GB_ELHVK
ID GB_ELHVK Reviewed; 845 AA.
AC Q77JN0;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 12-AUG-2020, entry version 54.
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 Elephantid herpesvirus 1 (isolate Asian elephant/Berlin/Kiba/1998) (EIHV-1)
OS (Elephant endotheliotropic herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Proboscivirus.
OX NCBI_TaxID=654902;
OH NCBI_TaxID=9783; Elephas maximus (Indian elephant).
OH NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH NCBI_TaxID=99490; Loxodonta cyclotis (African forest elephant).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17507487; DOI=10.1128/jvi.00255-07;
RA Ehlers B., Kuchler J., Yasmum N., Dural G., Voigt S., Schmidt-Chanasit J.,
RA Jakel T., Matuschka F.R., Richter D., Essbauer S., Hughes D.J., Summers C.,
RA Bennett M., Stewart J.P., Ulrich R.G.;
RT "Identification of novel rodent herpesviruses, including the first
RT gammaherpesvirus of Mus musculus.";
RL J. Virol. 81:8091-8100(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11172087; DOI=10.1099/0022-1317-82-3-475;
RA Ehlers B., Burkhardt S., Goltz M., Bergmann V., Ochs A., Weiler H.,
RA Hentschke J.;
RT "Genetic and ultrastructural characterization of a European isolate of the
RT fatal endotheliotropic elephant herpesvirus.";
RL J. Gen. Virol. 82:475-482(2001).
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; AF322977; AAG41998.1; -; Genomic_DNA.
DR SMR; Q77JN0; -.
DR PRIDE; Q77JN0; -.
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..41
FT /evidence="ECO:0000255"
FT CHAIN 42..845
FT /note="Envelope glycoprotein B"
FT /id="PRO_0000408177"
FT TOPO_DOM 42..727
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 728..748
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 749..845
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 120..126
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 204..212
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 677..725
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT MOTIF 837..840
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 388
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 420
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 564
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 632
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 62..523
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 80..479
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 153..218
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 310..358
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 552..591
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 845 AA; 96909 MW; 0E2AF1FEAF917D1F CRC64;
MSFTDQTYTR SCMHTCITRD HRLYGIVIIS LLLLLDNSVF CQNENKVIDI KKDEKIWPYR
ICSGMSQATD IVRFGRNIQC PEYSPKDEGT EGILLIYKQN IVPYIFPVRI YYKELTIRYR
YADVFSYYDM GDVTKKIPIM ETEKTLIDMD GKCYSAARYV EGGAYMDAYD GDEHNHTVPF
MLGYQNPDGG VTRYVTVDTH RPCLPGTWLR KTCTTVNCIV TDTYAKSRYP YDFFAISTGE
IVDGSPFYTG DNDKKFSETY TKFKVYNEYE RLEELTVSST KKRTFDKIAF LEKRDYSISW
EVKEEDQAPC QYVLWKASTQ ALMTKTVNNT YHFTSRELTA TFGANDKEEL KLAEKYPCVY
EDAKETFEKM FSQNLKDTHV LNNDAKNNYS YVSHGGLILI FKPVKNKEIV QLMNITHLLN
NTHANMTKHR RKRETSSSAS SKGIYDLYGD LNVAQVQFAF NTLKSYINQA LMSIADAWCR
DQKRTNEIWG IISKINPSAA LSAIFDKPVS ARYLGDVISV SKCINVNQDS VRIYQTLKVP
KTGEEWGDRM QCYSRPLVTF RLDNETASTI RTGQLGVDNE ILLGNYRTEL CQENSIRYFV
AGAQIHVFQD YDFYHTIKLS DVDIVDTFVH LNISFLQNID FQMLRLYTQE EQYASRLLDL
ETLLRDFNTY RQRIYKLEQA IVTKPYVPPA GMQQALQGLS GVGSVITGTL GAMQSLVSGV
ASFLQNPFGG TLSIILIGCI IVGVIIIYNR MNQSRGSPID YYFPYVNQTL PQRQLQQHVG
DPPSYDESIG SSHTYSKEDA LLMLKAMKEL DKSEKEAQIE ATKSQPSIID RIRRRGYTTL
SSMNI
