GO_HCMVM
ID GO_HCMVM Reviewed; 472 AA.
AC F5HGP1;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 23-FEB-2022, entry version 27.
DE RecName: Full=Envelope glycoprotein O;
DE Flags: Precursor;
GN Name=UL74;
OS Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=295027;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT "Genetic content of wild-type human cytomegalovirus.";
RL J. Gen. Virol. 85:1301-1312(2004).
RN [2]
RP FUNCTION, AND INTERACTION WITH GL; GH AND HOST PDGFRA.
RX PubMed=28403202; DOI=10.1371/journal.ppat.1006281;
RA Wu Y., Prager A., Boos S., Resch M., Brizic I., Mach M., Wildner S.,
RA Scrivano L., Adler B.;
RT "Human cytomegalovirus glycoprotein complex gH/gL/gO uses PDGFR-alpha as a
RT key for entry.";
RL PLoS Pathog. 13:E1006281-E1006281(2017).
CC -!- FUNCTION: Plays a role in viral entry into host cells. Forms a trimeric
CC complex at the surface of the viral envelope together with gH and gL.
CC This complex is required for entry in host fibroblasts
CC (PubMed:28403202). Mechanistically, engages host receptor(s) including
CC PDGFRA to mediate infection (PubMed:28403202).
CC {ECO:0000269|PubMed:28403202}.
CC -!- SUBUNIT: Forms the envelope trimer complex composed of gH, gL, and gO.
CC The trimer interacts with host PDGFRA. {ECO:0000269|PubMed:28403202}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}. Note=Host membrane
CC associated, either via its interaction with gH, or as a type II
CC transmembrane protein. {ECO:0000305}.
CC -!- PTM: N-glycosylated.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the herpesviridae U47 family. {ECO:0000305}.
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DR EMBL; AY446894; AAR31626.1; -; Genomic_DNA.
DR RefSeq; YP_081522.1; NC_006273.2.
DR SMR; F5HGP1; -.
DR PRIDE; F5HGP1; -.
DR DNASU; 3077572; -.
DR GeneID; 3077572; -.
DR KEGG; vg:3077572; -.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Proteomes; UP000000938; Genome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0019031; C:viral envelope; TAS:Reactome.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IMP:CACAO.
DR InterPro; IPR012564; Herpes_UL74.
DR Pfam; PF07982; Herpes_UL74; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Reference proteome; Signal; Viral envelope protein;
KW Virion.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..472
FT /note="Envelope glycoprotein O"
FT /id="PRO_0000418232"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 472 AA; 54701 MW; 5C6291E5CC9F65E0 CRC64;
MGKKEMIMVK GIPKIMLLIS ITFLLLSLIN CNVLVNSRGT RRSWPYTVLS YRGKEILKKQ
KEDILKRLMS TSSDGYRFLM YPSQQKFHAI VISMDKFPQD YILAGPIRND SITHMWFDFY
STQLRKPAKY VYSEYNHTAH KITLRPPPCG TVPSMNCLSE MLNVSKRNDT GEKGCGNFTT
FNPMFFNVPR WNTKLYIGSN KVNVDSQTIY FLGLTALLLR YAQRNCTRSF YLVNAMSRNL
FRVPKYINGT KLKNTMRKLK RKQALVKEQP QKKNKKSQST TTPYLSYTTS TAFNVTTNVT
YSATAAVTRV ATSTTGYRPD SNFMKSIMAT QLRDLATWVY TTLRYRNEPF CKPDRNRTAV
SEFMKNTHVL IRNETPYTIY GTLDMSSLYY NETMSVENET ASDNNETTPT SPSTRFQRTF
IDPLWDYLDS LLFLDKIRNF SLQLPAYGNL TPPEHRRAAN LSTLNSLWWW SQ
