GB_TUHV2
ID GB_TUHV2 Reviewed; 944 AA.
AC Q9WRL5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 02-JUN-2021, entry version 74.
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};
OS Tupaiid herpesvirus (strain 2) (TuHV-2) (Herpesvirus tupaia (strain 2)).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae.
OX NCBI_TaxID=132678;
OH NCBI_TaxID=37347; Tupaia belangeri (Common tree shrew) (Tupaia glis belangeri).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10392721; DOI=10.1016/s0168-1702(99)00012-x;
RA Bahr U., Springfeld C., Tidona C.A., Darai G.;
RT "Structural organization of a conserved gene cluster of Tupaia herpesvirus
RT encoding the DNA polymerase, glycoprotein B, a probable processing and
RT transport protein, and the major DNA binding protein.";
RL Virus Res. 60:123-136(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:0000305}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein B family.
CC {ECO:0000255|HAMAP-Rule:MF_04032}.
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DR EMBL; AF084543; AAD42935.1; -; Genomic_DNA.
DR SMR; Q9WRL5; -.
DR PRIDE; Q9WRL5; -.
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 Signal; Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Virion; Virus entry into host cell.
FT SIGNAL 1..55
FT /evidence="ECO:0000255"
FT CHAIN 56..944
FT /note="Envelope glycoprotein B"
FT /id="PRO_0000038184"
FT TOPO_DOM 56..785
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 786..806
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 807..944
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..188
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 267..274
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 731..783
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 762..782
FT /note="Hydrophobic membrane proximal region"
FT REGION 834..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 931..934
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT COMPBIAS 13..27
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..944
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 491..492
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 369
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 414
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 125..577
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 142..533
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 215..280
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 372..420
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 608..645
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 944 AA; 106060 MW; 1B063A4CD1561EE2 CRC64;
MGPPPPLRRQ RLLLPRPSRR RPPARLASGR RSSRPGSSWT WYATLIASLV WYPTVSSTTL
EATVVSSTDG GATGQASGGG GGGAGDSTPS ESPETSADTT VPRERVTGTE WVSNLTSERY
PYRICSMSQG TDIVRFARTI TCAPYDAKSV STEGIMLIYK ANIVPYTFDV FTYQKELFFQ
RSYAYIYTTY LLGNSREHVA LPLWEVDAAN IWNYCYSSYV RTIGTEQYVS YHQDSYRNET
MWLIPEEYQS GNTRRYVTVK DQYHVYGSTW LYKETCSMNC IVTQTKAKSK YPYDYFALSS
GLVVEASPFY DTVNGHTFHE NRRKFHVREQ YRMLERFGAV NAPVRVVPKM AFLERPDIVL
AWEIKEPKNV TCHLALWETV NRAIRTEHAT SFHFVSRGLT ATFVTAKANE TLYNNSRYDC
IRDSANRTID RVFREEYDGK YELDGDPVIF TTNGGLTVVW QGLRQKALAA LSALAGIPGA
NGTTNHSRHR RDTAAIAARE HASDLTYAQL QFAYDTIRDY VNQAIGHIAE AWCLEQRRTG
EMLHELSKIN PSSMLTAIYD RPIAARLAGD VIALAKCVEV DQDTVQVQRD MRKFETSVDG
TEEQGQFCYS RPVVLFRFVN SSETQYGQLG EDNEILLGTF RTEACQLPSL KIFVAGKVAY
EYRDYLYKRQ IDLDSIDVVN TMISLKVEPL ENTDFQVLEL YSRGELKSAN VFDLEDIMRE
YNAHKLRLRY ITSKIVNPIP PFMRGLDDFM SGLGAAGKGL GLVLGAVGGA VASVVGGFVS
FFTNPFGSLT LIILVVAVVV IVFLLYQRQR SAVRQPLDFF FPYLAQQTQR HQQTVTTTEY
LDSPPPYAER DSYKSGPPDP AAEGLGGSGA LPGSSATAAT KYTTEDAWQM LLAIRRLDEE
KREVPTMVAP SARPPSQQGP GLLDRIRRRG YRRLRDTGSD SELA
