GB_HHV1K
ID GB_HHV1K Reviewed; 904 AA.
AC P06437;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Envelope glycoprotein B {ECO:0000255|HAMAP-Rule:MF_04032};
DE Short=gB {ECO:0000255|HAMAP-Rule:MF_04032};
DE Flags: Precursor;
GN Name=gB {ECO:0000255|HAMAP-Rule:MF_04032}; ORFNames=UL27;
OS Human herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10306;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6324454; DOI=10.1016/0042-6822(84)90397-0;
RA Bzik D.J., Fox B.A., Deluca N.A., Person S.;
RT "Nucleotide sequence specifying the glycoprotein gene, gB, of herpes
RT simplex virus type 1.";
RL Virology 133:301-314(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RX PubMed=3024391; DOI=10.1016/0042-6822(86)90196-0;
RA Bzik D.J., Debroy C., Fox B.A., Pederson N.E., Person S.;
RT "The nucleotide sequence of the gB glycoprotein gene of HSV-2 and
RT comparison with the corresponding gene of HSV-1.";
RL Virology 155:322-333(1986).
RN [3]
RP SEQUENCE REVISION.
RA Pederson N.E.;
RL Submitted (APR-1987) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP BINDING TO HEPARAN SULFATE.
RX PubMed=8207388; DOI=10.1099/0022-1317-75-6-1211;
RA Herold B.C., Visalli R.J., Susmarski N., Brandt C.R., Spear P.G.;
RT "Glycoprotein C-independent binding of herpes simplex virus to cells
RT requires cell surface heparan sulphate and glycoprotein B.";
RL J. Gen. Virol. 75:1211-1222(1994).
RN [5]
RP FUNCTION.
RX PubMed=17299053; DOI=10.1073/pnas.0608374104;
RA Subramanian R.P., Geraghty R.J.;
RT "Herpes simplex virus type 1 mediates fusion through a hemifusion
RT intermediate by sequential activity of glycoproteins D, H, L, and B.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2903-2908(2007).
RN [6]
RP INTERACTION WITH GH/GL HETERODIMER.
RX PubMed=18003913; DOI=10.1073/pnas.0707452104;
RA Atanasiu D., Whitbeck J.C., Cairns T.M., Reilly B., Cohen G.H.,
RA Eisenberg R.J.;
RT "Bimolecular complementation reveals that glycoproteins gB and gH/gL of
RT herpes simplex virus interact with each other during cell fusion.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18718-18723(2007).
RN [7]
RP INTERACTION WITH THE HUMAN CORECEPTOR PILRA.
RX PubMed=18358807; DOI=10.1016/j.cell.2008.01.043;
RA Satoh T., Arii J., Suenaga T., Wang J., Kogure A., Uehori J., Arase N.,
RA Shiratori I., Tanaka S., Kawaguchi Y., Spear P.G., Lanier L.L., Arase H.;
RT "PILRalpha is a herpes simplex virus-1 entry coreceptor that associates
RT with glycoprotein B.";
RL Cell 132:935-944(2008).
RN [8]
RP PHOSPHORYLATION AT THR-887 BY VIRAL KINASE US3, AND MUTAGENESIS OF THR-887.
RX PubMed=18945776; DOI=10.1128/jvi.01451-08;
RA Kato A., Arii J., Shiratori I., Akashi H., Arase H., Kawaguchi Y.;
RT "Herpes simplex virus 1 protein kinase Us3 phosphorylates viral envelope
RT glycoprotein B and regulates its expression on the cell surface.";
RL J. Virol. 83:250-261(2009).
RN [9]
RP PHOSPHORYLATION AT THR-887 BY VIRAL KINASE US3, AND MUTAGENESIS OF THR-887.
