Database: UniProt
Entry: A0A0B5D3K5_9GAMA
LinkDB: A0A0B5D3K5_9GAMA
Original site: A0A0B5D3K5_9GAMA 
ID   A0A0B5D3K5_9GAMA        Unreviewed;        70 AA.
AC   A0A0B5D3K5;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   07-OCT-2020, entry version 14.
DE   RecName: Full=Cytoplasmic envelopment protein 3 {ECO:0000256|HAMAP-Rule:MF_04042};
GN   Name=ORF38 {ECO:0000313|EMBL:AJE29681.1};
OS   Macaca nemestrina rhadinovirus 2.
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus;
OC   Macacine gammaherpesvirus 12.
OX   NCBI_TaxID=123630 {ECO:0000313|EMBL:AJE29681.1, ECO:0000313|Proteomes:UP000297089};
RN   [1] {ECO:0000313|EMBL:AJE29681.1, ECO:0000313|Proteomes:UP000297089}
RC   STRAIN=J97167 {ECO:0000313|EMBL:AJE29681.1,
RC   ECO:0000313|Proteomes:UP000297089};
RA   Rose T.M., Bruce A.G.;
RT   "Complete genome sequence of MneRV2, the pig-tailed macaque RV2
RT   rhadinovirus, and evolutionary relationship with rhesus macaque RRV and
RT   human herpesvirus 8/KSHV.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC       Rule:MF_04042}.
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:0000256|HAMAP-Rule:MF_04042}.
CC   -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000256|HAMAP-
CC       Rule:MF_04042}. Virion membrane {ECO:0000256|HAMAP-Rule:MF_04042};
CC       Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_04042}. Host cell membrane
CC       {ECO:0000256|HAMAP-Rule:MF_04042}; Lipid-anchor {ECO:0000256|HAMAP-
CC       Rule:MF_04042}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_04042}.
CC       Host Golgi apparatus membrane {ECO:0000256|HAMAP-Rule:MF_04042}; Lipid-
CC       anchor {ECO:0000256|HAMAP-Rule:MF_04042}; Cytoplasmic side
CC       {ECO:0000256|HAMAP-Rule:MF_04042}. 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:0000256|HAMAP-
CC       Rule:MF_04042}.
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:0000256|HAMAP-Rule:MF_04042}.
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:0000256|HAMAP-Rule:MF_04042}.
CC   -!- SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment
CC       protein 3 family. {ECO:0000256|HAMAP-Rule:MF_04042}.
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DR   EMBL; KP265674; AJE29681.1; -; Genomic_DNA.
DR   Proteomes; UP000297089; 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: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_04042; HSV_CEP3_gammahv; 1.
DR   InterPro; IPR024360; Herpesvirus_UL11_homo.
DR   Pfam; PF10813; DUF2733; 1.
PE   3: Inferred from homology;
KW   Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04042};
KW   Host Golgi apparatus {ECO:0000256|ARBA:ARBA00022812, ECO:0000256|HAMAP-
KW   Rule:MF_04042}; Host membrane {ECO:0000256|HAMAP-Rule:MF_04042};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW   Rule:MF_04042};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_04042};
KW   Myristate {ECO:0000256|ARBA:ARBA00022707, ECO:0000256|HAMAP-Rule:MF_04042};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_04042};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW   Rule:MF_04042}; Reference proteome {ECO:0000313|Proteomes:UP000297089};
KW   Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04042};
KW   Virion tegument {ECO:0000256|ARBA:ARBA00022580, ECO:0000256|HAMAP-
KW   Rule:MF_04042}.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04042"
FT   REGION          49..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04042"
SQ   SEQUENCE   70 AA;  7895 MW;  570FC25EBC4513F1 CRC64;
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