CEP3_HHV2H
ID CEP3_HHV2H Reviewed; 96 AA.
AC P13294; P89434;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Cytoplasmic envelopment protein 3 {ECO:0000255|HAMAP-Rule:MF_04040};
GN ORFNames=UL11;
OS Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10315;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT "The genome sequence of herpes simplex virus type 2.";
RL J. Virol. 72:2010-2021(1998).
RN [3]
RP INTERACTION WITH UL56, SUBCELLULAR LOCATION, MUTAGENESIS OF 11-CYS--CYS-13,
RP PALMITOYLATION, AND MUTAGENESIS OF GLY-2.
RC STRAIN=186;
RX PubMed=16604447; DOI=10.1007/s11262-005-6871-7;
RA Koshizuka T., Kawaguchi Y., Goshima F., Mori I., Nishiyama Y.;
RT "Association of two membrane proteins encoded by herpes simplex virus type
RT 2, UL11 and UL56.";
RL Virus Genes 32:153-163(2006).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=17694428; DOI=10.1007/s11262-007-0156-2;
RA Koshizuka T., Kawaguchi Y., Nozawa N., Mori I., Nishiyama Y.;
RT "Herpes simplex virus protein UL11 but not UL51 is associated with lipid
RT rafts.";
RL Virus Genes 35:571-575(2007).
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:16604447}.
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, ECO:0000269|PubMed:17694428}; Lipid-
CC anchor {ECO:0000255|HAMAP-Rule:MF_04040}; Cytoplasmic side
CC {ECO:0000255|HAMAP-Rule:MF_04040, ECO:0000269|PubMed:17694428}. Host
CC Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04040,
CC ECO:0000269|PubMed:16604447}; Lipid-anchor {ECO:0000255|HAMAP-
CC Rule:MF_04040}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04040,
CC ECO:0000269|PubMed:17694428}. Note=Virion membrane-associated tegument
CC protein. Associates with host membrane lipids rafts. During virion
CC morphogenesis, this protein probably accumulates in the endosomes and
CC trans-Golgi where secondary envelopment occurs. It is probably
CC transported to the cell surface from where it is endocytosed and
CC 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, ECO:0000305|PubMed:16604447}.
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; M11854; AAA45836.1; -; Genomic_DNA.
DR EMBL; Z86099; CAB06771.1; -; Genomic_DNA.
DR RefSeq; YP_009137162.1; NC_001798.2.
DR PRIDE; P13294; -.
DR DNASU; 24271454; -.
DR GeneID; 24271454; -.
DR KEGG; vg:24271454; -.
DR Proteomes; UP000001874; 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: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; Reference proteome; Virion;
KW 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_0000115926"
FT REGION 37..43
FT /note="Asp/Glu-rich (acidic)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04040"
FT REGION 50..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000255|HAMAP-Rule:MF_04040"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04040"
FT MUTAGEN 2
FT /note="G->A: Complete loss of myristoylation and almost
FT complete loss of interaction with UL56."
FT /evidence="ECO:0000269|PubMed:16604447"
FT MUTAGEN 11..13
FT /note="CCC->AAA: Complete loss of palmitoylation and almost
FT complete loss of interaction with UL56."
FT /evidence="ECO:0000269|PubMed:16604447"
FT MUTAGEN 11..13
FT /note="CCC->SSS: Complete loss of palmitoylation and almost
FT complete loss of interaction with UL56."
FT /evidence="ECO:0000269|PubMed:16604447"
FT CONFLICT 66
FT /note="P -> A (in Ref. 2; CAB06771)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 96 AA; 10556 MW; 8ECB31EE11EF423F CRC64;
MGLAFSGARP CCCRHNVITT DGGEVVSLTA HEFDVVDIES EEEGNFYVPP DVRVVTRAPG
PQYRRPSDPP SRHTRRRDPD VARPPATLTP PLSDSE
