GH_MUHVS
ID GH_MUHVS Reviewed; 725 AA.
AC P30673; Q07745;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 25-MAY-2022, entry version 74.
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}; Synonyms=UL75;
OS Murid herpesvirus 1 (strain Smith) (MuHV-1) (Mouse cytomegalovirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Muromegalovirus.
OX NCBI_TaxID=10367;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8113726; DOI=10.1099/0022-1317-75-1-183;
RA Rapp M., Lucin P., Messerle M., Loh L.C., Koszinowski U.H.;
RT "Expression of the murine cytomegalovirus glycoprotein H by recombinant
RT vaccinia virus.";
RL J. Gen. Virol. 75:183-188(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1321219; DOI=10.1099/0022-1317-73-7-1849;
RA Xu J., Dallas P.B., Lyons P.A., Shellam G.R., Scalzo A.A.;
RT "Identification of the glycoprotein H gene of murine cytomegalovirus.";
RL J. Gen. Virol. 73:1849-1854(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8971012; DOI=10.1128/jvi.70.12.8833-8849.1996;
RA Rawlinson W.D., Farrell H.E., Barrell B.G.;
RT "Analysis of the complete DNA sequence of murine cytomegalovirus.";
RL J. Virol. 70:8833-8849(1996).
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; L18782; AAA20190.1; -; Unassigned_DNA.
DR EMBL; D10089; BAA00984.1; -; Genomic_DNA.
DR EMBL; U68299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JQ1622; JQ1622.
DR SMR; P30673; -.
DR Proteomes; UP000008774; Genome.
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;
KW Reference proteome; Sialic acid; Signal; Transmembrane;
KW 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..725
FT /note="Envelope glycoprotein H"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT /id="PRO_0000436661"
FT TOPO_DOM 20..700
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TRANSMEM 701..721
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TOPO_DOM 722..725
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT REGION 184..247
FT /note="Interaction with gL"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 621
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CONFLICT 321
FT /note="T -> S (in Ref. 2; BAA00984)"
FT /evidence="ECO:0000305"
FT CONFLICT 367..370
FT /note="LTEK -> IAAN (in Ref. 2; BAA00984)"
FT /evidence="ECO:0000305"
FT CONFLICT 374..379
FT /note="AHSSNA -> TKPSNS (in Ref. 2; BAA00984)"
FT /evidence="ECO:0000305"
FT CONFLICT 517..528
FT /note="ALMESAHRPERR -> GPDGVGAPSGET (in Ref. 2; BAA00984)"
FT /evidence="ECO:0000305"
FT CONFLICT 602..613
FT /note="SPCVLSRSYRER -> APASCRGATAN (in Ref. 2; BAA00984)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="E -> D (in Ref. 2; BAA00984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 725 AA; 81314 MW; D3907BB532125D0D CRC64;
MKLSLILSIA LCSTRVVYAA GAEAPRISRN TVKLHSYNES RVCRHDESSN QTVSHAAMFT
FNFQDGDGYR VYQVPRCLFN THAAREVLSS VDMTETLESY RKRFRVYFVV PIYGAYRLVA
RSPTAKYPGG VLNPPPASSV TMQDLIVDAT NIHTVVPDKL CVITEHPVIF SMKVPCSHQV
ITWTGYTVTV SLAQKFFVLT IKPTRDHTSE NTLAMFFGDV REVDLKAPYT VGAFLLRQTP
DHDLLVVVKQ TAFIQRYMFL TDVVFLQRTL SADYADTSVC LRVLSVLASV VARGKQCGLI
TRDTVEFFFT YSLCQLMANG TRYQSTAPVS TALWRQSELE LFGEFIRHCF KTTTPNPTPA
FQTRMQLTEK HKPAHSSNAI DVRVLAATYS SGMHAASMAD LAFLLRSTRI PPNVNTDALL
QKLLFTTDAY YRMSLKIPLS GSMRRILIRV DLTVRTQLNE SSVARRHFVL LTSMCSPREQ
ISWGELLMNP QRGAPSEIYS PCVSGGRRDY TGPSVRALME SAHRPERRAE QVMSVTEALR
PKRSQMSDEA NCVPDSTQGA VITANEKTYL ISSDFIVKGL AIPVSNTVVD RNLMITVLDR
RSPCVLSRSY RERGSVIVMN NITFTERCEF CASTLVEYDE VDGLTSIMHI PSIEVLKYLT
DPENDILVAT PRVHYLLLTA NGTVFEVTDI LVNVRPSMPY SVVVALVIIA ILMALGLYRL
CRQKR
