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
