GB_HSV2S
ID GB_HSV2S Reviewed; 885 AA.
AC P24994;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 02-JUN-2021, entry version 90.
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 Herpes simplex virus type 2 (strain SA8) (Simian agent 8).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10316;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B264;
RX PubMed=1895066; DOI=10.1099/0022-1317-72-9-2299;
RA Borchers K., Weigelt W., Buhk H.-J., Ludwig H., Mankertz J.;
RT "Conserved domains of glycoprotein B (gB) of the monkey virus, simian agent
RT 8, identified by comparison with herpesvirus gBs.";
RL J. Gen. Virol. 72:2299-2304(1991).
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; X56935; CAA40256.1; -; Genomic_DNA.
DR SMR; P24994; -.
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..34
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 35..885
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000038166"
FT TOPO_DOM 35..759
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 760..780
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 781..885
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 29..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..160
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 239..246
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 455..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..757
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 716..756
FT /note="Hydrophobic membrane proximal region"
FT REGION 866..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 834..837
FT /note="Golgi targeting"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT MOTIF 874..877
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 97..558
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 114..514
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 188..252
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 345..393
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 581..618
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 885 AA; 97812 MW; 39E495B329AB94E4 CRC64;
MRPRGTPPSF LPLPVLLALA VIAAAGRAAP AAAAAPTADP AATPALPEDE EVPDEDGEGV
ATPAPAANAS VEAGRATLRE DLREIKARDG DATFYVCPPP TGATVVQFEQ PRPCPRAPDG
QNYTEGIAVV FKENIAPYKF KATMYYKDVT VSQVWFGHRY SQFMGIFEDR APVPFEEVMD
KINAKGVCRS TAKYVRNNME STAFHRDDHE SDMALKPAKA ATRTSRGWHT TDLKYNPARV
EAFHRYGTTV NCIVEEVEAR SVYPYDEFVL ATGDFVYMSP FYGYRDGSHG EHTAYAADRF
RQVDGYYERD LSTGRRAAAP VTRNLLTTPK FTVGWDWAPK RPSVCTLTKW REVDEMLRAE
YGPSFRFSSA ALSTTFTANR TEYALSRVDL ADCVGREARE AVDRIFLRRY NGTHVKVGQV
QYYLATGGFL IAYQPLLSNA LVELYVRELV REQTRRPAGG DPGEAATPGP SVDPPSVERI
KTTSSVEFAR LQFTYDHIQR HVNDMLGRIA TAWCELQNRE LTLWNEARRL NPGAIASATV
GRRVSARMLG DVMAVSTCVP VAPDNVIMQN SIGVAARPGT CYSRPLVSFR YEADGPLVEG
QLGEDNEIRL ERDALEPCTV GHRRYFTFGA GYVYFEEYAY SHQLGRADVT TVSTFINLNL
TMLEDHEFVP LEVYTRQEIK DSGLLDYTEV QRRNQLHALR FADIDTVIKA DAHAALFAGL
YSFFEGLGDV GRAVGKVVMG IVGGVVSAVS GVSSFLSNPF GALAVGLLVL AGLAAAFFAF
RYVMRLQRNP MKALYPLTTK ELKSDGAPLA GGGEDGAEDF DEAKLAQARE MIRYMALVSA
MERTEHKARK KGTSALLSAK VTDAVMRKRA RPRYSPLRDT DEEEL
