GH_GPCMV
ID GH_GPCMV Reviewed; 723 AA.
AC P87730; E9RH81;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 25-MAY-2022, entry version 81.
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=UL75;
OS Guinea pig cytomegalovirus (strain 22122) (GPCMV).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Quwivirus.
OX NCBI_TaxID=103920;
OH NCBI_TaxID=10141; Cavia porcellus (Guinea pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9526546; DOI=10.1007/bf01718640;
RA Brady R.C., Schleiss M.R.;
RT "Identification and characterization of the guinea-pig cytomegalovirus
RT glycoprotein H gene.";
RL Arch. Virol. 141:2409-2424(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RX PubMed=19014498; DOI=10.1186/1743-422x-5-139;
RA Schleiss M.R., McGregor A., Choi K.Y., Date S.V., Cui X., McVoy M.A.;
RT "Analysis of the nucleotide sequence of the guinea pig cytomegalovirus
RT (GPCMV) genome.";
RL Virol. J. 5:139-139(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22122/ATCC-P5;
RX PubMed=21270288; DOI=10.1099/vir.0.027789-0;
RA Kanai K., Yamada S., Yamamoto Y., Fukui Y., Kurane I., Inoue N.;
RT "Re-evaluation of the genome sequence of guinea pig cytomegalovirus.";
RL J. Gen. Virol. 92:1005-1020(2011).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22122;
RX PubMed=23516193; DOI=10.1128/genomea.00054-13;
RA Yang D., Tamburro K., Dittmer D., Cui X., McVoy M.A.,
RA Hernandez-Alvarado N., Schleiss M.R.;
RT "Complete genome sequence of pathogenic Guinea pig cytomegalovirus from
RT salivary gland homogenates of infected animals.";
RL Genome Announc. 1:E0005413-E0005413(2013).
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; KC503762; AGE11545.1; -; Genomic_DNA.
DR EMBL; AB592928; BAJ78533.1; -; Genomic_DNA.
DR RefSeq; YP_007417841.1; NC_020231.1.
DR SMR; P87730; -.
DR PRIDE; P87730; -.
DR GeneID; 14536668; -.
DR KEGG; vg:14536668; -.
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..23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CHAIN 24..723
FT /note="Envelope glycoprotein H"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT /id="PRO_0000038254"
FT TOPO_DOM 24..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..723
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT REGION 197..263
FT /note="Interaction with gL"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 543
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"
SQ SEQUENCE 723 AA; 81772 MW; E6F80077767F46C9 CRC64;
MSPATRFTVI SCLVVSLITP SETSSWFDPF IEWARSSPNM TCVNNRTGTR SLATEGLISF
NFYEASRTVR TYQVPKCIFM SSVSKTIMQG VDLFESLESY RRRYYSYIIV PVHASFQIFI
HDLRTDLSSP TEELTSPVDK TLPNVTIWHT PSGYVIRLLD VVTPRFEECT LFPNHTVIFD
MTVPCSQEVY LRQTGKHQFA IVLTFTPSFF VLNIQTAQHQ HVTENDEDVI LIFGDVRSID
VKAPYSKPVL TLRQSYRDDL LIVAKTSIVN ATYPFIKTQD FLKGTLSGNY LDFNHVYTEF
NRLVIHNLVE GLCDAPPDDR TVSMVFSYAV LARTLYHTSN VTARLEDVAL RYVRLTLART
FLQQCFDVGP RYMRFPTIDG ALSVLLKLIR NSRDVDGGLK LSLTFALIFG NNTDMTKERD
LENALYEMKS IHRAGLVSPL SPRQRSLLYM MAYVTHHTTA FPDIRREMLA MQTSLCSPQE
LYNWAPHVSS AGLTMQEMFT PCSGSGRRDY SEARIAEIVQ LNPLTTKTPA DLYRILAHFD
RSNLTNFPAL SCISHLSGYV AVTLRDVTYV VSSNVMLKGT SYPVTNLAVD KTMIVTVSPA
QHPCEKTEVA HATRSIPIVK NITIGNDCEY CKSAIMEYDE VNGLSNIVYL ADTADLVLVT
NLDNRILASS PRTRYIMMTA NGTLMEITSV IIDIRQTSIF MIMLYCSLGV LLLYGLYRLL
HMI
