GB_VZVD
ID GB_VZVD Reviewed; 931 AA.
AC P09257;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 93.
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 Dumas) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10338;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA Davison A.J., Scott J.E.;
RT "The complete DNA sequence of varicella-zoster virus.";
RL J. Gen. Virol. 67:1759-1816(1986).
RN [2]
RP IDENTIFICATION OF START CODON, AND INTERACTION WITH GLYCOPROTEIN E.
RC STRAIN=VZV 80-2;
RX PubMed=12627491; DOI=10.1002/jmv.10324;
RA Maresova L., Pasieka T.J., Wagenaar T., Jackson W., Grose C.;
RT "Identification of the authentic varicella-zoster virus gB (gene 31)
RT initiating methionine overlapping the 3' end of gene 30.";
RL J. Med. Virol. 70:S64-S70(2003).
RN [3]
RP SUBCELLULAR LOCATION, AND INTERNALIZATION MOTIF.
RC STRAIN=VZV-32;
RX PubMed=15613328; DOI=10.1128/jvi.79.2.997-1007.2005;
RA Maresova L., Pasieka T.J., Homan E., Gerday E., Grose C.;
RT "Incorporation of three endocytosed varicella-zoster virus glycoproteins,
RT gE, gH, and gB, into the virion envelope.";
RL J. Virol. 79:997-1007(2005).
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 (By similarity).
CC Interacts with gE. {ECO:0000255|HAMAP-Rule:MF_04032,
CC ECO:0000269|PubMed:15613328}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04032,
CC ECO:0000269|PubMed:15613328}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04032, ECO:0000269|PubMed:15613328}. Host
CC cell membrane {ECO:0000255|HAMAP-Rule:MF_04032,
CC ECO:0000269|PubMed:15613328}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04032, ECO:0000269|PubMed:15613328}. Host
CC endosome membrane {ECO:0000255|HAMAP-Rule:MF_04032,
CC ECO:0000269|PubMed:15613328}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04032, ECO:0000269|PubMed:15613328}. Host
CC Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass
CC type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032,
CC ECO:0000269|PubMed:15613328}. Note=During virion morphogenesis, this
CC protein probably accumulates in the endosomes and trans-Golgi where
CC secondary envelopment occurs. It is probably transported to the cell
CC surface from where it is endocytosed and directed to the trans-Golgi
CC 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.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein B family.
CC {ECO:0000255|HAMAP-Rule:MF_04032}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA27914.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X04370; CAA27914.1; ALT_INIT; Genomic_DNA.
DR PIR; E27214; VGBE31.
DR PDB; 6VN1; EM; 2.80 A; A/B/C=1-931.
DR PDBsum; 6VN1; -.
DR SMR; P09257; -.
DR PRIDE; P09257; -.
DR ABCD; P09257; 1 sequenced antibody.
DR Proteomes; UP000002602; 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; Reference proteome; 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_0000038189"
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 904..906
FT /note="Di-leucine internalization motif"
FT /evidence="ECO:0000255"
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 STRAND 129..133
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 163..181
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 186..197
FT /evidence="ECO:0007829|PDB:6VN1"
FT HELIX 200..210
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 211..221
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:6VN1"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 274..286
FT /evidence="ECO:0007829|PDB:6VN1"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:6VN1"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 355..360
FT /evidence="ECO:0007829|PDB:6VN1"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 370..383
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:6VN1"
FT TURN 394..397
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 398..405
FT /evidence="ECO:0007829|PDB:6VN1"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:6VN1"
FT HELIX 417..433
FT /evidence="ECO:0007829|PDB:6VN1"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 454..462
FT /evidence="ECO:0007829|PDB:6VN1"
FT HELIX 513..553
FT /evidence="ECO:0007829|PDB:6VN1"
FT TURN 554..556
FT /evidence="ECO:0007829|PDB:6VN1"
FT HELIX 558..565
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 576..580
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 589..598
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 605..611
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 613..621
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 624..629
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 631..638
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 642..644
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 650..655
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 658..672
FT /evidence="ECO:0007829|PDB:6VN1"
FT HELIX 673..675
FT /evidence="ECO:0007829|PDB:6VN1"
FT STRAND 676..679
FT /evidence="ECO:0007829|PDB:6VN1"
FT HELIX 703..706
FT /evidence="ECO:0007829|PDB:6VN1"
FT HELIX 714..721
FT /evidence="ECO:0007829|PDB:6VN1"
FT HELIX 724..728
FT /evidence="ECO:0007829|PDB:6VN1"
SQ SEQUENCE 931 AA; 105347 MW; 4844DB77C69A56A3 CRC64;
MSPCGYYSKW RNRDRPEYRR NLRFRRFFSS IHPNAAAGSG FNGPGVFITS VTGVWLCFLC
IFSMFVTAVV SVSPSSFYES LQVEPTQSED ITRSAHLGDG DEIREAIHKS QDAETKPTFY
VCPPPTGSTI VRLEPTRTCP 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
