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Cytoplasmic envelopment protein 3

 CEP3_HHV11              Reviewed;          96 AA.
P04289; B9VQD8; Q09IC2;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
15-MAR-2017, entry version 91.
RecName: Full=Cytoplasmic envelopment protein 3 {ECO:0000255|HAMAP-Rule:MF_04040};
ORFNames=UL11;
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus
1).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Alphaherpesvirinae; Simplexvirus.
NCBI_TaxID=10299;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3010237; DOI=10.1093/nar/14.8.3435;
McGeoch D.J., Dolan A., Frame M.C.;
"DNA sequence of the region in the genome of herpes simplex virus type
1 containing the exonuclease gene and neighbouring genes.";
Nucleic Acids Res. 14:3435-3448(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C.,
McNab D., Perry L.J., Scott J.E., Taylor P.;
"The complete DNA sequence of the long unique region in the genome of
herpes simplex virus type 1.";
J. Gen. Virol. 69:1531-1574(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Nonneuroinvasive mutant HF10;
PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
"Determination and analysis of the DNA sequence of highly attenuated
herpes simplex virus type 1 mutant HF10, a potential oncolytic
virus.";
Microbes Infect. 9:142-149(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=17 syn+;
Cunningham C., Davison A.J.;
"Herpes simplex virus type 1 bacterial artificial chromosome.";
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[5]
MYRISTOYLATION AT GLY-2, AND SUBCELLULAR LOCATION.
PubMed=1312117; DOI=10.1099/0022-1317-73-3-539;
MacLean C.A., Dolan A., Jamieson F.E., McGeoch D.J.;
"The myristylated virion proteins of herpes simplex virus type 1:
investigation of their role in the virus life cycle.";
J. Gen. Virol. 73:539-547(1992).
[6]
FUNCTION.
PubMed=1321297;
Baines J.D., Roizman B.;
"The UL11 gene of herpes simplex virus 1 encodes a function that
facilitates nucleocapsid envelopment and egress from cells.";
J. Virol. 66:5168-5174(1992).
[7]
SUBCELLULAR LOCATION.
PubMed=10954570; DOI=10.1128/JVI.74.18.8692-8699.2000;
Bowzard J.B., Visalli R.J., Wilson C.B., Loomis J.S., Callahan E.M.,
Courtney R.J., Wills J.W.;
"Membrane targeting properties of a herpesvirus tegument protein-
retrovirus Gag chimera.";
J. Virol. 74:8692-8699(2000).
[8]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-40, DI-LEUCINE-LIKE
INTERNALIZATION MOTIF, AND ACIDIC REGION.
PubMed=11711612; DOI=10.1128/JVI.75.24.12209-12219.2001;
Loomis J.S., Bowzard J.B., Courtney R.J., Wills J.W.;
"Intracellular trafficking of the UL11 tegument protein of herpes
simplex virus type 1.";
J. Virol. 75:12209-12219(2001).
[9]
FUNCTION, AND PHOSPHORYLATION.
PubMed=16928743; DOI=10.1128/JVI.01172-06;
Loomis J.S., Courtney R.J., Wills J.W.;
"Packaging determinants in the UL11 tegument protein of herpes simplex
virus type 1.";
J. Virol. 80:10534-10541(2006).
[10]
INTERACTION WITH GLYCOPROTEIN D AND GLYCOPROTEIN E.
STRAIN=F;
PubMed=17035313; DOI=10.1128/JVI.01842-06;
Farnsworth A., Wisner T.W., Johnson D.C.;
"Cytoplasmic residues of herpes simplex virus glycoprotein gE required
for secondary envelopment and binding of tegument proteins VP22 and
UL11 to gE and gD.";
J. Virol. 81:319-331(2007).
[11]
SUBCELLULAR LOCATION.
STRAIN=F;
PubMed=18596102; DOI=10.1128/JVI.00904-08;
Loret S., Guay G., Lippe R.;
"Comprehensive characterization of extracellular herpes simplex virus
type 1 virions.";
J. Virol. 82:8605-8618(2008).
[12]
FUNCTION.
PubMed=23150560; DOI=10.1073/pnas.1212900109;
Han J., Chadha P., Starkey J.L., Wills J.W.;
"Function of glycoprotein E of herpes simplex virus requires
coordinated assembly of three tegument proteins on its cytoplasmic
tail.";
Proc. Natl. Acad. Sci. U.S.A. 109:19798-19803(2012).
[13]
INTERACTION WITH UL16.
PubMed=22915809; DOI=10.1128/JVI.01879-12;
Chadha P., Han J., Starkey J.L., Wills J.W.;
"Regulated interaction of tegument proteins UL16 and UL11 from herpes
simplex virus.";
J. Virol. 86:11886-11898(2012).
[14]
FUNCTION.
PubMed=23678175; DOI=10.1128/JVI.01181-13;
Kim I.J., Chouljenko V.N., Walker J.D., Kousoulas K.G.;
"Herpes simplex virus 1 glycoprotein M and the membrane-associated
protein UL11 are required for virus-induced cell fusion and efficient
virus entry.";
J. Virol. 87:8029-8037(2013).
-!- FUNCTION: Plays an important role in the cytoplasmic envelopment
of tegument proteins and capsids during the assembly and egress
processes. Participates also in viral entry at the fusion step
probably by regulating the core fusion machinery.
{ECO:0000255|HAMAP-Rule:MF_04040, ECO:0000269|PubMed:1321297,
ECO:0000269|PubMed:16928743, ECO:0000269|PubMed:23150560,
ECO:0000269|PubMed:23678175}.
