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GH_EHV1
ID   GH_EHV1                 Reviewed;         848 AA.
AC   P68330; P09101; Q66681;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 61.
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};
OS   Equine herpesvirus 1 (strain HVS25A) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10327;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1666854; DOI=10.3109/10425179109020779;
RA   Robertson G.R., Scott N.A., Miller J.M., Sabine M., Zheng M., Bell C.W.,
RA   Whalley J.M.;
RT   "Sequence characteristics of a gene in equine herpesvirus 1 homologous to
RT   glycoprotein H of herpes simplex virus.";
RL   DNA Seq. 1:241-249(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-256.
RX   PubMed=2849761; DOI=10.1093/nar/16.23.11303;
RA   Robertson G.R., Whalley J.M.;
RT   "Evolution of the herpes thymidine kinase: identification and comparison of
RT   the equine herpesvirus 1 thymidine kinase gene reveals similarity to a
RT   cell-encoded thymidylate kinase.";
RL   Nucleic Acids Res. 16:11303-11317(1988).
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; X51324; CAA35707.1; -; Genomic_DNA.
DR   EMBL; X13209; CAA31600.1; -; Genomic_DNA.
DR   EMBL; X13209; CAA31601.1; -; Genomic_DNA.
DR   PIR; E36799; VGBED3.
DR   RefSeq; YP_053085.1; NC_001491.2.
DR   SMR; P68330; -.
DR   GeneID; 1487534; -.
DR   KEGG; vg:1487534; -.
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; 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..24
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CHAIN           25..848
FT                   /note="Envelope glycoprotein H"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT                   /id="PRO_0000038238"
FT   TOPO_DOM        25..808
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   TRANSMEM        809..829
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   TOPO_DOM        830..848
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   REGION          166..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          240..303
FT                   /note="Interaction with gL"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        41
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        60
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        496
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        672
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        766
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT   CARBOHYD        789
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
SQ   SEQUENCE   848 AA;  92842 MW;  AD0C64DAE9EA5A7E CRC64;
     MLQPYRKMLI FAVVTVAFAM AVWSTPVPAT PSGVGNATWA NNSFNITRYD KITMGQVYSN
     TSNSPIFFVV ISERNFRIVN TPLGASVFWI PKGAMNPPQH QPCVANGPEP GDPRGPCVNS
     TVSLLFNENV EPFLMSKNLL EFEVLPDTYI TGWTFERSKT ATTKSNPVGV VLSPPRGSPS
     ANTTIRDDGG PKKPLSIIDE YTTLVADLQN FTMTLTYISP FAAVWPIEAF QTGITVMGCD
     TTQVVAYLGH GFMGLQISSV NNPPLEMIVV PNDVSARILN RRPSRLRLEP PGPHAGPIYK
     VYVLSDGNFY LGHGMSRISR EVAAYPEESL DYRYHLSLAN LDTLAMLAEL SSGKSTDVSY
     YMYRIVARLA VATFSLAEVI RLSDYMLLQE AIDVDMNLRL IVPLVMKYAA GGAADSSYTS
     SDVAMDQFDV AQSQIEKIVS DINVEAELRK PMYEHRSLLR SVYAYSRKPL PNAVALADRL
     ILAMYKEAIK DRITWNSTMR EVLFFAVGAA AGSHVILTDE PEPGAPAHKD ASLFLSLNRN
     ILLLCTAMCT ASHAVSAGLK LEEVMAGLVA GGVQFSLLEV FSPCMASTRF DLAEEEHVLD
     LLSVIPPRLY TDLNTGFEDD GTTIHSYGRS ANGILNSRIA YNFDAVSVFT PELASCSTKL
     PKVLVVLPIF TNRSYVITRT APSIGLTYSL DGVNIAKPIV ISYITYGNCE VSRATIKSGY
     LDNPGHTQTC VYCGSVFMRY MVSGAIMDLI YIDDKEVELQ LVAGENSTIP AFNPKLYTPS
     MNALLMFPNG TVTLMSAFAS YSSFKVPSTY LWASIGGLLL AILILYIIIK MLCGGVTNDG
     YKLLLSYE
 
 
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