GB_HCMVT
ID GB_HCMVT Reviewed; 907 AA.
AC P13201;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, 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=UL55;
OS Human cytomegalovirus (strain Towne) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10363;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2460994; DOI=10.1016/0042-6822(88)90071-2;
RA Spaete R.R., Thayer R.M., Probert W.S., Masiarz F.R., Chamberlain S.H.,
RA Rasmussen L., Merigan T.C., Pachl C.;
RT "Human cytomegalovirus strain Towne glycoprotein B is processed by
RT proteolytic cleavage.";
RL Virology 167:207-225(1988).
RN [2]
RP INTERACTION WITH HEPARAN SULFATE.
RX PubMed=8384757; DOI=10.1006/viro.1993.1192;
RA Compton T., Nowlin D.M., Cooper N.R.;
RT "Initiation of human cytomegalovirus infection requires initial interaction
RT with cell surface heparan sulfate.";
RL Virology 193:834-841(1993).
RN [3]
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 [4]
RP FUNCTION, AND INTERACTION WITH HUMAN EGFR.
RX PubMed=12879076; DOI=10.1038/nature01818;
RA Wang X., Huong S.M., Chiu M.L., Raab-Traub N., Huang E.S.;
RT "Epidermal growth factor receptor is a cellular receptor for human
RT cytomegalovirus.";
RL Nature 424:456-461(2003).
RN [5]
RP FUNCTION, AND INTERACTION WITH HUMAN PDGFRA.
RX PubMed=18701889; DOI=10.1038/nature07209;
RA Soroceanu L., Akhavan A., Cobbs C.S.;
RT "Platelet-derived growth factor-alpha receptor activation is required for
RT human cytomegalovirus infection.";
RL Nature 455:391-395(2008).
RN [6]
RP FUNCTION, AND INTERACTION WITH HUMAN INTEGRIN 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).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 69-78.
RX PubMed=18772881; DOI=10.1038/emboj.2008.179;
RA Thomson C.A., Bryson S., McLean G.R., Creagh A.L., Pai E.F., Schrader J.W.;
RT "Germline V-genes sculpt the binding site of a family of antibodies
RT neutralizing human cytomegalovirus.";
RL EMBO J. 27:2592-2602(2008).
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:12879076,
CC ECO:0000269|PubMed:18701889, ECO:0000269|PubMed:20660204}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Binds to heparan sulfate
CC proteoglycans. Interacts with gH/gL heterodimer (By similarity).
CC Interacts with host C-type lectin CD209/DC-SIGN. Interacts with host
CC ITGB1, EGFR, and PDGFRA. {ECO:0000255|HAMAP-Rule:MF_04032,
CC ECO:0000269|PubMed:12433371, ECO:0000269|PubMed:12879076,
CC ECO:0000269|PubMed:18701889, ECO:0000269|PubMed:20660204,
CC ECO:0000269|PubMed:8384757}.
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; M22343; AAA45920.1; -; mRNA.
DR PIR; A31288; VGBETE.
DR PDB; 3EYF; X-ray; 2.30 A; E/F=69-78.
DR PDB; 4OSN; X-ray; 1.76 A; A=114-133, A=344-438.
DR PDB; 4OT1; X-ray; 2.11 A; A=114-133, A=344-438.
DR PDB; 5C6T; X-ray; 3.60 A; A=87-698.
DR PDB; 7KDD; EM; 3.50 A; A/B/C=1-907.
DR PDB; 7KDP; EM; 3.60 A; A/B/C=1-907.
DR PDBsum; 3EYF; -.
DR PDBsum; 4OSN; -.
DR PDBsum; 4OT1; -.
DR PDBsum; 5C6T; -.
DR PDBsum; 7KDD; -.
DR PDBsum; 7KDP; -.
DR SMR; P13201; -.
DR ABCD; P13201; 17 sequenced antibodies.
