GH_FHV1
ID GH_FHV1 Reviewed; 821 AA.
AC P13160; Q86643;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 25-MAY-2022, entry version 77.
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 Feline herpesvirus 1 (FeHV-1) (Feline viral rhinotracheitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10334;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8394688; DOI=10.1007/bf01309852;
RA Maeda K., Kawaguchi Y., Kamiya N., Ono M., Tohya Y., Kai C., Mikami T.;
RT "Identification and nucleotide sequence of a gene in feline herpesvirus
RT type 1 homologous to the herpes simplex virus gene encoding the
RT glycoprotein H.";
RL Arch. Virol. 132:183-191(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX PubMed=2746729; DOI=10.1128/jvi.63.8.3240-3249.1989;
RA Nunberg J.H., Wright D.K., Cole G.E., Petrovskis E.A., Post L.E.,
RA Compton T., Gilbert J.H.;
RT "Identification of the thymidine kinase gene of feline herpesvirus: use of
RT degenerate oligonucleotides in the polymerase chain reaction to isolate
RT herpesvirus gene homologs.";
RL J. Virol. 63:3240-3249(1989).
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; S64566; AAB27840.1; -; Genomic_DNA.
DR EMBL; M26660; AAA46173.1; -; Genomic_DNA.
DR SMR; P13160; -.
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..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CHAIN 21..821
FT /note="Envelope glycoprotein H"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT /id="PRO_0000038248"
FT TOPO_DOM 21..783
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TRANSMEM 784..804
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TOPO_DOM 805..821
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT REGION 163..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..299
FT /note="Interaction with gL"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 647
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
SQ SEQUENCE 821 AA; 92511 MW; 1F14D4CC944044F7 CRC64;
MMCLIIYLSI FLIIVSRMLT GLPMMDRPDE GGLARRTVGE VEGEFSYRDD VDVADVRNLF
IMLPKNGSDI FLFIFDRRSQ RQRGTMFLFP KAGFVQPTPA KVRDEAAAAP FGFISPVYPL
SSLLFNPYNG RYLTTRHLIA FEVTPESSLH DWYFARSPTT ATQTQPLGHI TNPPRRSPKD
KPTTSGHTDL IIRYCALELD FFQDTRRQRD GIYLPNYEAV WPLAMNFLEG MWIWSNRTLV
NVTIGVGFMG FSLTSISYPP LEIIVTPHYT NARMITRFKS SLVLDPPGPS EGPLYKVYVL
GYGNNRINGS FYKTMRTIAS YPRTKPRLSL PPFHGTYGTA LFLSHATPQD MDGTTAYISK
ISTRLATALF SLSEVRRLSG YVAIDELIDL DFNTRLLANT LLADGMQNFQ DPINITYYYN
SDVGRTHLRD ALDTIDHQHV SHGSLITRAR YLQLIYTYTS MEKQSQLSLK LSGDIVKDLY
LETLYSDVVR WNTTAKQALF LSSMLIYIAG NIQSSVEQEA INAGRMLFLQ CTSMCTTEHA
STVRWNPQQI LYDLTKSSTR FNIFDGFSPC MASNRYDIIS PYGILDLFSA FPISSYRSIE
KPAVDSNTHN IIFNLRNLYT FIPELFSCPG VSSNHQRPIA VLPIGINCTY LITRRDPRRG
TLYIVDGIDV SNPIIISYLR SGECGIERGI ILPGNLNNPE NTDQCLYCGC VFMRYKSSGE
IVDLLLINDK AVELELVAGE NSTISAFNPT KYSSPSSVLL LFPNGTIVTL MAFTSHEVIV
FSSNFIWASI GGVFAACLII YIIIKMLCSF TPDVRYTLLN N
