ID   X2FCN7_CHV16            Unreviewed;        95 AA.
AC   X2FCN7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Cytoplasmic envelopment protein 3 {ECO:0000256|HAMAP-Rule:MF_04040};
GN   Name=UL11 {ECO:0000313|EMBL:AHM96059.1};
OS   Cercopithecine herpesvirus 16 (CeHV-16) (Herpesvirus papio 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC   Simplexvirus papiinealpha2.
OX   NCBI_TaxID=340907 {ECO:0000313|EMBL:AHM96059.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9541; Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OH   NCBI_TaxID=90387; Macaca leonina (Northern pig-tailed macaque) (Macaca nemestrina leonina).
OH   NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
OH   NCBI_TaxID=9545; Macaca nemestrina (Pig-tailed macaque).
RN   [1] {ECO:0000313|EMBL:AHM96059.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OU1-76 {ECO:0000313|EMBL:AHM96059.1};
RX   PubMed=24606686; DOI=10.1016/j.virol.2013.12.038;
RA   Black D., Ohsawa K., Tyler S., Maxwell L., Eberle R.;
RT   "A single viral gene determines lethal cross-species neurovirulence of
RT   baboon herpesvirus HVP2.";
RL   Virology 452-453:86-94(2014).
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_04040}.
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_04040}.
CC   -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000256|HAMAP-
CC       Rule:MF_04040}. Virion membrane {ECO:0000256|HAMAP-Rule:MF_04040};
CC       Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_04040}. Host cell membrane
CC       {ECO:0000256|HAMAP-Rule:MF_04040}; Lipid-anchor {ECO:0000256|HAMAP-
CC       Rule:MF_04040}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_04040}.
CC       Host Golgi apparatus membrane {ECO:0000256|HAMAP-Rule:MF_04040}; Lipid-
CC       anchor {ECO:0000256|HAMAP-Rule:MF_04040}; Cytoplasmic side
CC       {ECO:0000256|HAMAP-Rule:MF_04040}. 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_04040}.
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_04040}.
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_04040}.
CC   -!- SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment
CC       protein 3 family. {ECO:0000256|HAMAP-Rule:MF_04040}.
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DR   EMBL; KF908240; AHM96059.1; -; Genomic_DNA.
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:0009653; P:anatomical structure morphogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0046760; P:viral budding from Golgi membrane; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04040; HSV_CEP3_alphahv; 1.
DR   InterPro; IPR024351; Tegument_UL11_Herpesvir.
DR   InterPro; IPR016395; UL11_simplexvirus.
DR   Pfam; PF11094; UL11; 1.
DR   PIRSF; PIRSF003496; Myristoylat_tegument_UL11; 1.
PE   3: Inferred from homology;
KW   Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04040};
KW   Host Golgi apparatus {ECO:0000256|ARBA:ARBA00022812, ECO:0000256|HAMAP-
KW   Rule:MF_04040}; Host membrane {ECO:0000256|HAMAP-Rule:MF_04040};
KW   Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04040};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_04040};
KW   Myristate {ECO:0000256|HAMAP-Rule:MF_04040};
KW   Palmitate {ECO:0000256|HAMAP-Rule:MF_04040};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW   Rule:MF_04040}; Virion {ECO:0000256|HAMAP-Rule:MF_04040};
KW   Virion tegument {ECO:0000256|ARBA:ARBA00022580, ECO:0000256|HAMAP-
KW   Rule:MF_04040}.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04040"
FT   REGION          37..43
FT                   /note="Asp/Glu-rich (acidic)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04040"
FT   REGION          56..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           18..19
FT                   /note="Di-leucine-like internalization motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04040"
FT   COMPBIAS        68..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         40
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04040"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04040"
SQ   SEQUENCE   95 AA;  10316 MW;  BB96234388837752 CRC64;
     MGLTGSRVGP CCCRRNVLVT DRGETVSLTA NEFDAVELES DAGGNFYISP ELRVVTQPPA
     QAPHPRGPPS RGDRHWSRGG RHPDHISYPT PPAVR
//