CEP3_HCMVA
ID CEP3_HCMVA Reviewed; 190 AA.
AC P13200; Q7M6J2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Cytoplasmic envelopment protein 3 {ECO:0000255|HAMAP-Rule:MF_04041};
GN Name=UL99;
OS Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PHOSPHORYLATION.
RX PubMed=2836608; DOI=10.1128/jvi.62.7.2243-2250.1988;
RA Meyer H., Bankier A.T., Landini M.P., Brown C.M., Barrell B.G., Rueger B.,
RA Mach M.;
RT "Identification and procaryotic expression of the gene coding for the
RT highly immunogenic 28-kilodalton structural phosphoprotein (pp28) of human
RT cytomegalovirus.";
RL J. Virol. 62:2243-2250(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [3]
RP GENOME REANNOTATION.
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [4]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
RN [5]
RP FUNCTION.
RX PubMed=12970444; DOI=10.1128/jvi.77.19.10594-10605.2003;
RA Silva M.C., Yu Q.-C., Enquist L., Shenk T.;
RT "Human cytomegalovirus UL99-encoded pp28 is required for the cytoplasmic
RT envelopment of tegument-associated capsids.";
RL J. Virol. 77:10594-10605(2003).
RN [6]
RP FUNCTION, AND MYRISTOYLATION AT GLY-2.
RX PubMed=14722304; DOI=10.1128/jvi.78.3.1488-1502.2004;
RA Jones T.R., Lee S.-W.;
RT "An acidic cluster of human cytomegalovirus UL99 tegument protein is
RT required for trafficking and function.";
RL J. Virol. 78:1488-1502(2004).
RN [7]
RP FUNCTION, AND INTERACTION WITH UL94.
RX PubMed=22761384; DOI=10.1128/jvi.01078-12;
RA Phillips S.L., Cygnar D., Thomas A., Bresnahan W.A.;
RT "Interaction between the human cytomegalovirus tegument proteins UL94 and
RT UL99 is essential for virus replication.";
RL J. Virol. 86:9995-10005(2012).
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-Rule:MF_04041,
CC ECO:0000269|PubMed:12970444, ECO:0000269|PubMed:14722304,
CC ECO:0000269|PubMed:22761384}.
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, ECO:0000269|PubMed:22761384}.
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, ECO:0000269|PubMed:14722304}.
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; X17403; CAA35335.1; -; Genomic_DNA.
DR EMBL; M21013; AAA45985.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00196.1; -; Genomic_DNA.
DR PIR; A28842; WMBE28.
DR iPTMnet; P13200; -.
DR PRIDE; P13200; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; 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:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046760; P:viral budding from Golgi membrane; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04041; HSV_CEP3_betahv; 1.
DR InterPro; IPR034705; HSV_CEP3_betahv.
PE 1: Evidence at protein level;
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_0000115342"
FT REGION 27..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,
FT ECO:0000269|PubMed:14722304"
SQ SEQUENCE 190 AA; 20923 MW; A08CC061D2B4B792 CRC64;
MGAELCKRIC CEFGTTPGEP LKDALGRQVS LRSYDNIPPT SSSDEGEDDD DGEDDDNEER
QQKLRLCGSG CGGNDSSSGS HREATHDGSK KNAVRSTFRE DKAPKPSKQS KKKKKPSKHH
HHQQSSIMQE TDDLDEEDTS IYLSPPPVPP VQVVAKRLPR PDTPRTPRQK KISQRPPTPG
TKKPAASLPF
