ID   X2FCN7_CHV16            Unreviewed;        95 AA.
AC   X2FCN7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   05-JUN-2019, entry version 12.
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; Herpesvirales; Herpesviridae; Alphaherpesvirinae;
OC   Simplexvirus.
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
CC       of tegument proteins and capsids during the assembly and egress
CC       processes. Participates also in viral entry at the fusion step
CC       probably by regulating the core fusion machinery.
CC       {ECO:0000256|HAMAP-Rule:MF_04040}.
CC   -!- SUBUNIT: Interacts with cytoplasmic envelopment protein 2; this
CC       interaction is essential for the proper localization of each
CC       protein to the assembly complex and thus for the production of
CC       infectious virus. {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
CC       {ECO:0000256|HAMAP-Rule:MF_04040}; Cytoplasmic side
CC       {ECO:0000256|HAMAP-Rule:MF_04040}. Host Golgi apparatus membrane
CC       {ECO:0000256|HAMAP-Rule:MF_04040}; Lipid-anchor
CC       {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.
CC       During virion morphogenesis, this protein probably accumulates in
CC       the endosomes and trans-Golgi where secondary envelopment occurs.
CC       It is probably transported to the cell surface from where it is
CC       endocytosed and directed to the trans-Golgi network (TGN).
CC       {ECO:0000256|HAMAP-Rule:MF_04040}.
CC   -!- PTM: Myristoylation and palmitoylation (probably on one or more of
CC       the nearby cysteines at the N-terminus) enable membrane-binding
CC       and Golgi apparatus-specific targeting and are essential for
CC       efficient packaging. {ECO:0000256|HAMAP-Rule:MF_04040}.
CC   -!- PTM: Phosphorylated. Phosphorylation does not seem to be required
CC       for recycling to the host Golgi apparatus. Packaging is selective
CC       for 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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: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_simplexvir-type.
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|HAMAP-Rule:MF_04040};
KW   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|HAMAP-Rule:MF_04040};
KW   Virion {ECO:0000256|HAMAP-Rule:MF_04040};
KW   Virion tegument {ECO:0000256|HAMAP-Rule:MF_04040}.
FT   INIT_MET      1      1       Removed; by host. {ECO:0000256|HAMAP-
FT                                Rule:MF_04040}.
FT   REGION       37     43       Asp/Glu-rich (acidic).
FT                                {ECO:0000256|HAMAP-Rule:MF_04040}.
FT   REGION       56     95       Disordered. {ECO:0000256|MobiDB-lite:
FT                                X2FCN7}.
FT   MOTIF        18     19       Di-leucine-like internalization motif.
FT                                {ECO:0000256|HAMAP-Rule:MF_04040}.
FT   COMPBIAS     68     82       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                X2FCN7}.
FT   MOD_RES      40     40       Phosphoserine. {ECO:0000256|HAMAP-Rule:
FT                                MF_04040}.
FT   LIPID         2      2       N-myristoyl glycine; by host.
FT                                {ECO:0000256|HAMAP-Rule:MF_04040}.
SQ   SEQUENCE   95 AA;  10316 MW;  BB96234388837752 CRC64;
     MGLTGSRVGP CCCRRNVLVT DRGETVSLTA NEFDAVELES DAGGNFYISP ELRVVTQPPA
     QAPHPRGPPS RGDRHWSRGG RHPDHISYPT PPAVR
//