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GH_GAHVM
ID   GH_GAHVM                Reviewed;         813 AA.
AC   Q9E6P6;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=MDV034;
OS   Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS   disease herpesvirus type 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX   NCBI_TaxID=10389;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA   Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT   "The genome of a very virulent Marek's disease virus.";
RL   J. Virol. 74:7980-7988(2000).
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; AF243438; AAG14214.1; -; Genomic_DNA.
DR   RefSeq; YP_001033950.1; NC_002229.3.
DR   SMR; Q9E6P6; -.
DR   GeneID; 4811495; -.
DR   KEGG; vg:4811495; -.
DR   Proteomes; UP000008072; 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..18
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CHAIN           19..813
FT                   /note="Envelope glycoprotein H"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT                   /id="PRO_0000436653"
FT   TOPO_DOM        19..769
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   TRANSMEM        770..790
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   TOPO_DOM        791..813
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   REGION          135..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..273
FT                   /note="Interaction with gL"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        410
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        434
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        576
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        727
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        750
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
SQ   SEQUENCE   813 AA;  90903 MW;  1059AEEEA8257882 CRC64;
     MGLPGSIVFL IMIHAFCAKK TPTNTLPSLL SLLGITDLPS LRLNILSLDG SANNQGSWVR
     DNTTFVYIGA SSPANGVLFY MPTSHVQQMT FYKRPVSKLL ASNNLIKFLN TGSYINHSFM
     TAMPPYRRNV QIPSDRSGLK LDDKDDAQPT GTNPPTELKN LKPIDVVNPE HRFILTSELT
     GTYVKHVCFV DPMDMLIPVD YAHIRTIIFG SDGAEVIMKI GITFASITIS MKSAPPVELI
     LSERARNISL IWPALKPYEP VDKFTRRPYL IYLLGPHMNA SDMEIKSYIN MIESVEESSN
     YDFQIAQTHA QLFIFAATPI SDINDIYCFR VVTTRLFMSL VASVRNAFQS GYISFDEIIK
     TEANIKMITE TLSTFALHSN PGTYFLLSGM HLRNENADII KSLIRKTIIN ASKNTASLSI
     LQHLYVLRSA YAFNISQESG NLGEHVSSIS LELIIALHEE SVRDTIAWNT SARHALYYAF
     ASIFQRPPNE WDASRTARKA LLFASSMCTE EHIVATELVI QEMYIKINVK NSPVHILDVY
     TPCVTALRMD ISEHHHRLYA MSDVILHPVI EKYLENDSRG IDAEEELETK AELVITKLKT
     PLMRRLTIYA SEVVTCSDAD ILEATALLVL PISGLGSYVV TRQLGIRGIV YNVDGVDVNN
     QLYITYVRLP CTTTAGNIVP MVLPRPLGSD CPYCGCVLLR YSTNGNLRHT IYISSQDLQR
     ELIAGGNSSI RYFNPTIAQI YGTSLLLYPN GTIVRILAFE SERVTIISAT YVATATAGAS
     IAISIAIITV RMIINNFRYN YHRYKKLSLY DDL
 
 
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