-!- SUBUNIT: Interacts with cytoplasmic envelopment protein 2; this
interaction is essential for the proper localization of each
protein to the assembly complex and thus for the production of
infectious virus (By similarity). Interacts with gE (via C-
terminus). Interacts with gD (via C-terminus). Interacts with
UL56. {ECO:0000250|UniProtKB:P13294, ECO:0000255|HAMAP-
Rule:MF_04040, ECO:0000269|PubMed:17035313,
ECO:0000269|PubMed:22915809}.
-!- INTERACTION:
P10200:UL16; NbExp=3; IntAct=EBI-7044930, EBI-7044955;
-!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000255|HAMAP-
Rule:MF_04040, ECO:0000269|PubMed:1312117,
ECO:0000269|PubMed:18596102}. Virion membrane {ECO:0000255|HAMAP-
Rule:MF_04040}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04040}.
Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04040,
ECO:0000269|PubMed:11711612}; Lipid-anchor {ECO:0000255|HAMAP-
Rule:MF_04040}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04040,
ECO:0000269|PubMed:11711612}. Host Golgi apparatus membrane
{ECO:0000255|HAMAP-Rule:MF_04040, ECO:0000269|PubMed:10954570,
ECO:0000269|PubMed:11711612}; Lipid-anchor {ECO:0000255|HAMAP-
Rule:MF_04040}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04040,
ECO:0000269|PubMed:11711612}. Note=Virion membrane-associated
tegument protein. Associates with host membrane lipids rafts.
During virion morphogenesis, this protein probably accumulates in
the endosomes and trans-Golgi where secondary envelopment occurs.
It is probably transported to the cell surface from where it is
endocytosed and directed to the trans-Golgi network (TGN).
{ECO:0000255|HAMAP-Rule:MF_04040}.
-!- DOMAIN: The acidic region is required for efficient packaging. It
is also involved in recycling the protein from the plasma membrane
to the Golgi apparatus, and in the interaction with the capsid-
binding protein UL16. {ECO:0000269|PubMed:16928743}.
-!- PTM: Myristoylation and palmitoylation (probably on one or more of
the nearby cysteines at the N-terminus) enable membrane-binding
and Golgi apparatus-specific targeting and are essential for
efficient packaging. {ECO:0000255|HAMAP-Rule:MF_04040,
ECO:0000269|PubMed:11711612, ECO:0000269|PubMed:16928743}.
-!- PTM: Phosphorylated. Phosphorylation does not seem to be required
for recycling to the host Golgi apparatus. Packaging is selective
for underphosphorylated forms. {ECO:0000255|HAMAP-Rule:MF_04040,
ECO:0000269|PubMed:16928743}.
-!- SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment
protein 3 family. {ECO:0000255|HAMAP-Rule:MF_04040}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X14112; CAA32347.1; -; Genomic_DNA.
EMBL; X03839; CAA27452.1; -; Genomic_DNA.
EMBL; DQ889502; ABI63473.1; -; Genomic_DNA.
EMBL; FJ593289; ACM62233.1; -; Genomic_DNA.
PIR; A03737; WMBE11.
RefSeq; YP_009137085.1; NC_001806.2.
IntAct; P04289; 1.
MINT; MINT-6732677; -.
iPTMnet; P04289; -.
GeneID; 24271464; -.
KEGG; vg:24271464; -.
OrthoDB; VOG090002QO; -.
Proteomes; UP000009294; Genome.
Proteomes; UP000180652; Genome.
GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0009653; P:anatomical structure morphogenesis; IEA:InterPro.
GO; GO:0046760; P:viral budding from Golgi membrane; IDA:UniProtKB.
HAMAP; MF_04040; HSV_CEP3_alphahv; 1.
InterPro; IPR024351; Tegument_UL11_Herpesvir.
InterPro; IPR016395; UL11_simplexvir-type.
Pfam; PF11094; UL11; 1.
PIRSF; PIRSF003496; Myristoylat_tegument_UL11; 1.
1: Evidence at protein level;
Complete proteome; Host cell membrane; Host Golgi apparatus;
Host membrane; Lipoprotein; Membrane; Myristate; Palmitate;
Phosphoprotein; Reference proteome; Virion; Virion tegument.
INIT_MET 1 1 Removed; by host. {ECO:0000255|HAMAP-
Rule:MF_04040}.
CHAIN 2 96 Cytoplasmic envelopment protein 3.
{ECO:0000255|HAMAP-Rule:MF_04040}.
/FTId=PRO_0000115925.
REGION 37 43 Asp/Glu-rich (acidic).
{ECO:0000255|HAMAP-Rule:MF_04040}.
MOTIF 18 19 Di-leucine-like internalization motif.
{ECO:0000255|HAMAP-Rule:MF_04040}.
MOD_RES 40 40 Phosphoserine. {ECO:0000255|HAMAP-
Rule:MF_04040,
ECO:0000269|PubMed:11711612}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000255|HAMAP-Rule:MF_04040,
ECO:0000269|PubMed:1312117}.
VARIANT 39 39 E -> K (in strain: 17 syn+).
VARIANT 54 54 G -> V (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 65 65 R -> C (in strain: Nonneuroinvasive
mutant HF10).
SEQUENCE 96 AA; 10487 MW; 5D09A5B1F2034B09 CRC64;
MGLSFSGARP CCCRNNVLIT DDGEVVSLTA HDFDVVDIES EEEGNFYVPP DMRGVTRAPG
RQRLRSSDPP SRHTHRRTPG GACPATQFPP PMSDSE


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