CEP3_HHV11
ID CEP3_HHV11 Reviewed; 96 AA.
AC P04289; B9VQD8; Q09IC2;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Cytoplasmic envelopment protein 3 {ECO:0000255|HAMAP-Rule:MF_04040};
GN ORFNames=UL11;
OS Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10299;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3010237; DOI=10.1093/nar/14.8.3435;
RA McGeoch D.J., Dolan A., Frame M.C.;
RT "DNA sequence of the region in the genome of herpes simplex virus type 1
RT containing the exonuclease gene and neighbouring genes.";
RL Nucleic Acids Res. 14:3435-3448(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA Perry L.J., Scott J.E., Taylor P.;
RT "The complete DNA sequence of the long unique region in the genome of
RT herpes simplex virus type 1.";
RL J. Gen. Virol. 69:1531-1574(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nonneuroinvasive mutant HF10;
RX PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
RA Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
RT "Determination and analysis of the DNA sequence of highly attenuated herpes
RT simplex virus type 1 mutant HF10, a potential oncolytic virus.";
RL Microbes Infect. 9:142-149(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17 syn+;
RA Cunningham C., Davison A.J.;
RT "Herpes simplex virus type 1 bacterial artificial chromosome.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP MYRISTOYLATION AT GLY-2, AND SUBCELLULAR LOCATION.
RX PubMed=1312117; DOI=10.1099/0022-1317-73-3-539;
RA MacLean C.A., Dolan A., Jamieson F.E., McGeoch D.J.;
RT "The myristylated virion proteins of herpes simplex virus type 1:
RT investigation of their role in the virus life cycle.";
RL J. Gen. Virol. 73:539-547(1992).
RN [6]
RP FUNCTION.
RX PubMed=1321297; DOI=10.1128/jvi.66.8.5168-5174.1992;
RA Baines J.D., Roizman B.;
RT "The UL11 gene of herpes simplex virus 1 encodes a function that
RT facilitates nucleocapsid envelopment and egress from cells.";
RL J. Virol. 66:5168-5174(1992).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=10954570; DOI=10.1128/jvi.74.18.8692-8699.2000;
RA Bowzard J.B., Visalli R.J., Wilson C.B., Loomis J.S., Callahan E.M.,
RA Courtney R.J., Wills J.W.;
RT "Membrane targeting properties of a herpesvirus tegument protein-retrovirus
RT Gag chimera.";
RL J. Virol. 74:8692-8699(2000).
RN [8]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-40, DI-LEUCINE-LIKE
RP INTERNALIZATION MOTIF, AND ACIDIC REGION.
RX PubMed=11711612; DOI=10.1128/jvi.75.24.12209-12219.2001;
RA Loomis J.S., Bowzard J.B., Courtney R.J., Wills J.W.;
RT "Intracellular trafficking of the UL11 tegument protein of herpes simplex
RT virus type 1.";
RL J. Virol. 75:12209-12219(2001).
RN [9]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=16928743; DOI=10.1128/jvi.01172-06;
RA Loomis J.S., Courtney R.J., Wills J.W.;
RT "Packaging determinants in the UL11 tegument protein of herpes simplex
RT virus type 1.";
RL J. Virol. 80:10534-10541(2006).
RN [10]
RP INTERACTION WITH GLYCOPROTEIN D AND GLYCOPROTEIN E.
RC STRAIN=F;
RX PubMed=17035313; DOI=10.1128/jvi.01842-06;
RA Farnsworth A., Wisner T.W., Johnson D.C.;
RT "Cytoplasmic residues of herpes simplex virus glycoprotein gE required for
RT secondary envelopment and binding of tegument proteins VP22 and UL11 to gE
RT and gD.";
RL J. Virol. 81:319-331(2007).
RN [11]
RP SUBCELLULAR LOCATION.
RC STRAIN=F;
RX PubMed=18596102; DOI=10.1128/jvi.00904-08;
RA Loret S., Guay G., Lippe R.;
RT "Comprehensive characterization of extracellular herpes simplex virus type
RT 1 virions.";
RL J. Virol. 82:8605-8618(2008).
RN [12]
RP FUNCTION.
RX PubMed=23150560; DOI=10.1073/pnas.1212900109;
RA Han J., Chadha P., Starkey J.L., Wills J.W.;
RT "Function of glycoprotein E of herpes simplex virus requires coordinated
RT assembly of three tegument proteins on its cytoplasmic tail.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:19798-19803(2012).
RN [13]
RP INTERACTION WITH UL16.
