GB_HHV23
ID GB_HHV23 Reviewed; 904 AA.
AC P06763; Q69095;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 02-JUN-2021, entry version 97.
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 2 (strain 333) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10313;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3027364; DOI=10.1128/jvi.61.2.326-335.1987;
RA Stuve L.L., Brown-Shimer S., Pachl C., Najarian R., Dina D., Burke R.L.;
RT "Structure and expression of the herpes simplex virus type 2 glycoprotein
RT gB gene.";
RL J. Virol. 61:326-335(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2446730; DOI=10.1139/m87-154;
RA Zwaagstra J.C., Leung W.C.;
RT "The nucleotide sequence of herpes simplex virus type 2 (333) glycoprotein
RT gB2 and analysis of predicted antigenic sites.";
RL Can. J. Microbiol. 33:879-887(1987).
RN [3]
RP DISULFIDE BONDS.
RX PubMed=8892856; DOI=10.1128/jvi.70.11.7379-7387.1996;
RA Norais N., Tang D., Kaur S., Chamberlain S.H., Masiarz F.R., Burke R.L.,
RA Marcus F.;
RT "Disulfide bonds of herpes simplex virus type 2 glycoprotein gB.";
RL J. Virol. 70:7379-7387(1996).
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.
CC {ECO:0000255|HAMAP-Rule:MF_04032}.
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 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 -!- SIMILARITY: Belongs to the herpesviridae glycoprotein B family.
CC {ECO:0000255|HAMAP-Rule:MF_04032}.
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DR EMBL; M15118; AAA45837.1; -; Genomic_DNA.
DR EMBL; M24771; AAA60540.1; -; Genomic_DNA.
DR PIR; A26790; VGBEB2.
DR SMR; P06763; -.
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 Disulfide bond; Glycoprotein; Host cell membrane; Host endosome;
KW Host Golgi apparatus; Host membrane; Host-virus interaction; Membrane;
KW Signal; Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Virion; Virus entry into host cell.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 23..904
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000038165"
FT TOPO_DOM 23..771
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 772..792
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 793..904
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 40..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..174
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 253..260
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 467..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..769
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 728..768
FT /note="Hydrophobic membrane proximal region"
FT REGION 816..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 671
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 111..570
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:8892856"
FT DISULFID 128..526
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:8892856"
FT DISULFID 202..266
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:8892856"
FT DISULFID 359..407
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:8892856"
FT DISULFID 593..630
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:8892856"
FT CONFLICT 35..41
FT /note="GVAATVA -> AWPTV (in Ref. 2; AAA60540)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="S -> T (in Ref. 2; AAA60540)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="A -> R (in Ref. 2; AAA60540)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="I -> M (in Ref. 2; AAA60540)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="S -> R (in Ref. 2; AAA60540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 904 AA; 100187 MW; A8B36F74FDBCB539 CRC64;
MRGGGLICAL VVGALVAAVA SAAPAAPAAP RASGGVAATV AANGGPASRP PPVPSPATTK
ARKRKTKKPP KRPEATPPPD ANATVAAGHA TLRAHLREIK VENADAQFYV CPPPTGATVV
QFEQPRRCPT RPEGQNYTEG IAVVFKENIA PYKFKATMYY KDVTVSQVWF GHRYSQFMGI
FEDRAPVPFE EVIDKINAKG VCRSTAKYVR NNMETTAFHR DDHETDMELK PAKVATRTSR
GWHTTDLKYN PSRVEAFHRY GTTVNCIVEE VDARSVYPYD EFVLATGDFV YMSPFYGYRE
GSHTEHTSYA ADRFKQVDGF YARDLTTKAR ATSPTTRNLL TTPKFTVAWD WVPKRPAVCT
MTKWQEVDEM LRAEYGGSFR FSSDAISTTF TTNLTQYSLS RVDLGDCIGR DAREAIDRMF
ARKYNATHIK VGQPQYYLAT GGFLIAYQPL LSNTLAELYV REYMREQDRK PRNATPAPLR
EAPSANASVE RIKTTSSIEF ARLQFTYNHI QRHVNDMLGR IAVAWCELQN HELTLWNEAR
KLNPNAIASA TVGRRVSARM LGDVMAVSTC VPVAPDNVIV QNSMRVSSRP GTCYSRPLVS
FRYEDQGPLI EGQLGENNEL RLTRDALEPC TVGHRRYFIF GGGYVYFEEY AYSHQLSRAD
VTTVSTFIDL NITMLEDHEF VPLEVYTRHE IKDSGLLDYT EVQRRNQLHD LRFADIDTVI
RADANAAMFA GLCAFFEGMG DLGRAVGKVV MGVVGGVVSA VSGVSSFMSN PFGALAVGLL
VLAGLVAAFF AFRYVLQLQR NPMKALYPLT TKELKTSDPG GVGGEGEEGA EGGGFDEAKL
AEAREMIRYM ALVSAMERTE HKARKKGTSA LLSSKVTNMV LRKRNKARYS PLHNEDEAGD
EDEL
