ID X2FCN7_CHV16 Unreviewed; 95 AA. AC X2FCN7; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 22-FEB-2023, entry version 21. 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; Herpesviridae; Alphaherpesvirinae; 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 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}. 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: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|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|ARBA:ARBA00022553, ECO:0000256|HAMAP- KW Rule:MF_04040}; KW Virion {ECO:0000256|ARBA:ARBA00022844, 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 //