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Protein

Envelope glycoprotein B

Gene

gB

Organism
Tupaiid herpesvirus (strain 2) (TuHV-2) (Herpesvirus tupaia (strain 2))
Status
Reviewed-Annotation score: -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

Keywordsi

Biological processHost-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
OrganismiTupaiid herpesvirus (strain 2) (TuHV-2) (Herpesvirus tupaia (strain 2))
Taxonomic identifieri132678 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeBetaherpesvirinae
Virus hostiTupaia belangeri (Common tree shrew) (Tupaia glis belangeri) [TaxID: 37347]

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 domaini56 – 785Virion surfaceUniRule annotationAdd BLAST730
Transmembranei786 – 806HelicalUniRule annotationAdd BLAST21
Topological domaini807 – 944IntravirionUniRule annotationAdd BLAST138

GO - Cellular componenti

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 – 55Sequence analysisAdd BLAST55
ChainiPRO_000003818456 – 944Envelope glycoprotein BAdd BLAST889

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi114N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi125 ↔ 577UniRule annotation
Disulfide bondi142 ↔ 533UniRule annotation
Disulfide bondi215 ↔ 280UniRule annotation
Glycosylationi238N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi369N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi372 ↔ 420UniRule annotation
Glycosylationi409N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi414N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi426N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi481N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi485N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi608 ↔ 645UniRule annotation
Glycosylationi620N-linked (GlcNAc...) asparagine; by hostUniRule annotation1

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei491 – 492Cleavage; by host furinSequence analysis2

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ9WRL5
SMRiQ9WRL5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni182 – 188Involved in fusion and/or binding to host membraneUniRule annotation7
Regioni267 – 274Involved in fusion and/or binding to host membraneUniRule annotation8
Regioni731 – 783Hydrophobic membrane proximal regionUniRule annotationAdd BLAST53
Regioni762 – 782Hydrophobic membrane proximal regionAdd BLAST21

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi931 – 934Internalization motifUniRule annotation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi70 – 85Gly-richAdd BLAST16

Sequence similaritiesi

Belongs to the herpesviridae glycoprotein B family.UniRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

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.

Q9WRL5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPPPPLRRQ RLLLPRPSRR RPPARLASGR RSSRPGSSWT WYATLIASLV
60 70 80 90 100
WYPTVSSTTL EATVVSSTDG GATGQASGGG GGGAGDSTPS ESPETSADTT
110 120 130 140 150
VPRERVTGTE WVSNLTSERY PYRICSMSQG TDIVRFARTI TCAPYDAKSV
160 170 180 190 200
STEGIMLIYK ANIVPYTFDV FTYQKELFFQ RSYAYIYTTY LLGNSREHVA
210 220 230 240 250
LPLWEVDAAN IWNYCYSSYV RTIGTEQYVS YHQDSYRNET MWLIPEEYQS
260 270 280 290 300
GNTRRYVTVK DQYHVYGSTW LYKETCSMNC IVTQTKAKSK YPYDYFALSS
310 320 330 340 350
GLVVEASPFY DTVNGHTFHE NRRKFHVREQ YRMLERFGAV NAPVRVVPKM
360 370 380 390 400
AFLERPDIVL AWEIKEPKNV TCHLALWETV NRAIRTEHAT SFHFVSRGLT
410 420 430 440 450
ATFVTAKANE TLYNNSRYDC IRDSANRTID RVFREEYDGK YELDGDPVIF
460 470 480 490 500
TTNGGLTVVW QGLRQKALAA LSALAGIPGA NGTTNHSRHR RDTAAIAARE
510 520 530 540 550
HASDLTYAQL QFAYDTIRDY VNQAIGHIAE AWCLEQRRTG EMLHELSKIN
560 570 580 590 600
PSSMLTAIYD RPIAARLAGD VIALAKCVEV DQDTVQVQRD MRKFETSVDG
610 620 630 640 650
TEEQGQFCYS RPVVLFRFVN SSETQYGQLG EDNEILLGTF RTEACQLPSL
660 670 680 690 700
KIFVAGKVAY EYRDYLYKRQ IDLDSIDVVN TMISLKVEPL ENTDFQVLEL
710 720 730 740 750
YSRGELKSAN VFDLEDIMRE YNAHKLRLRY ITSKIVNPIP PFMRGLDDFM
760 770 780 790 800
SGLGAAGKGL GLVLGAVGGA VASVVGGFVS FFTNPFGSLT LIILVVAVVV
810 820 830 840 850
IVFLLYQRQR SAVRQPLDFF FPYLAQQTQR HQQTVTTTEY LDSPPPYAER
860 870 880 890 900
DSYKSGPPDP AAEGLGGSGA LPGSSATAAT KYTTEDAWQM LLAIRRLDEE
910 920 930 940
KREVPTMVAP SARPPSQQGP GLLDRIRRRG YRRLRDTGSD SELA
Length:944
Mass (Da):106,060
Last modified:November 1, 1999 - v1
Checksum:i1B063A4CD1561EE2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF084543 Genomic DNA Translation: AAD42935.1

Similar proteinsi

Entry informationi

Entry nameiGB_TUHV2
AccessioniPrimary (citable) accession number: Q9WRL5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: March 28, 2018
This is version 65 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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