GB_HHV6Z
ID GB_HHV6Z Reviewed; 830 AA.
AC P36320; Q9QJ31;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 09-SEP-2003, sequence version 2.
DT 02-JUN-2021, entry version 91.
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=U39;
OS Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=36351;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1329336; DOI=10.1016/0042-6822(92)90224-d;
RA Chou S., Marousek G.I.;
RT "Homology of the envelope glycoprotein B of human herpesvirus-6 and
RT cytomegalovirus.";
RL Virology 191:523-528(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10482553; DOI=10.1128/jvi.73.10.8040-8052.1999;
RA Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA Pellett P.E.;
RT "Human herpesvirus 6B genome sequence: coding content and comparison with
RT human herpesvirus 6A.";
RL J. Virol. 73:8040-8052(1999).
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 -!- 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; M97927; AAA43846.1; -; Genomic_DNA.
DR EMBL; AF157706; AAD49653.1; -; Genomic_DNA.
DR PIR; B44047; B44047.
DR RefSeq; NP_050220.1; NC_000898.1.
DR SMR; P36320; -.
DR PRIDE; P36320; -.
DR DNASU; 1497041; -.
DR GeneID; 1497041; -.
DR KEGG; vg:1497041; -.
DR Proteomes; UP000006930; 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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Host cell membrane; Host endosome;
KW Host Golgi apparatus; Host membrane; Host-virus interaction; Membrane;
KW 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..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 20..830
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000038187"
FT TOPO_DOM 20..688
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 710..830
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 98..104
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 184..191
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 634..686
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 644..685
FT /note="Hydrophobic membrane proximal region"
FT MOTIF 822..825
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT SITE 399..400
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 247
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 329
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 361
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 DISULFID 41..482
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 58..438
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 131..197
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 290..337
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 510..548
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CONFLICT 96
FT /note="P -> Q (in Ref. 1; AAA43846)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="A -> D (in Ref. 1; AAA43846)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 830 AA; 93134 MW; 630907C6024DCE9D CRC64;
MSKMRVLFLA VFLMNSVLMI YCDSDDYIRA GYNHKYPFRI CSIAKGTDLM RFDRDISCSP
YKSNAKMSEG FFIIYKTNIE TYTFPVRTYK NELTFPTSYR DVGVVYFLDR TVMGLAMPVY
EANLVNSRAQ CYSAVAIKRP DGTVFSAYHE DNNKNETLEL FPLNFKSVTN KRFITTKEPY
FARGPLWLYS TSTSLNCIVT EATAKAKYPF SYFALTTGEI VEGSPFFDGS NGKHFAEPLE
KLTILENYTM IEDLMNGMNG ATTLVRKIAF LEKGDTLFSW EIKEENESVC MLKHWTTVTH
GLRAETDETY HFISKELTAA FVASKESLNL TDPKQTCIKN EFEKIITDVY MSDYNDAYSM
NGSYQIFKTT GDLILIWQPL VQKSLMVLEQ GSVNLRRRRD LVDVKSRHDI LYVQLQYLYD
TLKDYINDAL GNLAESWCLD QKRTITMLHE LSKISPSSIV SEVYGRPISA QLHGDVLAIS
KCIEVNQSSV QLYKSMRVVD AKGVRSETMC YNRPLVTFSF VNSTPEVVLG QLGLDNEILL
GDHRTEECEI PSTKIFLSGN HAHVYTDYTH TNSTPIEDIE VLDAFIRLKI DPLENADFKL
LDLYSPDELS RANVFDLENI LREYNSYKSA LYTIEAKIAT NTPSYVNGIN SFLQGLGAIG
TGLGSVISVT AGALGDIVGG VVSFLKNPFG GGLMLILAIV VVVIIIVVFV RQKHVLSKPI
DMMFPYATNP VTTVSSVTGT TVVKTPSVKD ADGGTSVAVS EKEEGMADVS GQISGDEYSQ
EDALKMLKAI KSLDESYRRK PSSSESHASK PSLIDRIRYR GYKSVNVEEA
