GB_HCMVA
ID GB_HCMVA Reviewed; 906 AA.
AC P06473; Q7M6M8;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=UL55;
OS Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3024973; DOI=10.1002/j.1460-2075.1986.tb04606.x;
RA Cranage M.P., Kouzarides T., Bankier A.T., Satchwell S., Weston K.,
RA Tomlinson P., Barrell B.G., Hart H., Bell S.E., Minson A.C., Smith G.L.;
RT "Identification of the human cytomegalovirus glycoprotein B gene and
RT induction of neutralizing antibodies via its expression in recombinant
RT vaccinia virus.";
RL EMBO J. 5:3057-3063(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3029980; DOI=10.1016/0042-6822(87)90282-0;
RA Kouzarides T., Bankier A.T., Satchwell S.C., Weston K.M., Tomlinson P.,
RA Barrell B.G.;
RT "Large-scale rearrangement of homologous regions in the genomes of HCMV and
RT EBV.";
RL Virology 157:397-413(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 735-906.
RX PubMed=3023690; DOI=10.1128/jvi.61.1.125-133.1987;
RA Kouzarides T., Bankier A.T., Satchwell S.C., Weston K.M., Tomlinson P.,
RA Barrell B.G.;
RT "Sequence and transcription analysis of the human cytomegalovirus DNA
RT polymerase gene.";
RL J. Virol. 61:125-133(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [5]
RP DISULFIDE BONDS.
RX PubMed=12021340; DOI=10.1128/jvi.76.12.6073-6082.2002;
RA Lopper M., Compton T.;
RT "Disulfide bond configuration of human cytomegalovirus glycoprotein B.";
RL J. Virol. 76:6073-6082(2002).
RN [6]
RP FUNCTION, AND INTERACTION WITH HUMAN CD209/DC-SIGN.
RX PubMed=12433371; DOI=10.1016/s1074-7613(02)00447-8;
RA Halary F., Amara A., Lortat-Jacob H., Messerle M., Delaunay T., Houles C.,
RA Fieschi F., Arenzana-Seisdedos F., Moreau J.-F., Dechanet-Merville J.;
RT "Human cytomegalovirus binding to DC-SIGN is required for dendritic cell
RT infection and target cell trans-infection.";
RL Immunity 17:653-664(2002).
RN [7]
RP GENOME REANNOTATION.
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [8]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
RN [9]
RP IDENTIFICATION.
RX PubMed=15452216; DOI=10.1128/jvi.78.20.10960-10966.2004;
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RT "Identification of proteins in human cytomegalovirus (HCMV) particles: the
RT HCMV proteome.";
RL J. Virol. 78:10960-10966(2004).
RN [10]
RP ERRATUM OF PUBMED:15452216.
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RL J. Virol. 78:13395-13395(2004).
RN [11]
RP INTERACTION WITH HOST TLR1 AND TLR2.
RX PubMed=17082626; DOI=10.4049/jimmunol.177.10.7094;
RA Boehme K.W., Guerrero M., Compton T.;
RT "Human cytomegalovirus envelope glycoproteins B and H are necessary for
RT TLR2 activation in permissive cells.";
RL J. Immunol. 177:7094-7102(2006).
RN [12]
RP FUNCTION.
RX PubMed=19193805; DOI=10.1128/jvi.01251-08;
RA Isaacson M.K., Compton T.;
RT "Human cytomegalovirus glycoprotein B is required for virus entry and cell-
RT to-cell spread but not for virion attachment, assembly, or egress.";
RL J. Virol. 83:3891-3903(2009).
RN [13]
RP INTERACTION WITH HOST ITGB1.
RX PubMed=20660204; DOI=10.1128/jvi.00710-10;
RA Feire A.L., Roy R.M., Manley K., Compton T.;
RT "The glycoprotein B disintegrin-like domain binds beta 1 integrin to
RT mediate cytomegalovirus entry.";
RL J. Virol. 84:10026-10037(2010).
CC -!- FUNCTION: Envelope glycoprotein that plays a role in host cell entry,
CC cell to-cell virus transmission, and fusion of infected cells. May be
CC involved in the initial attachment via binding to heparan sulfate
CC together with the gM/gN complex that binds heparin with higher
CC affinity. Interacts with host integrin ITGB1, PDGFRA and EGFR that
CC likely serve as postattachment entry receptors. Participates also in
CC the fusion of viral and cellular membranes leading to virus entry into
CC the host cell. Membrane fusion is mediated by the fusion machinery
CC composed at least of gB and the heterodimer gH/gL.
