CEP3_HCMVM
ID CEP3_HCMVM Reviewed; 190 AA.
AC F5HI87;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 29-SEP-2021, entry version 25.
DE RecName: Full=Cytoplasmic envelopment protein 3 {ECO:0000255|HAMAP-Rule:MF_04041};
DE AltName: Full=28 kDa structural phosphoprotein;
DE AltName: Full=pp28;
GN Name=UL99;
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).
CC -!- FUNCTION: Plays an important role in the cytoplasmic envelopment of
CC tegument proteins and capsids during the assembly and egress processes.
CC Participates also in viral entry at the fusion step probably by
CC regulating the core fusion machinery. {ECO:0000255|HAMAP-
CC Rule:MF_04041}.
CC -!- SUBUNIT: Interacts with cytoplasmic envelopment protein 2; this
CC interaction is essential for the proper localization of each protein to
CC the assembly complex and thus for the production of infectious virus.
CC {ECO:0000255|HAMAP-Rule:MF_04041}.
CC -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000255|HAMAP-
CC Rule:MF_04041}. Virion membrane {ECO:0000255|HAMAP-Rule:MF_04041};
CC Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04041}. Host cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04041}; Lipid-anchor {ECO:0000255|HAMAP-
CC Rule:MF_04041}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04041}.
CC Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04041}; Lipid-
CC anchor {ECO:0000255|HAMAP-Rule:MF_04041}; Cytoplasmic side
CC {ECO:0000255|HAMAP-Rule:MF_04041}. Note=Virion membrane-associated
CC tegument protein. Associates with host membrane lipids rafts. 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_04041}.
CC -!- PTM: Myristoylation and palmitoylation (probably on one or more of the
CC nearby cysteines at the N-terminus) enable membrane-binding and Golgi
CC apparatus-specific targeting and are essential for efficient packaging.
CC {ECO:0000255|HAMAP-Rule:MF_04041}.
CC -!- PTM: Phosphorylated. Phosphorylation does not seem to be required for
CC recycling to the host Golgi apparatus. Packaging is selective for
CC underphosphorylated forms. {ECO:0000255|HAMAP-Rule:MF_04041}.
CC -!- SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment
CC protein 3 family. {ECO:0000255|HAMAP-Rule:MF_04041}.
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DR EMBL; AY446894; AAR31650.1; -; Genomic_DNA.
DR RefSeq; YP_081546.1; NC_006273.2.
DR PRIDE; F5HI87; -.
DR DNASU; 3077533; -.
DR GeneID; 3077533; -.
DR KEGG; vg:3077533; -.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Proteomes; UP000000938; Genome.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0072517; C:host cell viral assembly compartment; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019033; C:viral tegument; TAS:Reactome.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046760; P:viral budding from Golgi membrane; IDA:UniProtKB.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IDA:UniProtKB.
DR HAMAP; MF_04041; HSV_CEP3_betahv; 1.
DR InterPro; IPR034705; HSV_CEP3_betahv.
PE 3: Inferred from homology;
KW Host cell membrane; Host Golgi apparatus; Host membrane; Lipoprotein;
KW Membrane; Myristate; Palmitate; Phosphoprotein; Reference proteome; Virion;
KW Virion tegument.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04041"
FT CHAIN 2..190
FT /note="Cytoplasmic envelopment protein 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04041"
FT /id="PRO_0000418277"
FT REGION 14..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..57
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..122
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04041"
SQ SEQUENCE 190 AA; 20923 MW; 7FBD4803A6DA4471 CRC64;
MGAELCKRIC CEFGTTSGEP LKDALGRQVS LRSYDNIPPT SSSDEGEDDD DGEDDDNEER
QQKLRLCGSG CGGNDSSSGS HREATHDGPK KNAVRSTFRE DKAPKPSKQS KKKKKPSKHH
HHQQSSIMQE TDDLDEEDTS IYLSPPPVPP VQVVAKRLPR PDTPRTPRQK KISQRPPTPG
TKKPAASLPF
