GH_HHV1F
ID GH_HHV1F Reviewed; 838 AA.
AC Q9DHD5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 50.
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=UL22;
OS Human herpesvirus 1 (strain F) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10304;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kang H., Cha S.C., Han Y.J., Park I.H., Lee M.J., Byun S.M., Lee H.H.;
RT "High level production of glycoprotein H of HSV-1(F) using HcNPV vector
RT system.";
RL J. Biochem. Mol. Biol. 33:483-492(2000).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=18596102; DOI=10.1128/jvi.00904-08;
RA Loret S., Guay G., Lippe R.;
RT "Comprehensive characterization of extracellular herpes simplex virus type
RT 1 virions.";
RL J. Virol. 82:8605-8618(2008).
RN [3]
RP FUNCTION.
RX PubMed=19386594; DOI=10.1074/jbc.m109.005728;
RA Gianni T., Amasio M., Campadelli-Fiume G.;
RT "Herpes simplex virus gD forms distinct complexes with fusion executors gB
RT and gH/gL in part through the C-terminal profusion domain.";
RL J. Biol. Chem. 284:17370-17382(2009).
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 ECO:0000269|PubMed:19386594}.
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:18596102}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04033, ECO:0000269|PubMed:18596102}. Host
CC cell membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_04033,
CC ECO:0000269|PubMed:18596102}. Host endosome membrane
CC {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04033, ECO:0000269|PubMed:18596102}.
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; AF296257; AAG17895.1; -; Genomic_DNA.
DR BMRB; Q9DHD5; -.
DR SMR; Q9DHD5; -.
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..18
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CHAIN 19..838
FT /note="Envelope glycoprotein H"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT /id="PRO_0000385471"
FT TOPO_DOM 19..803
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TRANSMEM 804..824
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TOPO_DOM 825..838
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT REGION 174..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..323
FT /note="Interaction with gL"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 784
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
SQ SEQUENCE 838 AA; 90310 MW; EE73EF3DC9884922 CRC64;
MGNGLWFVGV IILGAAWGQV HDWTEQTDPW FLDGLGMDRM YWRDTNTGRL WLPNTPDPQK
PPRGFLAPPD ELNLTTASLP LLRWYEERFC FVLVTTAEFP RDPGQLLYIP KTYLLGRPPN
ASLPAPTTVE PTAQPPPAVA PLKGLLHNPT ASVLLRSRAW VTFSAVPDPE ALTFPRGDNV
ATASHPSGPR DTPPPRPPVG ARRHPTTELD ITHLHNASTT WLATRGLLRS PGRYVYFSPS
ASTWPVGIWT TGELVLGCDA ALVRARYGRE FMGLVISMHD SPPAEVMVVP AGQTLDRVGD
PADENPPGAL PGPPGGPRYR VFVLGSLTRA DNGSALDALR RVGGYPEEGT NYAQFLSRAY
AEFFSGDAGA EQGPRPPLFW RLTGLLATSG FAFVNAAHAN GAVCLSDLLG FLAHSRALAG
LAARGAAGCA ADSVFFNVSV LDPTARLQLE ARLQHLVAEI LEREQSLALH ALGYQLAFVL
DSPSAYDAVA PSAAHLIDAL YAEFLGGRVV TTPVVHRALF YASAVLRQPF LAGVPSAVQR
ERARRSLLIA SALCTSDVAA ATNADLRTAL ARADHQKTLF WLPDHFSPCA ASLRFDLDES
VFILDALAQA TRSETPVEVL AQQTHGLAST LTRWAHYNAL IRAFVPEASH RCGGQSANVE
PRILVPITHN ASYVVTHSPL PRGIGYKLTG VDVRRPLFLT YLTATCEGST RDIESKRLVR
TQNQRDLGLV GAVFMRYTPA GEVMSVLLVD TDNTQQQIAA GPTEGAPSVF SSDVPSTALL
LFPNGTVIHL LAFDTQPVAA IAPGFLAASA LGVVMITAAL AGILKVLRTS VPFFWRRE