RX PubMed=19158241; DOI=10.1128/jvi.01462-08;
RA Wisner T.W., Wright C.C., Kato A., Kawaguchi Y., Mou F., Baines J.D.,
RA Roller R.J., Johnson D.C.;
RT "Herpesvirus gB-induced fusion between the virion envelope and outer
RT nuclear membrane during virus egress is regulated by the viral US3
RT kinase.";
RL J. Virol. 83:3115-3126(2009).
RN [10]
RP MUTAGENESIS OF TRP-174; TYR-179; HIS-263 AND ARG-264.
RX PubMed=19369321; DOI=10.1128/jvi.00301-09;
RA Hannah B.P., Cairns T.M., Bender F.C., Whitbeck J.C., Lou H.,
RA Eisenberg R.J., Cohen G.H.;
RT "Herpes simplex virus glycoprotein B associates with target membranes via
RT its fusion loops.";
RL J. Virol. 83:6825-6836(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 103-730, AND DISULFIDE BONDS.
RX PubMed=16840698; DOI=10.1126/science.1126548;
RA Heldwein E.E., Lou H., Bender F.C., Cohen G.H., Eisenberg R.J.,
RA Harrison S.C.;
RT "Crystal structure of glycoprotein B from herpes simplex virus 1.";
RL Science 313:217-220(2006).
CC -!- FUNCTION: Envelope glycoprotein that forms spikes at the surface of
CC virion envelope. Essential for the initial attachment to heparan
CC sulfate moieties of the host cell surface proteoglycans. Involved in
CC fusion of viral and cellular membranes leading to virus entry into the
CC host cell. Following initial binding to its host receptors, membrane
CC fusion is mediated by the fusion machinery composed at least of gB and
CC the heterodimer gH/gL. May be involved in the fusion between the virion
CC envelope and the outer nuclear membrane during virion egress. Also
CC plays a role, together with gK, in virus-induced cell-to-cell fusion
CC (syncytia formation). {ECO:0000255|HAMAP-Rule:MF_04032,
CC ECO:0000269|PubMed:17299053}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Binds to heparan sulfate
CC proteoglycans. Interacts with gH/gL heterodimer (By similarity).
CC Interacts with the host coreceptor PILRA. {ECO:0000255|HAMAP-
CC Rule:MF_04032, ECO:0000269|PubMed:18358807}.
CC -!- INTERACTION:
CC P06437; P06437: gB; NbExp=3; IntAct=EBI-16064668, EBI-16064668;
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04032}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04032};
CC Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}.
CC Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass
CC type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host Golgi
CC apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type
CC I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Note=During
CC virion morphogenesis, this protein probably accumulates in the
CC endosomes and trans-Golgi where secondary envelopment occurs. It is
CC probably transported to the cell surface from where it is endocytosed
CC and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-
CC Rule:MF_04032}.
CC -!- PTM: The cytoplasmic tail is phosphorylated by the viral kinase US3.
CC Phosphorylation may be linked to a down-regulation of gB expression on
CC cell surface. {ECO:0000269|PubMed:18945776,
CC ECO:0000269|PubMed:19158241}.
CC -!- PTM: ubiquitinated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein B family.
CC {ECO:0000255|HAMAP-Rule:MF_04032}.
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DR EMBL; K01760; AAA45774.1; -; Genomic_DNA.
DR PIR; A03751; VGBEK1.
DR PDB; 2GUM; X-ray; 2.10 A; A/B/C=103-730.
DR PDB; 3NW8; X-ray; 2.76 A; A/B/C/D=30-730.
DR PDB; 3NWA; X-ray; 2.26 A; A/B/C/D=30-730.
DR PDB; 3NWD; X-ray; 2.88 A; A/B/C/D=30-730.
DR PDB; 3NWF; X-ray; 3.00 A; A/B/C/D=30-730.
DR PDB; 3WV0; X-ray; 2.30 A; X/Y=50-56.
DR PDB; 4BOM; EM; 27.00 A; A/B/C=103-724.
DR PDB; 4HSI; X-ray; 3.10 A; A/B/C/D=61-730.
