GB_HHV1F
ID GB_HHV1F Reviewed; 903 AA.
AC P06436;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 02-JUN-2021, entry version 102.
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 F) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10304;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2981343; DOI=10.1128/jvi.53.1.243-253.1985;
RA Pellett P.E., Kousoulas K.G., Pereira L., Roizman B.;
RT "Anatomy of the herpes simplex virus 1 strain F glycoprotein B gene:
RT primary sequence and predicted protein structure of the wild type and of
RT monoclonal antibody-resistant mutants.";
RL J. Virol. 53:243-253(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176.
RX PubMed=2457278; DOI=10.1016/0042-6822(88)90584-3;
RA Hammerschmidt W., Conraths F., Mankertz J., Buhk H.-J., Pauli G.,
RA Ludwig H.;
RT "Common epitopes of glycoprotein B map within the major DNA-binding
RT proteins of bovine herpesvirus type 2 (BHV-2) and herpes simplex virus type
RT 1 (HSV-1).";
RL Virology 165:406-418(1988).
RN [3]
RP FUNCTION.
RX PubMed=17548810; DOI=10.1073/pnas.0703790104;
RA Farnsworth A., Wisner T.W., Webb M., Roller R.J., Cohen G.H.,
RA Eisenberg R.J., Johnson D.C.;
RT "Herpes simplex virus glycoproteins gB and gH function in fusion between
RT the virion envelope and the outer nuclear membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10187-10192(2007).
RN [4]
RP INTERACTION WITH GD.
RX PubMed=19386594; DOI=10.1074/jbc.m109.005728;
RA Gianni T., Amasio M., Campadelli-Fiume G.;
RT "Herpes simplex virus gD forms distinct complexes with fusion executors gB
RT and gH/gL in part through the C-terminal profusion domain.";
RL J. Biol. Chem. 284:17370-17382(2009).
RN [5]
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 [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 498-505 IN COMPLEX WITH H-2K(B)
RP AND K(BM8).
RX PubMed=15210799; DOI=10.4049/jimmunol.173.1.402;
RA Webb A.I., Borg N.A., Dunstone M.A., Kjer-Nielsen L., Beddoe T.,
RA McCluskey J., Carbone F.R., Bottomley S.P., Aguilar M.I., Purcell A.W.,
RA Rossjohn J.;
RT "The structure of H-2K(b) and K(bm8) complexed to a herpes simplex virus
RT determinant: evidence for a conformational switch that governs T cell
RT repertoire selection and viral resistance.";
RL J. Immunol. 173:402-409(2004).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=18596102; DOI=10.1128/jvi.00904-08;
RA Loret S., Guay G., Lippe R.;
RT "Comprehensive characterization of extracellular herpes simplex virus type
RT 1 virions.";
RL J. Virol. 82:8605-8618(2008).
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:17548810}.
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. Interacts with gD.
CC {ECO:0000255|HAMAP-Rule:MF_04032, ECO:0000269|PubMed:18358807,
CC ECO:0000269|PubMed:19386594}.
CC -!- INTERACTION:
CC P06436; Q9UKJ1: PILRA; Xeno; NbExp=3; IntAct=EBI-1771271, EBI-965833;
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 (By similarity). {ECO:0000250}.
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; M14164; AAA45776.1; -; Genomic_DNA.
DR EMBL; M21633; AAA45788.1; -; Genomic_DNA.
DR PIR; A03750; VGBEB1.
DR PDB; 1RJY; X-ray; 1.90 A; P/Q=498-505.
DR PDB; 1RJZ; X-ray; 2.60 A; P/Q=498-505.
DR PDB; 1RK0; X-ray; 2.61 A; P=498-505.
DR PDB; 1RK1; X-ray; 2.10 A; P=498-505.
DR PDB; 1T0M; X-ray; 2.00 A; P/Q=498-505.
DR PDB; 1T0N; X-ray; 1.80 A; P/Q=498-505.
DR PDBsum; 1RJY; -.
DR PDBsum; 1RJZ; -.
DR PDBsum; 1RK0; -.
DR PDBsum; 1RK1; -.
DR PDBsum; 1T0M; -.
DR PDBsum; 1T0N; -.
DR SMR; P06436; -.
DR IntAct; P06436; 1.
DR PRIDE; P06436; -.
DR ABCD; P06436; 2 sequenced antibodies.
DR EvolutionaryTrace; P06436; -.
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; IDA:CACAO.
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; Signal; Transmembrane; Transmembrane helix; Ubl conjugation;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..29
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 30..903
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000038161"
FT TOPO_DOM 30..773
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 795..903
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 30..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..178
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 257..264
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 469..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..771
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 882..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 848..851
FT /note="Golgi targeting"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT MOTIF 888..891
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 673
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 115..572
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 132..528
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 206..270
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 363..411
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 595..632
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 903 AA; 100104 MW; 73BDCA7813DB35E8 CRC64;
MRQGAARGCR WFVVWALLGL TLGVLVASAA PSSPGTPGVA AATQAANGGP ATPAPPAPGP
APTGDTKPKK NKKPKNPPPP RPAGDNATVA AGHATLREHL RDIKAENTDA NFYVCPPPTG
ATVVQFEQPR RCPTRPEGQN YTEGIAVVFK ENIAPYKFKA TMYYKDVTVS QVWFGHRYSQ
FMGIFEDRAP VPFEEVIDKI NAKGVCRSTA KYVRNNLETT AFHRDDHETD MELKPANAAT
RTSRGWHTTD LKYNPSRVEA FHRYGTTVNC IVEEVDARSV YPYDEFVLAT GDFVYMSPFY
GYREGSHTEH TSYAADRFKQ VDGFYARDLT TKARATAPTT RNLLTTPKFT VAWDWVPKRP
SVCTMTKWQE VDEMLRSEYG GSFRFSSDAI STTFTTNLTE YPLSRVDLGD CIGKDARDAM
DRIFARRYNA THIKVGQPQY YLANGGFLIA YQPLLSNTLA ELYVREHLRE QSRKPPNPTP
PPPGASANAS VERIKTTSSI EFARLQFTYN HIQRHVNDML GRVAIAWCEL QNHELTLWNE
ARKLNPNAIA SATVGRRVSA RMLGDVMAVS TCVPVAADNV IVQNSMRISS RPGACYSRPL
VSFRYEDQGP LVEGQLGENN ELRLTRDAIE PCTVGHRRYF TFGGGYVYFE EYAYSHQLSR
ADITTVSTFI DLNITMLEDH EFVPLEVYTR HEIKDSGLLD YTEVQRRNQL HDLRFADIDT
VIHADANAAM FAGLGAFFEG MGDLGRAVGK VVMGIVGGVV SAVSGVSSFM SNPFGALAVG
LLVLAGLAAA FFAFRYVMRL QSNPMKALYP LTTKELKNPT NPDASGEGEE GGDFDEAKLA
EAREMIRYMA LVSAMERTEH KAKKKGTSAL LSAKVTDMVM RKRRNTNYTQ VPNKDGDADE
DDL
