GB_GAHVR
ID GB_GAHVR Reviewed; 865 AA.
AC P18538;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 02-JUN-2021, entry version 92.
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 Gallid herpesvirus 2 (strain RB-1b) (GaHV-2) (Marek's disease herpesvirus
OS type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=33707;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2544666; DOI=10.1099/0022-1317-70-7-1789;
RA Ross L.J.N., Sanderson M., Scott S.D., Binns M.M., Doel T., Milne B.;
RT "Nucleotide sequence and characterization of the Marek's disease virus
RT homologue of glycoprotein B of herpes simplex virus.";
RL J. Gen. Virol. 70:1789-1804(1989).
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; D13713; BAA02866.1; -; Genomic_DNA.
DR RefSeq; YP_001033956.1; NC_002229.3.
DR SMR; P18538; -.
DR PRIDE; P18538; -.
DR GeneID; 4811501; -.
DR KEGG; vg:4811501; -.
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..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 22..865
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000038176"
FT TOPO_DOM 22..731
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 732..752
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 753..865
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 106..112
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 191..198
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 676..729
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 683..729
FT /note="Hydrophobic membrane proximal region"
FT REGION 843..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 809..812
FT /note="Golgi targeting"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT MOTIF 850..853
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT SITE 434..435
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 406
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 631
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 49..530
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 66..486
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 140..204
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 298..346
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 553..590
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 865 AA; 98092 MW; B30E93C1AC65C6C3 CRC64;
MHYFRRNCIF FLIVILYGTN SSPSTQNVTS REVVSSVQLS EEESTFYLCP PPVGSTVIRL
EPPRKCPEPR KATEWGEGIA ILFKENISPY KFKVTLYYKN IIQTTTWTGT TYRQITNRYT
DRTPVSIEEI TDLIDGKGRC SSKARYLRNN VYVEAFDRDA GEKQVLLKPS KFNTPESRAW
HTTNETYTVW GSPWIYRTGT SVNCIVEEMD ARSVFPYSYF AMANGDIANI SPFYGLSPPE
AAAEPMGYPQ DNFKQLDSYF SMDLDKRRKA SLPVKRNFLI TSHFTVGWDW APKTTRVCSM
TKWKEVTEML RATVNGRYRF MARELSATFI SNTTEFDPNR IILGQCIKRE AEAAIEQIFR
TKYNDSHVKV GHVQYFLALG GFIVAYQPVL SKSLAHMYLR ELMRDNRTDE MLDLVNNKHA
IYKKNATSLS RLRRDIRNAP NRKITLDDTT AIKSTSSVQF AMLQFLYDHI QTHINDMFSR
IATAWCELQN RELVLWHEGI KINPSATASA TLGRRVAAKM LGDVAAVSSC TAIDAESVTL
QNSMRVITST NTCYSRPLVL FSYGENQGNI QGQLGENNEL LPTLEAVEPC SANHRRYFLF
GSGYALFENY NFVKMVDAAD IQIASTFVEL NLTLLEDREI LPLSVYTKEE LRDVGVLDYA
EVARRNQLHE LKFYDINKVI EVDTNYAFMN GLAELFNGMG QVGQAIGKVV VGAAGAIVST
ISGVSAFMSN PFGALAIGLI IIAGLVAAFL AYRYVNKLKS NPMKALYPMT TEVLKAQATR
ELHGEESDDL ERTSIDERKL EEAREMIKYM ALVSAEERHE KKLRRKRRGT TAVLSDHLAK
MRIKNSNPKY DKLPTTYSDS EDDAV