DR PDB; 4L1R; X-ray; 3.03 A; A/B=30-730.
DR PDB; 5XO2; X-ray; 2.20 A; X/Y=50-56.
DR PDB; 6Z9M; EM; 9.10 A; A/B/C=1-904.
DR PDBsum; 2GUM; -.
DR PDBsum; 3NW8; -.
DR PDBsum; 3NWA; -.
DR PDBsum; 3NWD; -.
DR PDBsum; 3NWF; -.
DR PDBsum; 3WV0; -.
DR PDBsum; 4BOM; -.
DR PDBsum; 4HSI; -.
DR PDBsum; 4L1R; -.
DR PDBsum; 5XO2; -.
DR PDBsum; 6Z9M; -.
DR SMR; P06437; -.
DR DIP; DIP-60474N; -.
DR iPTMnet; P06437; -.
DR EvolutionaryTrace; P06437; -.
DR GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.29.100; -; 1.
DR HAMAP; MF_04032; HSV_GB; 1.
DR InterPro; IPR035377; Glycoprot_B_PH1.
DR InterPro; IPR035381; Glycoprot_B_PH2.
DR InterPro; IPR038631; Glycoprot_B_PH2_sf.
DR InterPro; IPR000234; Herpes_Glycoprot_B.
DR Pfam; PF17416; Glycoprot_B_PH1; 1.
DR Pfam; PF17417; Glycoprot_B_PH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Host cell membrane;
KW Host endosome; Host Golgi apparatus; Host membrane; Host-virus interaction;
KW Membrane; Phosphoprotein; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation; Viral attachment to host cell; Viral envelope protein;
KW Virion; Virus entry into host cell.
FT SIGNAL 1..30
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 31..904
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000038162"
FT TOPO_DOM 31..774
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 775..795
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 796..904
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 32..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..179
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 258..265
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 470..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..772
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 883..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 849..852
FT /note="Golgi targeting"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT MOTIF 889..892
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT MOD_RES 887
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000269|PubMed:18945776,
FT ECO:0000269|PubMed:19158241"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 116..573
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:16840698, ECO:0007744|PDB:2GUM"
FT DISULFID 133..529
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:16840698, ECO:0007744|PDB:2GUM"
FT DISULFID 207..271
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:16840698, ECO:0007744|PDB:2GUM"
FT DISULFID 364..412
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:16840698, ECO:0007744|PDB:2GUM"
FT DISULFID 596..633
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:16840698, ECO:0007744|PDB:2GUM"
FT MUTAGEN 174
FT /note="W->R: 90% loss of fusion with host cell."
FT /evidence="ECO:0000269|PubMed:19369321"
FT MUTAGEN 179
FT /note="Y->S: Complete loss of fusion with host cell."
FT /evidence="ECO:0000269|PubMed:19369321"
FT MUTAGEN 263
FT /note="H->A: 50% loss of fusion with host cell."
FT /evidence="ECO:0000269|PubMed:19369321"
FT MUTAGEN 264
FT /note="R->A: 70% loss of fusion with host cell."
FT /evidence="ECO:0000269|PubMed:19369321"
FT MUTAGEN 887
FT /note="T->A: Defects in nuclear egress."