CC {ECO:0000269|PubMed:12433371, ECO:0000269|PubMed:19193805}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Binds to heparan sulfate
CC proteoglycans. Interacts with gH/gL heterodimer (By similarity).
CC Interacts with host TLR1 and TLR2. Interacts with host C-type lectin
CC CD209/DC-SIGN. Interacts with host ITGB1, EGFR, and PDGFRA.
CC {ECO:0000255|HAMAP-Rule:MF_04032, ECO:0000269|PubMed:12433371,
CC ECO:0000269|PubMed:17082626, ECO:0000269|PubMed:20660204}.
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: A proteolytic cleavage by host furin generates two subunits that
CC remain linked by disulfide bonds. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein B family.
CC {ECO:0000255|HAMAP-Rule:MF_04032}.
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DR EMBL; X17403; CAA35414.1; -; Genomic_DNA.
DR EMBL; X04606; CAA28274.1; -; Genomic_DNA.
DR EMBL; M17209; AAA46009.1; -; Genomic_DNA.
DR EMBL; M14709; AAA45987.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00160.1; -; Genomic_DNA.
DR PIR; A25365; VGBEC1.
DR PDB; 5CXF; X-ray; 3.60 A; A/B/C=78-706.
DR PDB; 6UOE; X-ray; 1.80 A; P=65-79.
DR PDBsum; 5CXF; -.
DR PDBsum; 6UOE; -.
DR SMR; P06473; -.
DR ChEMBL; CHEMBL3988503; -.
DR PRIDE; P06473; -.
DR ABCD; P06473; 55 sequenced antibodies.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; 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; -; 2.
DR HAMAP; MF_04032; HSV_GB; 1.
DR InterPro; IPR021044; Glycoprot_B_antigenic_N.
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.
DR Pfam; PF12154; HCMVantigenic_N; 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 Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..31
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 32..906
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000038192"
FT TOPO_DOM 32..750
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 751..771
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 772..906
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 29..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..158
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 237..244
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 696..748
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 727..747
FT /note="Hydrophobic membrane proximal region"
FT REGION 797..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 894..897
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT COMPBIAS 797..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 459..460
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 94..550
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:12021340"
FT DISULFID 111..506
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:12021340"
FT DISULFID 185..250
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 246..250
FT /evidence="ECO:0000269|PubMed:12021340"
FT DISULFID 344..391
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:12021340"
FT DISULFID 573..610
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:12021340"
SQ SEQUENCE 906 AA; 102004 MW; D4C7A6A3C7083FEE CRC64;
MESRIWCLVV CVNLCIVCLG AAVSSSSTSH ATSSTHNGSH TSRTTSAQTR SVYSQHVTSS
EAVSHRANET IYNTTLKYGD VVGVNTTKYP YRVCSMAQGT DLIRFERNII CTSMKPINED
LDEGIMVVYK RNIVAHTFKV RVYQKVLTFR RSYAYIYTTY LLGSNTEYVA PPMWEIHHIN
KFAQCYSSYS RVIGGTVFVA YHRDSYENKT MQLIPDDYSN THSTRYVTVK DQWHSRGSTW
LYRETCNLNC MLTITTARSK YPYHFFATST GDVVYISPFY NGTNRNASYF GENADKFFIF
PNYTIVSDFG RPNAAPETHR LVAFLERADS VISWDIQDEK NVTCQLTFWE ASERTIRSEA
EDSYHFSSAK MTATFLSKKQ EVNMSDSALD CVRDEAINKL QQIFNTSYNQ TYEKYGNVSV
FETSGGLVVF WQGIKQKSLV ELERLANRSS LNITHRTRRS TSDNNTTHLS SMESVHNLVY
AQLQFTYDTL RGYINRALAQ IAEAWCVDQR RTLEVFKELS KINPSAILSA IYNKPIAARF
MGDVLGLASC VTINQTSVKV LRDMNVKESP GRCYSRPVVI FNFANSSYVQ YGQLGEDNEI
LLGNHRTEEC QLPSLKIFIA GNSAYEYVDY LFKRMIDLSS ISTVDSMIAL DIDPLENTDF
RVLELYSQKE LRSSNVFDLE EIMREFNSYK QRVKYVEDKV VDPLPPYLKG LDDLMSGLGA
AGKAVGVAIG AVGGAVASVV EGVATFLKNP FGAFTIILVA IAVVIITYLI YTRQRRLCTQ
PLQNLFPYLV SADGTTVTSG STKDTSLQAP PSYEESVYNS GRKGPGPPSS DASTAAPPYT
NEQAYQMLLA LARLDAEQRA QQNGTDSLDG QTGTQDKGQK PNLLDRLRHR KNGYRHLKDS
DEEENV
