CEP3_HHV1K
ID CEP3_HHV1K Reviewed; 96 AA.
AC Q68980;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Cytoplasmic envelopment protein 3 {ECO:0000255|HAMAP-Rule:MF_04040};
GN ORFNames=UL11;
OS Human herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10306;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3005609; DOI=10.1128/jvi.57.3.1023-1036.1986;
RA Draper K.G., Devi-Rao G., Costa R.H., Blair E.D., Thompson R.L.,
RA Wagner E.K.;
RT "Characterization of the genes encoding herpes simplex virus type 1 and
RT type 2 alkaline exonucleases and overlapping proteins.";
RL J. Virol. 57:1023-1036(1986).
RN [2]
RP INTERACTION WITH UL16.
RX PubMed=14557627; DOI=10.1128/jvi.77.21.11417-11424.2003;
RA Loomis J.S., Courtney R.J., Wills J.W.;
RT "Binding partners for the UL11 tegument protein of herpes simplex virus
RT type 1.";
RL J. Virol. 77:11417-11424(2003).
RN [3]
RP INTERACTION WITH UL16.
RX PubMed=18715918; DOI=10.1128/jvi.01230-08;
RA Yeh P.-C., Meckes D.G. Jr., Wills J.W.;
RT "Analysis of the interaction between the UL11 and UL16 tegument proteins of
RT herpes simplex virus.";
RL J. Virol. 82:10693-10700(2008).
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-
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 (By similarity). Interacts with gE (via C-terminus). Interacts with gD
CC (via C-terminus). Interacts with UL56. {ECO:0000255|HAMAP-
CC Rule:MF_04040, ECO:0000269|PubMed:14557627,
CC ECO:0000269|PubMed:18715918}.
CC -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000255|HAMAP-
CC Rule:MF_04040}. Virion membrane {ECO:0000255|HAMAP-Rule:MF_04040};
CC Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04040}. Host cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04040}; Lipid-anchor {ECO:0000255|HAMAP-
CC Rule:MF_04040}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04040}.
CC Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04040}; Lipid-
CC anchor {ECO:0000255|HAMAP-Rule:MF_04040}; Cytoplasmic side
CC {ECO:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_04040}.
CC -!- SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment
CC protein 3 family. {ECO:0000255|HAMAP-Rule:MF_04040}.
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DR EMBL; K02022; AAA45773.1; -; 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 1: Evidence at protein level;
KW Host cell membrane; Host Golgi apparatus; Host membrane; Lipoprotein;
KW Membrane; Myristate; Palmitate; Phosphoprotein; Virion; Virion tegument.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04040"
FT CHAIN 2..96
FT /note="Cytoplasmic envelopment protein 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04040"
FT /id="PRO_0000385489"
FT REGION 37..43
FT /note="Asp/Glu-rich (acidic)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04040"
FT REGION 57..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 18..19
FT /note="Di-leucine-like internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04040"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04040"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04040"
SQ SEQUENCE 96 AA; 10529 MW; 5D09B1F4E6464B09 CRC64;
MGLSFSGARP CCCRNNVLIT DDGEVVSLTA HDFDVVDIES EEEGNFYVPP DMRVVTRAPG
RQRLRSSDPP SRHTHRRTPG GACPATQFPP PMSDSE
