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P06437 (GB_HHV1K) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Envelope glycoprotein B

Short name=gB
Alternative name(s):
gB-1
gB1
Gene names
Name:gB
ORF Names:UL27
OrganismHuman herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifier10306 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length904 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 of gD to one of its receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress. Also plays a role, together with gK, in virus-induced cell-to-cell fusion (syncytia formation). Ref.5

Subunit structure

Homotrimer; disulfide-linked. Interacts with the host coreceptor PILRA. Binds to heparan sulfate proteoglycans. Interacts with gD. Interacts with gH/gL heterodimer. Associates with the gB-gH/gL-gD complex By similarity. Ref.6 Ref.7

Subcellular location

Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity. Host endosome membrane; Single-pass type I membrane protein By similarity. Host Golgi apparatus membrane; Single-pass type I membrane protein By similarity. 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) By similarity.

Post-translational modification

The cytoplasmic tail is phosphorylated by the viral kinase US3. Phosphorylation may be linked to a down-regulation of gB expression on cell surface. Ref.8 Ref.9

ubiquitinated By similarity.

Sequence similarities

Belongs to the herpesviridae glycoprotein B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 904874Envelope glycoprotein B
PRO_0000038162

Regions

Topological domain31 – 774744Virion surface Potential
Transmembrane775 – 79521Helical; Potential
Topological domain796 – 904109Intravirion Potential
Region173 – 1797Involved in fusion and/or binding to host membrane Potential
Region258 – 2658Involved in fusion and/or binding to host membrane Potential
Region719 – 77254Hydrophobic membrane proximal region
Motif849 – 8524Internalization motif Potential
Compositional bias51 – 8333Pro-rich
Compositional bias476 – 4849Poly-Pro

Amino acid modifications

Modified residue8871Phosphothreonine Ref.8 Ref.9
Glycosylation871N-linked (GlcNAc...); by host Potential
Glycosylation1411N-linked (GlcNAc...); by host Potential
Glycosylation3981N-linked (GlcNAc...); by host Potential
Glycosylation4301N-linked (GlcNAc...); by host Potential
Glycosylation4891N-linked (GlcNAc...); by host Potential
Glycosylation6741N-linked (GlcNAc...); by host Potential
Disulfide bond116 ↔ 573
Disulfide bond133 ↔ 529
Disulfide bond207 ↔ 271
Disulfide bond364 ↔ 412
Disulfide bond596 ↔ 633

Experimental info

Mutagenesis1741W → R: 90% loss of fusion with host cell. Ref.10
Mutagenesis1791Y → S: Complete loss of fusion with host cell. Ref.10
Mutagenesis2631H → A: 50% loss of fusion with host cell. Ref.10
Mutagenesis2641R → A: 70% loss of fusion with host cell. Ref.10
Mutagenesis8871T → A: Defects in nuclear egress. Ref.8 Ref.9

Secondary structure

.......................................................................................................... 904
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06437 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: B97B7F8DE5FBA299

FASTA904100,368
        10         20         30         40         50         60 
MHQGAPSWGR RWFVVWALLG LTLGVLVASA APTSPGTPGV AAATQAANGG PATPAPPPLG 

        70         80         90        100        110        120 
AAPTGDPKPK KNKKPKNPTP PRPAGDNATV AAGHATLREH LRDIKAENTD ANFYVCPPPT 

       130        140        150        160        170        180 
GATVVQFEQP RRCPTRPEGQ NYTEGIAVVF KENIAPYKFK ATMYYKDVTV SQVWFGHRYS 

       190        200        210        220        230        240 
QFMGIFEDRA PVPFEEVIDK INAKGVCRST AKYVRNNLET TAFHRDDHET DMELKPANAA 

       250        260        270        280        290        300 
TRTSRGWHTT DLKYNPSRVE AFHRYGTTVN CIVEEVDARS VYPYDEFVLA TGDFVYMSPF 

       310        320        330        340        350        360 
YGYREGSHTE HTTYAADRFK QVDGFYARDL TTKARATAPT TRNLLTTPKF TVAWDWVPKR 

       370        380        390        400        410        420 
PSVCTMTKWQ EVDEMLRSEY GGSFRFSSDA ISTTFTTNLT EYPLSRVDLG DCIGKDARDA 

       430        440        450        460        470        480 
MDRIFARRYN ATHIKVGQPQ YYQANGGFLI AYQPLLSNTL AELYVREHLR EQSRKPPNPT 

       490        500        510        520        530        540 
PPPPGASANA SVERIKTTSS IEFARLQFTY NHIQRHVNDM LGRVAIAWCE LQNHELTLWN 

       550        560        570        580        590        600 
EARKLNPNAI ASVTVGRRVS ARMLGDVMAV STCVPVAADN VIVQNSMRIS SRPGACYSRP 

