GB_HHV11
ID GB_HHV11 Reviewed; 904 AA.
AC P10211; B9VQF5; Q09IA6;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 02-JUN-2021, entry version 112.
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 17) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10299;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA Perry L.J., Scott J.E., Taylor P.;
RT "The complete DNA sequence of the long unique region in the genome of
RT herpes simplex virus type 1.";
RL J. Gen. Virol. 69:1531-1574(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nonneuroinvasive mutant HF10;
RX PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
RA Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
RT "Determination and analysis of the DNA sequence of highly attenuated herpes
RT simplex virus type 1 mutant HF10, a potential oncolytic virus.";
RL Microbes Infect. 9:142-149(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17 syn+;
RA Cunningham C., Davison A.J.;
RT "Herpes simplex virus type 1 bacterial artificial chromosome.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=15596825; DOI=10.1128/jvi.79.1.299-313.2005;
RA Melancon J.M., Luna R.E., Foster T.P., Kousoulas K.G.;
RT "Herpes simplex virus type 1 gK is required for gB-mediated virus-induced
RT cell fusion, while neither gB and gK nor gB and UL20p function redundantly
RT in virion de-envelopment.";
RL J. Virol. 79:299-313(2005).
RN [5]
RP SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=17686835; DOI=10.1128/jvi.01364-07;
RA Calistri A., Sette P., Salata C., Cancellotti E., Forghieri C., Comin A.,
RA Goettlinger H., Campadelli-Fiume G., Palu G., Parolin C.;
RT "Intracellular trafficking and maturation of herpes simplex virus type 1 gB
RT and virus egress require functional biogenesis of multivesicular bodies.";
RL J. Virol. 81:11468-11478(2007).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH GH AND GD.
RX PubMed=17670828; DOI=10.1128/jvi.01343-07;
RA Avitabile E., Forghieri C., Campadelli-Fiume G.;
RT "Complexes between herpes simplex virus glycoproteins gD, gB, and gH
RT detected in cells by complementation of split enhanced green fluorescent
RT protein.";
RL J. Virol. 81:11532-11537(2007).
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 (By
CC similarity). Also plays a role, together with gK, in virus-induced
CC cell-to-cell fusion (syncytia formation). {ECO:0000255|HAMAP-
CC Rule:MF_04032, ECO:0000269|PubMed:15596825}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Binds to heparan sulfate
CC proteoglycans. Interacts with gH/gL heterodimer. {ECO:0000255|HAMAP-
CC Rule:MF_04032}.
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 ECO:0000269|PubMed:17686835}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04032}. Host endosome membrane
CC {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04032}. Host Golgi apparatus membrane
CC {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04032}. Note=During virion morphogenesis,
CC this protein probably accumulates in the endosomes and trans-Golgi
CC where secondary envelopment occurs. It is probably transported to the
CC cell surface from where it is endocytosed and directed to the trans-
CC Golgi network (TGN). {ECO:0000255|HAMAP-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 (By similarity). {ECO:0000250}.
CC -!- PTM: ubiquitinated. {ECO:0000269|PubMed:17686835}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein B family.
CC {ECO:0000255|HAMAP-Rule:MF_04032}.
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DR EMBL; X14112; CAA32320.1; -; Genomic_DNA.
DR EMBL; DQ889502; ABI63489.1; -; Genomic_DNA.
DR EMBL; FJ593289; ACM62250.1; -; Genomic_DNA.
DR PIR; I30084; VGBEW7.
DR RefSeq; YP_009137102.1; NC_001806.2.
DR PDB; 5V2S; X-ray; 3.60 A; A=72-904.
DR PDB; 6BM8; X-ray; 4.10 A; A=72-904.
DR PDBsum; 5V2S; -.
DR PDBsum; 6BM8; -.
DR SMR; P10211; -.
DR BioGRID; 971469; 1.
DR ChEMBL; CHEMBL2364696; -.
DR DrugCentral; P10211; -.
DR TCDB; 1.G.10.1.1; the herpes simplex virus membrane fusion complex (hsv-mfc) family.
DR PRIDE; P10211; -.
DR GeneID; 24271469; -.
DR KEGG; vg:24271469; -.
DR PRO; PR:P10211; -.
DR Proteomes; UP000009294; Genome.
DR Proteomes; UP000180652; Genome.
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: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; Reference proteome; 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_0000038160"
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 31..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 COMPBIAS 52..66
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 DISULFID 133..529
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 207..271
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 364..412
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 596..633
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT VARIANT 73
FT /note="R -> K"
FT VARIANT 80
FT /note="P -> L (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 555
FT /note="V -> M (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 572
FT /note="T -> M (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 668
FT /note="S -> N (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 817
FT /note="L -> P (in strain: Nonneuroinvasive mutant HF10)"
SQ SEQUENCE 904 AA; 100292 MW; 2C14E8B1284C1F3A CRC64;
MRQGAPARGR RWFVVWALLG LTLGVLVASA APSSPGTPGV AAATQAANGG PATPAPPAPG
APPTGDPKPK KNRKPKPPKP PRPAGDNATV AAGHATLREH LRDIKAENTD ANFYVCPPPT
GATVVQFEQP RRCPTRPEGQ NYTEGIAVVF KENIAPYKFK ATMYYKDVTV SQVWFGHRYS
QFMGIFEDRA PVPFEEVIDK INAKGVCRST AKYVRNNLET TAFHRDDHET DMELKPANAA
TRTSRGWHTT DLKYNPSRVE AFHRYGTTVN CIVEEVDARS VYPYDEFVLA TGDFVYMSPF
YGYREGSHTE HTSYAADRFK QVDGFYARDL TTKARATAPT TRNLLTTPKF TVAWDWVPKR
PSVCTMTKWQ EVDEMLRSEY GGSFRFSSDA ISTTFTTNLT EYPLSRVDLG DCIGKDARDA
MDRIFARRYN ATHIKVGQPQ YYLANGGFLI AYQPLLSNTL AELYVREHLR EQSRKPPNPT
PPPPGASANA SVERIKTTSS IEFARLQFTY NHIQRHVNDM LGRVAIAWCE LQNHELTLWN
EARKLNPNAI ASATVGRRVS 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
