAFRYVMR
810 820 830 840 850
LQSNPMKALY PLTTKELKNP TNPDASGEGE EGGDFDEAKL AEAREMIRYM
860 870 880 890 900
ALVSAMERTE HKAKKKGTSA LLSAKVTDMV MRKRRNTNYT QVPNKDGDAD

EDDL
Length:904
Mass (Da):100,292
Last modified:July 1, 1989 - v1
Checksum:i2C14E8B1284C1F3A
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti73R → K. 1
Natural varianti80P → L in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti555V → M in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti572T → M in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti668S → N in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti817L → P in strain: Nonneuroinvasive mutant HF10. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA Translation: CAA32320.1
DQ889502 Genomic DNA Translation: ABI63489.1
FJ593289 Genomic DNA Translation: ACM62250.1
PIRiI30084 VGBEW7
RefSeqiYP_009137102.1, NC_001806.2

Genome annotation databases

GeneIDi24271469
KEGGivg:24271469

Similar proteinsi

Entry informationi

Entry nameiGB_HHV11
AccessioniPrimary (citable) accession number: P10211
Secondary accession number(s): B9VQF5, Q09IA6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: March 28, 2018
This is version 100 of the entry and version 1 of the sequence. See 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health