GB_VZVO
ID GB_VZVO Reviewed; 931 AA.
AC Q4JR05; Q4JQU4; Q775J4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 02-JUN-2021, entry version 61.
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=ORF31;
OS Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=341980;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oka varicella vaccine Biken (V-Oka-Biken);
RX PubMed=11162813; DOI=10.1006/viro.2000.0775;
RA Faga B., Maury W., Bruckner D.A., Grose C.;
RT "Identification and mapping of single nucleotide polymorphisms in the
RT varicella-zoster virus genome.";
RL Virology 280:1-6(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate Human/Japan/P-Oka/1970, and
RC Oka varicella vaccine Biken (V-Oka-Biken);
RX PubMed=12388706; DOI=10.1128/jvi.76.22.11447-11459.2002;
RA Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M., Yamanishi K.;
RT "Comparison of the complete DNA sequences of the Oka varicella vaccine and
RT its parental virus.";
RL J. Virol. 76:11447-11459(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oka varicella vaccine VarilRix (V-Oka-GSK), and
RC Oka varicella vaccine Varivax (V-Oka-Merk);
RX PubMed=18787000; DOI=10.1128/jvi.00777-08;
RA Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M.,
RA Vassilev V.;
RT "Complete DNA sequences of two oka strain varicella-zoster virus genomes.";
RL J. Virol. 82:11023-11044(2008).
RN [4]
RP SUBCELLULAR LOCATION, INTERNALIZATION MOTIFS, AND MUTAGENESIS OF TYR-881;
RP 904-LEU-LEU-905 AND TYR-920.
RX PubMed=11414804; DOI=10.1006/viro.2001.0930;
RA Heineman T.C., Hall S.L.;
RT "VZV gB endocytosis and Golgi localization are mediated by YXXphi motifs in
RT its cytoplasmic domain.";
RL Virology 285:42-49(2001).
RN [5]
RP MUTAGENESIS OF 491-ARG--ARG-494.
RX PubMed=19474103; DOI=10.1128/jvi.00400-09;
RA Oliver S.L., Sommer M.H., Zerboni L., Rajamani J., Grose C., Arvin A.M.;
RT "Mutagenesis of varicella-zoster virus glycoprotein B: putative fusion loop
RT residues are essential for viral replication and the furin cleavage motif
RT contributes to pathogenesis in skin in vivo.";
RL J. Virol. 83:7495-7506(2009).
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,
CC ECO:0000269|PubMed:11414804}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04032}. Note=During virion morphogenesis,
CC this protein probably accumulates in the endosomes and trans-Golgi
CC where secondary envelopment occurs. It is probably transported to the
CC cell surface from where it is endocytosed and directed to the trans-
CC Golgi network (TGN). {ECO:0000255|HAMAP-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK19938.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAY57644.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAY57715.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY016445; AAK19938.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB097932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB097933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ008354; AAY57644.1; ALT_INIT; Genomic_DNA.
DR EMBL; DQ008355; AAY57715.1; ALT_INIT; Genomic_DNA.
DR PDB; 6VLK; X-ray; 2.45 A; A/B=1-736.
DR PDBsum; 6VLK; -.
DR SMR; Q4JR05; -.
DR DIP; DIP-56356N; -.
DR IntAct; Q4JR05; 5.
DR Proteomes; UP000002603; Genome.
DR Proteomes; UP000008504; Genome.
DR Proteomes; UP000008505; Genome.
DR Proteomes; UP000008506; 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.
DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Host cell membrane;
KW Host endosome; Host Golgi apparatus; Host membrane; Host-virus interaction;
KW Membrane; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..71
FT /evidence="ECO:0000255"
FT CHAIN 72..931
FT /note="Envelope glycoprotein B"
FT /id="PRO_0000385466"
FT TOPO_DOM 72..786
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 808..931
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 179..185
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 264..271
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 731..784
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 764..784
FT /note="Hydrophobic membrane proximal region"
FT MOTIF 881..884
FT /note="Golgi targeting"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT MOTIF 920..923
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT SITE 494..495
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 503
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 CARBOHYD 686
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 122..584
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 139..540
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 213..277
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 369..417
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 608..645
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT MUTAGEN 491..494
FT /note="RSRR->GSGG: Attenuation of viral replication in
FT human skin xenografts in vivo."