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; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 23..907
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000436645"
FT TOPO_DOM 23..751
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 752..772
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 773..907
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 29..62
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 697..749
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 708..748
FT /note="Hydrophobic membrane proximal region"
FT REGION 798..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 895..898
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT COMPBIAS 798..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 460..461
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255"
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 456
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 94..551
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 111..507
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 185..250
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 344..391
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 574..611
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 138..154
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 159..169
FT /evidence="ECO:0007829|PDB:7KDD"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:7KDD"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 248..258
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 294..308
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 316..326
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:7KDD"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 346..359
FT /evidence="ECO:0007829|PDB:4OSN"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:4OSN"
FT TURN 369..372
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:4OSN"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:4OSN"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:4OSN"
FT HELIX 393..407
FT /evidence="ECO:0007829|PDB:4OSN"
FT STRAND 413..422
FT /evidence="ECO:0007829|PDB:4OSN"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 428..435
FT /evidence="ECO:0007829|PDB:4OSN"
FT HELIX 481..520
FT /evidence="ECO:0007829|PDB:7KDD"
FT TURN 521..523
FT /evidence="ECO:0007829|PDB:7KDD"
FT HELIX 525..533
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 547..553
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 573..577
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 579..583
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 590..596
FT /evidence="ECO:0007829|PDB:7KDD"
FT TURN 597..599
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 608..610
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 617..620
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 622..629
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 632..637
FT /evidence="ECO:0007829|PDB:7KDD"
FT HELIX 639..641
FT /evidence="ECO:0007829|PDB:7KDD"
FT STRAND 642..644
FT /evidence="ECO:0007829|PDB:7KDD"
FT HELIX 669..673
FT /evidence="ECO:0007829|PDB:7KDD"
FT HELIX 680..691
FT /evidence="ECO:0007829|PDB:7KDD"
SQ SEQUENCE 907 AA; 101954 MW; E6F07B7742D359A2 CRC64;
MESRIWCLVV CVNLCIVCLG AAVSSSSTRG TSATHSHHSS HTTSAAHSRS GSVSQRVTSS
QTVSHGVNET IYNTTLKYGD VVGVNTTKYP YRVCSMAQGT DLIRFERNIV CTSMKPINED
LDEGIMVVYK RNIVAHTFKV RVYQKVLTFR RSYAYIHTTY LLGSNTEYVA PPMWEIHHIN
SHSQCYSSYS RVIAGTVFVA YHRDSYENKT MQLMPDDYSN THSTRYVTVK DQWHSRGSTW
LYRETCNLNC MVTITTARSK YPYHFFATST GDVVDISPFY NGTNRNASYF GENADKFFIF
PNYTIVSDFG RPNSALETHR LVAFLERADS VISWDIQDEK NVTCQLTFWE ASERTIRSEA
EDSYHFSSAK MTATFLSKKQ EVNMSDSALD CVRDEAINKL QQIFNTSYNQ TYEKYGNVSV
FETTGGLVVF WQGIKQKSLV ELERLANRSS LNLTHNRTKR STDGNNATHL SNMESVHNLV
YAQLQFTYDT LRGYINRALA QIAEAWCVDQ RRTLEVFKEL SKINPSAILS AIYNKPIAAR
FMGDVLGLAS CVTINQTSVK VLRDMNVKES PGRCYSRPVV IFNFANSSYV QYGQLGEDNE
ILLGNHRTEE CQLPSLKIFI AGNSAYEYVD YLFKRMIDLS SISTVDSMIA LDIDPLENTD
FRVLELYSQK ELRSSNVFDL EEIMREFNSY KQRVKYVEDK VVDPLPPYLK GLDDLMSGLG
AAGKAVGVAI GAVGGAVASV VEGVATFLKN PFGAFTIILV AIAVVIIIYL IYTRQRRLCM
QPLQNLFPYL VSADGTTVTS GNTKDTSLQA PPSYEESVYN SGRKGPGPPS SDASTAAPPY
TNEQAYQMLL ALVRLDAEQR AQQNGTDSLD GQTGTQDKGQ KPNLLDRLRH RKNGYRHLKD
SDEEENV
