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 cytomegalovirus (strain Towne) (HHV-5) (Human herpesvirus 5)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Envelope glycoprotein that plays a role in host cell entry, cell to-cell virus transmission, and fusion of infected cells. May be involved in the initial attachment via binding to heparan sulfate together with the gM/gN complex that binds heparin with higher affinity. Interacts with host integrin ITGB1, PDGFRA and EGFR that likely serve as postattachment entry receptors. Participates also in the fusion of viral and cellular membranes leading to virus entry into the host cell. Membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL.4 Publications

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
ORF Names:UL55
OrganismiHuman cytomegalovirus (strain Towne) (HHV-5) (Human herpesvirus 5)
Taxonomic identifieri10363 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeBetaherpesvirinaeCytomegalovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

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 domaini23 – 751Virion surfaceUniRule annotationAdd BLAST729
Transmembranei752 – 772HelicalUniRule annotationAdd BLAST21
Topological domaini773 – 907IntravirionUniRule annotationAdd BLAST135

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 – 22UniRule annotationAdd BLAST22
ChainiPRO_000043664523 – 907Envelope glycoprotein BUniRule annotationAdd BLAST885

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi68N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi73N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi85N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi94 ↔ 551UniRule annotation
Disulfide bondi111 ↔ 507UniRule annotation
Disulfide bondi185 ↔ 250UniRule annotation
Glycosylationi208N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi281N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi286N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi302N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi341N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi344 ↔ 391UniRule annotation
Glycosylationi383N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi405N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi409N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi417N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi447N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi452N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi456N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi466N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi555N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi574 ↔ 611UniRule annotation
Glycosylationi586N-linked (GlcNAc...) asparagine; by hostUniRule annotation1

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei460 – 461Cleavage; 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 (By similarity). Interacts with host C-type lectin CD209/DC-SIGN. Interacts with host ITGB1, EGFR, and PDGFRA.UniRule annotation5 Publications

Structurei

Secondary structure

1907
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi346 – 359Combined sources14
Beta strandi364 – 367Combined sources4
Beta strandi375 – 377Combined sources3
Helixi387 – 389Combined sources3
Turni390 – 392Combined sources3
Helixi393 – 407Combined sources15
Beta strandi413 – 422Combined sources10
Beta strandi428 – 435Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EYFX-ray2.30E/F69-78[»]
4OSNX-ray1.76A114-133[»]
A344-438[»]
4OT1X-ray2.11A114-133[»]
A344-438[»]
5C6TX-ray3.60A87-698[»]
ProteinModelPortaliP13201.
SMRiP13201.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni152 – 158Involved in fusion and/or binding to host membraneUniRule annotation7
Regioni237 – 244Involved in fusion and/or binding to host membraneUniRule annotation8
Regioni697 – 749Hydrophobic membrane proximal regionUniRule annotationAdd BLAST53
Regioni708 – 748Hydrophobic membrane proximal regionAdd BLAST41

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi895 – 898Internalization motifUniRule annotation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi24 – 64Ser-richAdd BLAST41

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.
InterProiView protein in InterPro
IPR021044. Glycoprot_B_antigenic_N.
IPR035377. Glycoprot_B_PH1.
IPR035381. Glycoprot_B_PH2.
IPR000234. Herpes_Glycoprot_B.
PfamiView protein in Pfam
PF17416. Glycoprot_B_PH1. 1 hit.
PF17417. Glycoprot_B_PH2. 1 hit.
PF12154. HCMVantigenic_N. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P13201-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESRIWCLVV CVNLCIVCLG AAVSSSSTRG TSATHSHHSS HTTSAAHSRS
60 70 80 90 100
GSVSQRVTSS QTVSHGVNET IYNTTLKYGD VVGVNTTKYP YRVCSMAQGT
110 120 130 140 150
DLIRFERNIV CTSMKPINED LDEGIMVVYK RNIVAHTFKV RVYQKVLTFR
160 170 180 190 200
RSYAYIHTTY LLGSNTEYVA PPMWEIHHIN SHSQCYSSYS RVIAGTVFVA
210 220 230 240 250
YHRDSYENKT MQLMPDDYSN THSTRYVTVK DQWHSRGSTW LYRETCNLNC
260 270 280 290 300
MVTITTARSK YPYHFFATST GDVVDISPFY NGTNRNASYF GENADKFFIF
310 320 330 340 350
PNYTIVSDFG RPNSALETHR LVAFLERADS VISWDIQDEK NVTCQLTFWE
360 370 380 390 400
ASERTIRSEA EDSYHFSSAK MTATFLSKKQ EVNMSDSALD CVRDEAINKL
410 420 430 440 450
QQIFNTSYNQ TYEKYGNVSV FETTGGLVVF WQGIKQKSLV ELERLANRSS
460 470 480 490 500
LNLTHNRTKR STDGNNATHL SNMESVHNLV YAQLQFTYDT LRGYINRALA
510 520 530 540 550
QIAEAWCVDQ RRTLEVFKEL SKINPSAILS AIYNKPIAAR FMGDVLGLAS
560 570 580 590 600
CVTINQTSVK VLRDMNVKES PGRCYSRPVV IFNFANSSYV QYGQLGEDNE
610 620 630 640 650
ILLGNHRTEE CQLPSLKIFI AGNSAYEYVD YLFKRMIDLS SISTVDSMIA
660 670 680 690 700
LDIDPLENTD FRVLELYSQK ELRSSNVFDL EEIMREFNSY KQRVKYVEDK
710 720 730 740 750
VVDPLPPYLK GLDDLMSGLG AAGKAVGVAI GAVGGAVASV VEGVATFLKN
760 770 780 790 800
PFGAFTIILV AIAVVIIIYL IYTRQRRLCM QPLQNLFPYL VSADGTTVTS
810 820 830 840 850
GNTKDTSLQA PPSYEESVYN SGRKGPGPPS SDASTAAPPY TNEQAYQMLL
860 870 880 890 900
ALVRLDAEQR AQQNGTDSLD GQTGTQDKGQ KPNLLDRLRH RKNGYRHLKD

SDEEENV
Length:907
Mass (Da):101,954
Last modified:January 1, 1990 - v1
Checksum:iE6F07B7742D359A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22343 mRNA. Translation: AAA45920.1.
PIRiA31288. VGBETE.

Similar proteinsi

Entry informationi

Entry nameiGB_HCMVT
AccessioniPrimary (citable) accession number: P13201
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 22, 2017
This is version 85 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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families