GH_VZVO
ID GH_VZVO Reviewed; 841 AA.
AC Q775J3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Envelope glycoprotein H {ECO:0000255|HAMAP-Rule:MF_04033};
DE Short=gH {ECO:0000255|HAMAP-Rule:MF_04033};
DE Flags: Precursor;
GN Name=gH {ECO:0000255|HAMAP-Rule:MF_04033}; ORFNames=ORF37;
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).
CC -!- FUNCTION: The heterodimer glycoprotein H-glycoprotein L is required for
CC the fusion of viral and plasma membranes leading to virus entry into
CC the host cell. Following initial binding to host receptor, membrane
CC fusion is mediated by the fusion machinery composed of gB and the
CC heterodimer gH/gL. May also be involved in the fusion between the
CC virion envelope and the outer nuclear membrane during virion
CC morphogenesis. {ECO:0000255|HAMAP-Rule:MF_04033}.
CC -!- SUBUNIT: Interacts with glycoprotein L (gL); this interaction is
CC necessary for the correct processing and cell surface expression of gH.
CC The heterodimer gH/gL seems to interact with gB trimers during fusion.
CC {ECO:0000255|HAMAP-Rule:MF_04033}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04033}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04033};
CC Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}.
CC Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass
CC type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. 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_04033}.
CC -!- PTM: N-glycosylated, O-glycosylated, and sialylated.
CC {ECO:0000255|HAMAP-Rule:MF_04033}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein H family.
CC {ECO:0000255|HAMAP-Rule:MF_04033}.
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DR EMBL; AY016446; AAK19939.1; -; Genomic_DNA.
DR EMBL; AB097932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB097933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ008354; AAY57649.1; -; Genomic_DNA.
DR EMBL; DQ008355; AAY57720.1; -; Genomic_DNA.
DR PDB; 4XHJ; X-ray; 3.16 A; A/E=1-795.
DR PDB; 4XI5; X-ray; 3.90 A; A=1-795.
DR PDBsum; 4XHJ; -.
DR PDBsum; 4XI5; -.
DR SMR; Q775J3; -.
DR IntAct; Q775J3; 5.
DR ABCD; Q775J3; 2 sequenced antibodies.
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: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:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.3190; -; 1.
DR HAMAP; MF_04033; HSV_GH; 1.
DR InterPro; IPR003493; Herpes_gH.
DR InterPro; IPR035305; Herpes_glycoH_C.
DR InterPro; IPR038172; Herpes_glycoH_C_sf.
DR Pfam; PF17488; Herpes_glycoH_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fusion of virus membrane with host cell membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host endosome; Host membrane; Membrane; Sialic acid;
KW Signal; Transmembrane; Transmembrane helix; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CHAIN 18..841
FT /note="Envelope glycoprotein H"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT /id="PRO_0000385473"
FT TOPO_DOM 18..802
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TRANSMEM 803..823
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TOPO_DOM 824..841
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT REGION 246..309
FT /note="Interaction with gL"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 760
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 783
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 72..81
FT /evidence="ECO:0007829|PDB:4XHJ"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:4XHJ"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 233..244
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 246..255
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 258..268
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 303..312
FT /evidence="ECO:0007829|PDB:4XHJ"
FT TURN 314..317
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 323..327
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 336..351
FT /evidence="ECO:0007829|PDB:4XHJ"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 361..385
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 390..409
FT /evidence="ECO:0007829|PDB:4XHJ"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 420..425
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 430..441
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 455..467
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 475..494
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 500..513
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 525..539
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 542..557
FT /evidence="ECO:0007829|PDB:4XHJ"
FT TURN 561..563
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 568..570
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 574..576
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 582..584
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 586..595
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 596..598
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 600..607
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 612..628
FT /evidence="ECO:0007829|PDB:4XHJ"
FT TURN 629..632
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 634..640
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 642..645
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:4XHJ"
FT TURN 651..655
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 657..662
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 667..674
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 678..683
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 694..701
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 705..707
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 711..714
FT /evidence="ECO:0007829|PDB:4XHJ"
FT TURN 718..720
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 730..735
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 740..742
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 749..755
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 764..766
FT /evidence="ECO:0007829|PDB:4XHJ"
FT TURN 768..770
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 775..780
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 786..790
FT /evidence="ECO:0007829|PDB:4XHJ"
SQ SEQUENCE 841 AA; 93640 MW; 7A22CFA48EDD8F3E CRC64;
MFALVLAVVI LPLWTTANKS YVTPTPATRS IGHMSALLRE YSDRNMSLKL EAFYPTGFDE
ELIKSLHWGN DRKHVFLVIV KVNPTTHEGD VGLVIFPKYL LSPYHFKAEH RAPFPAGRFG
FLSHPVTPDV SFFDSSFAPY LTTQHLVAFT TFPPNPLVWH LERAETAATA ERPFGVSLLP
ARPTVPKNTI LEHKAHFATW DALARHTFFS AEAIITNSTL RIHVPLFGSV WPIRYWATGS
VLLTSDSGRV EVNIGVGFMS SLISLSSGLP IELIVVPHTV KLNAVTSDTT WFQLNPPGPD
PGPSYRVYLL GRGLDMNFSK HATVDICAYP EESLDYRYHL SMAHTEALRM TTKADQHDIN
EESYYHIAAR IATSIFALSE MGRTTEYFLL DEIVDVQYQL KFLNYILMRI GAGAHPNTIS
GTSDLIFADP SQLHDELSLL FGQVKPANVD YFISYDEARD QLKTAYALSR GQDHVNALSL
ARRVIMSIYK GLLVKQNLNA TERQALFFAS MILLNFREGL ENSSRVLDGR TTLLLMTSMC
TAAHATQAAL NIQEGLAYLN PSKHMFTIPN VYSPCMGSLR TDLTEEIHVM NLLSAIPTRP
GLNEVLHTQL DESEIFDAAF KTMMIFTTWT AKDLHILHTH VPEVFTCQDA AARNGEYVLI
LPAVQGHSYV ITRNKPQRGL VYSLADVDVY NPISVVYLSK DTCVSEHGVI ETVALPHPDN
LKECLYCGSV FLRYLTTGAI MDIIIIDSKD TERQLAAMGN STIPPFNPDM HGDDSKAVLL
FPNGTVVTLL GFERRQAIRM SGQYLGASLG GAFLAVVGFG IIGWMLCGNS RLREYNKIPL
T