FT /evidence="ECO:0000269|PubMed:18945776,
FT ECO:0000269|PubMed:19158241"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 157..175
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 180..191
FT /evidence="ECO:0007829|PDB:2GUM"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:2GUM"
FT TURN 199..204
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 205..223
FT /evidence="ECO:0007829|PDB:2GUM"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 262..280
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:3NWF"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:3NWA"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:3NWD"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:2GUM"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:3NWA"
FT STRAND 340..346
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:2GUM"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 365..373
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 383..388
FT /evidence="ECO:0007829|PDB:2GUM"
FT TURN 389..392
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 393..400
FT /evidence="ECO:0007829|PDB:2GUM"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:3NW8"
FT HELIX 412..428
FT /evidence="ECO:0007829|PDB:2GUM"
FT TURN 429..432
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:3NWA"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:2GUM"
FT TURN 445..447
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 448..454
FT /evidence="ECO:0007829|PDB:2GUM"
FT HELIX 458..463
FT /evidence="ECO:0007829|PDB:3NWA"
FT HELIX 464..470
FT /evidence="ECO:0007829|PDB:3NWA"
FT HELIX 502..545
FT /evidence="ECO:0007829|PDB:2GUM"
FT HELIX 547..555
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 559..563
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 565..572
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:2GUM"
FT HELIX 578..580
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:3NWA"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 601..604
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 606..610
FT /evidence="ECO:0007829|PDB:3NWA"
FT STRAND 613..617
FT /evidence="ECO:0007829|PDB:2GUM"
FT HELIX 619..621
FT /evidence="ECO:0007829|PDB:3NW8"
FT STRAND 622..625
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 638..643
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 646..651
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 654..660
FT /evidence="ECO:0007829|PDB:2GUM"
FT HELIX 661..663
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 664..667
FT /evidence="ECO:0007829|PDB:2GUM"
FT HELIX 691..697
FT /evidence="ECO:0007829|PDB:2GUM"
FT STRAND 698..700
FT /evidence="ECO:0007829|PDB:2GUM"
FT HELIX 702..709
FT /evidence="ECO:0007829|PDB:2GUM"
FT HELIX 712..716
FT /evidence="ECO:0007829|PDB:2GUM"
SQ SEQUENCE 904 AA; 100368 MW; B97B7F8DE5FBA299 CRC64;
MHQGAPSWGR RWFVVWALLG LTLGVLVASA APTSPGTPGV AAATQAANGG PATPAPPPLG
AAPTGDPKPK KNKKPKNPTP PRPAGDNATV AAGHATLREH LRDIKAENTD ANFYVCPPPT
GATVVQFEQP RRCPTRPEGQ NYTEGIAVVF KENIAPYKFK ATMYYKDVTV SQVWFGHRYS
QFMGIFEDRA PVPFEEVIDK INAKGVCRST AKYVRNNLET TAFHRDDHET DMELKPANAA
TRTSRGWHTT DLKYNPSRVE AFHRYGTTVN CIVEEVDARS VYPYDEFVLA TGDFVYMSPF
YGYREGSHTE HTTYAADRFK QVDGFYARDL TTKARATAPT TRNLLTTPKF TVAWDWVPKR
PSVCTMTKWQ EVDEMLRSEY GGSFRFSSDA ISTTFTTNLT EYPLSRVDLG DCIGKDARDA
MDRIFARRYN ATHIKVGQPQ YYQANGGFLI AYQPLLSNTL AELYVREHLR EQSRKPPNPT
PPPPGASANA SVERIKTTSS IEFARLQFTY NHIQRHVNDM LGRVAIAWCE LQNHELTLWN
EARKLNPNAI ASVTVGRRVS ARMLGDVMAV STCVPVAADN VIVQNSMRIS SRPGACYSRP
LVSFRYEDQG PLVEGQLGEN NELRLTRDAI EPCTVGHRRY FTFGGGYVYF EEYAYSHQLS
RADITTVSTF IDLNITMLED HEFVPLEVYT RHEIKDSGLL DYTEVQRRNQ LHDLRFADID
TVIHADANAA MFAGLGAFFE GMGDLGRAVG KVVMGIVGGV VSAVSGVSSF MSNPFGALAV
GLLVLAGLAA AFFAFRYVMR LQSNPMKALY PLTTKELKNP TNPDASGEGE EGGDFDEAKL
AEAREMIRYM ALVSAMERTE HKAKKKGTSA LLSAKVTDMV MRKRRNTNYT QVPNKDGDAD
EDDL
