ID   GH_VZVD                 Reviewed;         841 AA.
AC   P09260;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 84.
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 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   SUBCELLULAR LOCATION.
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: 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-Rule:MF_04033,
CC       ECO:0000269|PubMed:15613328}; Single-pass type I membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_04033, ECO:0000269|PubMed:15613328}. Host
CC       cell membrane {ECO:0000255|HAMAP-Rule:MF_04033,
CC       ECO:0000269|PubMed:15613328}; Single-pass type I membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_04033, ECO:0000269|PubMed:15613328}. Host
CC       endosome membrane {ECO:0000255|HAMAP-Rule:MF_04033,
CC       ECO:0000269|PubMed:15613328}; Single-pass type I membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_04033, ECO:0000269|PubMed:15613328}.
CC       Note=During virion morphogenesis, this protein probably accumulates in
CC       the 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; X04370; CAA27920.1; -; Genomic_DNA.
DR   PIR; B27341; VGBE37.
DR   SMR; P09260; -.
DR   PRIDE; P09260; -.
DR   Proteomes; UP000002602; 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   3: Inferred from homology;
KW   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;
KW   Reference proteome; Sialic acid; Signal; Transmembrane;
KW   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_0000436663"
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"
SQ   SEQUENCE   841 AA;  93652 MW;  82B247F63CA51948 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 SLISLSSGPP 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 NPISVVYLSR DTCVSEHGVI ETVALPHPDN
     LKECLYCGSV FLRYLTTGAI MDIIIIDSKD TERQLAAMGN STIPPFNPDM HGDDSKAVLL
     FPNGTVVTLL GFERRQAIRM SGQYLGASLG GAFLAVVGFG IIGWMLCGNS RLREYNKIPL
     T