       610        620        630        640        650        660 
LVSFRYEDQG PLVEGQLGEN NELRLTRDAI EPCTVGHRRY FTFGGGYVYF EEYAYSHQLS 

       670        680        690        700        710        720 
RADITTVSTF IDLNITMLED HEFVPLEVYT RHEIKDSGLL DYTEVQRRNQ LHDLRFADID 

       730        740        750        760        770        780 
TVIHADANAA MFAGLGAFFE GMGDLGRAVG KVVMGIVGGV VSAVSGVSSF MSNPFGALAV 

       790        800        810        820        830        840 
GLLVLAGLAA AFFAFRYVMR LQSNPMKALY PLTTKELKNP TNPDASGEGE EGGDFDEAKL 

       850        860        870        880        890        900 
AEAREMIRYM ALVSAMERTE HKAKKKGTSA LLSAKVTDMV MRKRRNTNYT QVPNKDGDAD 


EDDL 

« Hide

References

[1]"Nucleotide sequence specifying the glycoprotein gene, gB, of herpes simplex virus type 1."
Bzik D.J., Fox B.A., Deluca N.A., Person S.
Virology 133:301-314(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of the gB glycoprotein gene of HSV-2 and comparison with the corresponding gene of HSV-1."
Bzik D.J., Debroy C., Fox B.A., Pederson N.E., Person S.
Virology 155:322-333(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
[3]Pederson N.E.
Submitted (APR-1987) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"Glycoprotein C-independent binding of herpes simplex virus to cells requires cell surface heparan sulphate and glycoprotein B."
Herold B.C., Visalli R.J., Susmarski N., Brandt C.R., Spear P.G.
J. Gen. Virol. 75:1211-1222(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: BINDING TO HEPARAN SULFATE.
[5]"Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B."
Subramanian R.P., Geraghty R.J.
Proc. Natl. Acad. Sci. U.S.A. 104:2903-2908(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion."
Atanasiu D., Whitbeck J.C., Cairns T.M., Reilly B., Cohen G.H., Eisenberg R.J.
Proc. Natl. Acad. Sci. U.S.A. 104:18718-18723(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GH/GL HETERODIMER.
[7]"PILRalpha is a herpes simplex virus-1 entry coreceptor that associates with glycoprotein B."
Satoh T., Arii J., Suenaga T., Wang J., Kogure A., Uehori J., Arase N., Shiratori I., Tanaka S., Kawaguchi Y., Spear P.G., Lanier L.L., Arase H.
Cell 132:935-944(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THE HUMAN CORECEPTOR PILRA.
[8]"Herpes simplex virus 1 protein kinase Us3 phosphorylates viral envelope glycoprotein B and regulates its expression on the cell surface."
Kato A., Arii J., Shiratori I., Akashi H., Arase H., Kawaguchi Y.
J. Virol. 83:250-261(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-887 BY VIRAL KINASE US3, MUTAGENESIS OF THR-887.
[9]"Herpesvirus gB-induced fusion between the virion envelope and outer nuclear membrane during virus egress is regulated by the viral US3 kinase."
Wisner T.W., Wright C.C., Kato A., Kawaguchi Y., Mou F., Baines J.D., Roller R.J., Johnson D.C.
J. Virol. 83:3115-3126(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-887 BY VIRAL KINASE US3, MUTAGENESIS OF THR-887.
[10]"Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops."
Hannah B.P., Cairns T.M., Bender F.C., Whitbeck J.C., Lou H., Eisenberg R.J., Cohen G.H.
J. Virol. 83:6825-6836(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TRP-174; TYR-179; HIS-263 AND ARG-264.
[11]"Crystal structure of glycoprotein B from herpes simplex virus 1."
Heldwein E.E., Lou H., Bender F.C., Cohen G.H., Eisenberg R.J., Harrison S.C.
Science 313:217-220(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 103-730.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K01760 Genomic DNA. Translation: AAA45774.1.
PIRVGBEK1. A03751.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GUMX-ray2.10A/B/C103-730[»]
3NW8X-ray2.76A/B/C/D30-730[»]
3NWAX-ray2.26A/B/C/D30-730[»]
3NWDX-ray2.88A/B/C/D30-730[»]
3NWFX-ray3.00A/B/C/D30-730[»]
4BOMelectron microscopy27.00A/B/C103-724[»]
4HSIX-ray3.10A/B/C/D61-730[»]
4L1RX-ray3.03A/B30-730[»]
ProteinModelPortalP06437.
SMRP06437. Positions 109-724.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60474N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000234. Herpes_Glycoprot_B.
[Graphical view]
PfamPF00606. Glycoprotein_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06437.

Entry information

Entry nameGB_HHV1K
AccessionPrimary (citable) accession number: P06437
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references