GH_EHV4
ID GH_EHV4 Reviewed; 855 AA.
AC P24430;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 84.
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 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10333;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2167933; DOI=10.1099/0022-1317-71-8-1793;
RA Nicolson L., Cullinane A.A., Onions D.E.;
RT "The nucleotide sequence of an equine herpesvirus 4 gene homologue of the
RT herpes simplex virus 1 glycoprotein H gene.";
RL J. Gen. Virol. 71:1793-1800(1990).
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; D14486; BAA03379.1; -; Genomic_DNA.
DR PIR; A36656; VGBE41.
DR RefSeq; NP_045257.1; NC_001844.1.
DR SMR; P24430; -.
DR GeneID; 1487605; -.
DR KEGG; vg:1487605; -.
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..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CHAIN 20..855
FT /note="Envelope glycoprotein H"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT /id="PRO_0000038240"
FT TOPO_DOM 20..815
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TRANSMEM 816..836
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TOPO_DOM 837..855
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT REGION 174..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..310
FT /note="Interaction with gL"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 773
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 796
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
SQ SEQUENCE 855 AA; 94086 MW; E4BC08B85DC33011 CRC64;
MSQPYLKIAI LVAATIVSAI PVWTTPVSTS PPQQTKLHYV GNGTWVHNNT FNVTRYDRIT
MEPVYNNNLS STTFFVAISE RNFRTVNTPL GASVFWILKS ALNPPKHQPC IANVPEPGDP
RGPCVNSTVS LFFNDNLEPF LMTKNLLEFE VLPDNYITGW TFERSKTVAT KGNPVGVVLS
PPRTSPDVNN TIRDDGTPKQ HLSIIDEHTT FVLDLQNFTK TLTYISPFAA VWPITAFHAG
ITVMGCDTTQ AIAYLGNGFM GLQISSVNNP PLEMIVAPND VRARIVNRLP PRRRLEPPGP
YAGPIYKVYV LSDGNFYLGH GMSKISREVA AYPEESLDYR YHLSLANLDT LAMLAELSSG
KSKDVSYYLY RIIARLAVAT FSLAEVIRLS DYMLLQEAID VDINLRLIVP LVMKYAAGGT
ADSSYTSSDV AMDQFEVAQA QIEKIVADIN IENELRKPMY EHRSLLKSVY AYSRKPLPNA
VSFANRLITA MYKEAIKDRI TWNSTMREVL FFAVGAAAGS HVILTDGPDL GLHAHKDSSM
FLSLNRNILL LCTAMCTASH AVSAGVKLEE VMAGLIAGGV QFSLLEVFSP CMASARFDLA
EEEHVLDLLS VIPPRLYTDL NTGLEDDGTT IHSYGRSANG ILNSRIAYNF DAVRVFTPEL
ASCSTKLPKV LVVLPLASNR SYVITRTAPN IGLTYSLDGV NIAKPIVISY ITYGNCQVSR
ATIRSVYLDH PGHTQSCVYC GSVFMRYMAS GAIMDLIYID DKDVELQLVA GENSTIPAFN
PKLYTPSMNA LLMFPNGTVT LMSAFASYSA FKIPSTYLWA SIGGLLLAIL ILYVIVKMLC
GGVINNDYSL LLNSE
