GH_ELHVK
ID GH_ELHVK Reviewed; 737 AA.
AC Q18LE9;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 38.
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 Elephantid herpesvirus 1 (isolate Asian elephant/Berlin/Kiba/1998) (EIHV-1)
OS (Elephant endotheliotropic herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Proboscivirus.
OX NCBI_TaxID=654902;
OH NCBI_TaxID=9783; Elephas maximus (Indian elephant).
OH NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH NCBI_TaxID=99490; Loxodonta cyclotis (African forest elephant).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17507487; DOI=10.1128/jvi.00255-07;
RA Ehlers B., Kuchler J., Yasmum N., Dural G., Voigt S., Schmidt-Chanasit J.,
RA Jakel T., Matuschka F.R., Richter D., Essbauer S., Hughes D.J., Summers C.,
RA Bennett M., Stewart J.P., Ulrich R.G.;
RT "Identification of novel rodent herpesviruses, including the first
RT gammaherpesvirus of Mus musculus.";
RL J. Virol. 81:8091-8100(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11172087; DOI=10.1099/0022-1317-82-3-475;
RA Ehlers B., Burkhardt S., Goltz M., Bergmann V., Ochs A., Weiler H.,
RA Hentschke J.;
RT "Genetic and ultrastructural characterization of a European isolate of the
RT fatal endotheliotropic elephant herpesvirus.";
RL J. Gen. Virol. 82:475-482(2001).
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; AF322977; ABG36570.1; -; Genomic_DNA.
DR SMR; Q18LE9; -.
DR PRIDE; Q18LE9; -.
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..25
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CHAIN 26..737
FT /note="Envelope glycoprotein H"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT /id="PRO_0000436652"
FT TOPO_DOM 26..702
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TRANSMEM 703..723
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TOPO_DOM 724..737
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT REGION 191..253
FT /note="Interaction with gL"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 683
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
SQ SEQUENCE 737 AA; 85745 MW; 8D3D6EBE716A0196 CRC64;
MLIRRRALWL TIPILIIMTS HKIMCAFDLS HVHSESCLKI QDISSDTINF TPNLVMFRFF
SNETHSDVFH LPKCIFDSKL TSYLFDHLNI YEDVSVYKNN FEKYYMGSVE GTYRTIIIKG
EDTTPYLDKT TAPTVEITEK DLIITYQGIR YMNPFPVLSL IDDESCEVFD DINELILPYF
GKCRKFYLNF GSVTLFGHIT SNFVTIKYTA QNGTDPYTIR LFFGNSAEIV HTLPFEAQDL
ALRMMMYDDF EIIGEVGPVK EMLKSFKLSL LDSLLEQNHE DVMNDFRHVF EAFYNHIKKI
RDGSIDIKSL HIEQLLDSLL AYSIGYYIQY RYPPYTGKWR GIEHFIETET YIHMVPELFD
LFAHNMTVKT PTRPNAIKFI NILIRLYSYT DYTKLDHRGL SLYFLKYIYQ GNVTDDIATY
AHRYMTNLYT KYTYPKTQEG EHLYKSYNDS LDTFILNTIG LKSKNKTLLH HILLLQTGMC
NIQNMIGHFH SLQNNDPKFG ALLSPCYRSL RYDLTAKKIG QLITKESLEP YGRLVNMVRF
MTKNSSMLNV LKCELPEDDG LLAIATVDNK TYIISSRPIA VGVVYKATYT AINLFLYVTR
IQNNTCIHID KVYRDGDVKA VYTFSLDTAK DCGDMCPSVL VEYQTNTGFI GIHVINSIAD
IQYISENRKL FPESSHYLWL LKNDTVLELE GTNFFLFSSK SPGAIVLYII IISLIVWTLY
EIIKLFCYKR QWQYQKL