FT /evidence="ECO:0000269|PubMed:19474103"
FT MUTAGEN 881
FT /note="Y->A: No effect on internalization. Complete loss of
FT Golgi targeting leads to mislocalization to the cytoplasm."
FT /evidence="ECO:0000269|PubMed:11414804"
FT MUTAGEN 904..905
FT /note="LL->HA: Complete loss of internalization leads to
FT mislocalization to the plasma membrane."
FT /evidence="ECO:0000269|PubMed:11414804"
FT MUTAGEN 920
FT /note="Y->A: No effect on internalization and Golgi
FT targeting."
FT /evidence="ECO:0000269|PubMed:11414804"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 148..158
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 163..181
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 186..197
FT /evidence="ECO:0007829|PDB:6VLK"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:6VLK"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 211..221
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:6VLK"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 269..286
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:6VLK"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:6VLK"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:6VLK"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:6VLK"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 370..385
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:6VLK"
FT TURN 394..397
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:6VLK"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:6VLK"
FT HELIX 417..433
FT /evidence="ECO:0007829|PDB:6VLK"
FT TURN 434..437
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:6VLK"
FT TURN 450..452
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 453..462
FT /evidence="ECO:0007829|PDB:6VLK"
FT HELIX 513..553
FT /evidence="ECO:0007829|PDB:6VLK"
FT TURN 554..556
FT /evidence="ECO:0007829|PDB:6VLK"
FT HELIX 558..565
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 570..574
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 576..583
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 589..595
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 605..611
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 613..618
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 624..629
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 634..638
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 642..644
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 650..655
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 658..663
FT /evidence="ECO:0007829|PDB:6VLK"
FT STRAND 666..672
FT /evidence="ECO:0007829|PDB:6VLK"
FT HELIX 673..675
FT /evidence="ECO:0007829|PDB:6VLK"
FT HELIX 703..706
FT /evidence="ECO:0007829|PDB:6VLK"
FT HELIX 714..721
FT /evidence="ECO:0007829|PDB:6VLK"
FT HELIX 724..728
FT /evidence="ECO:0007829|PDB:6VLK"
SQ SEQUENCE 931 AA; 105343 MW; 4397ABA2A874C570 CRC64;
MSPCGYYSKW RNRDRPEYRR NLRFRRFFSS IHPNAAAGSG FNGPGVFITS VTGVWLCFLC
IFSMFVTAVV SVSPSSFYES LQVEPTQSED ITRSAHLGDG DEIREAIHKS QDAETKPTFY
VCPPPTGSTI VRLEPPRTCP DYHLGKNFTE GIAVVYKENI AAYKFKATVY YKDVIVSTAW
AGSSYTQITN RYADRVPIPV SEITDTIDKF GKCSSKATYV RNNHKVEAFN EDKNPQDMPL
IASKYNSVGS KAWHTTNDTY MVAGTPGTYR TGTSVNCIIE EVEARSIFPY DSFGLSTGDI
IYMSPFFGLR DGAYREHSNY AMDRFHQFEG YRQRDLDTRA LLEPAARNFL VTPHLTVGWN
WKPKRTEVCS LVKWREVEDV VRDEYAHNFR FTMKTLSTTF ISETNEFNLN QIHLSQCVKE
EARAIINRIY TTRYNSSHVR TGDIQTYLAR GGFVVVFQPL LSNSLARLYL QELVRENTNH
SPQKHPTRNT RSRRSVPVEL RANRTITTTS SVEFAMLQFT YDHIQEHVNE MLARISSSWC
QLQNRERALW SGLFPINPSA LASTILDQRV KARILGDVIS VSNCPELGSD TRIILQNSMR
VSGSTTRCYS RPLISIVSLN GSGTVEGQLG TDNELIMSRD LLEPCVANHK RYFLFGHHYV
YYEDYRYVRE IAVHDVGMIS TYVDLNLTLL KDREFMPLQV YTRDELRDTG LLDYSEIQRR
NQMHSLRFYD IDKVVQYDSG TAIMQGMAQF FQGLGTAGQA VGHVVLGATG ALLSTVHGFT
TFLSNPFGAL AVGLLVLAGL VAAFFAYRYV LKLKTSPMKA LYPLTTKGLK QLPEGMDPFA
EKPNATDTPI EEIGDSQNTE PSVNSGFDPD KFREAQEMIK YMTLVSAAER QESKARKKNK
TSALLTSRLT GLALRNRRGY SRVRTENVTG V