RX PubMed=22915809; DOI=10.1128/jvi.01879-12;
RA Chadha P., Han J., Starkey J.L., Wills J.W.;
RT "Regulated interaction of tegument proteins UL16 and UL11 from herpes
RT simplex virus.";
RL J. Virol. 86:11886-11898(2012).
RN [14]
RP FUNCTION.
RX PubMed=23678175; DOI=10.1128/jvi.01181-13;
RA Kim I.J., Chouljenko V.N., Walker J.D., Kousoulas K.G.;
RT "Herpes simplex virus 1 glycoprotein M and the membrane-associated protein
RT UL11 are required for virus-induced cell fusion and efficient virus
RT entry.";
RL J. Virol. 87:8029-8037(2013).
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-Rule:MF_04040,
CC ECO:0000269|PubMed:1321297, ECO:0000269|PubMed:16928743,
CC ECO:0000269|PubMed:23150560, ECO:0000269|PubMed:23678175}.
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:0000250|UniProtKB:P13294,
CC ECO:0000255|HAMAP-Rule:MF_04040, ECO:0000269|PubMed:17035313,
CC ECO:0000269|PubMed:22915809}.
CC -!- INTERACTION:
CC P04289; P10200: UL16; NbExp=3; IntAct=EBI-7044930, EBI-7044955;
CC -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000255|HAMAP-Rule:MF_04040,
CC ECO:0000269|PubMed:1312117, ECO:0000269|PubMed:18596102}. Virion
CC membrane {ECO:0000255|HAMAP-Rule:MF_04040}; Lipid-anchor
CC {ECO:0000255|HAMAP-Rule:MF_04040}. Host cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04040, ECO:0000269|PubMed:11711612}; Lipid-
CC anchor {ECO:0000255|HAMAP-Rule:MF_04040}; Cytoplasmic side
CC {ECO:0000255|HAMAP-Rule:MF_04040, ECO:0000269|PubMed:11711612}. Host
CC Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04040,
CC ECO:0000269|PubMed:10954570, ECO:0000269|PubMed:11711612}; Lipid-anchor
CC {ECO:0000255|HAMAP-Rule:MF_04040}; Cytoplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_04040, ECO:0000269|PubMed:11711612}. Note=Virion membrane-
CC associated tegument protein. Associates with host membrane lipids
CC rafts. During virion morphogenesis, this protein probably accumulates
CC in the endosomes and trans-Golgi where secondary envelopment occurs. It
CC is probably transported to the cell surface from where it is
CC endocytosed and directed to the trans-Golgi network (TGN).
CC {ECO:0000255|HAMAP-Rule:MF_04040}.
CC -!- DOMAIN: The acidic region is required for efficient packaging. It is
CC also involved in recycling the protein from the plasma membrane to the
CC Golgi apparatus, and in the interaction with the capsid-binding protein
CC UL16. {ECO:0000269|PubMed:16928743}.
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:0000269|PubMed:11711612,
CC ECO:0000269|PubMed:16928743}.
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 ECO:0000269|PubMed:16928743}.
CC -!- SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment
CC protein 3 family. {ECO:0000255|HAMAP-Rule:MF_04040}.
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DR EMBL; X14112; CAA32347.1; -; Genomic_DNA.
DR EMBL; X03839; CAA27452.1; -; Genomic_DNA.
DR EMBL; DQ889502; ABI63473.1; -; Genomic_DNA.
DR EMBL; FJ593289; ACM62233.1; -; Genomic_DNA.
DR PIR; A03737; WMBE11.
DR RefSeq; YP_009137085.1; NC_001806.2.
DR SASBDB; P04289; -.
DR IntAct; P04289; 1.
DR MINT; P04289; -.
DR iPTMnet; P04289; -.
DR PRIDE; P04289; -.
DR GeneID; 24271464; -.
DR KEGG; vg:24271464; -.
DR Proteomes; UP000009294; Genome.
DR Proteomes; UP000180652; 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; IDA:UniProtKB.
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_0000115925"
FT REGION 37..43
FT /note="Asp/Glu-rich (acidic)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04040"
FT REGION 44..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 ECO:0000269|PubMed:11711612"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04040,
FT ECO:0000269|PubMed:1312117"
FT VARIANT 39
FT /note="E -> K (in strain: 17 syn+)"
FT VARIANT 54
FT /note="G -> V (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 65
FT /note="R -> C (in strain: Nonneuroinvasive mutant HF10)"
SQ SEQUENCE 96 AA; 10487 MW; 5D09A5B1F2034B09 CRC64;
MGLSFSGARP CCCRNNVLIT DDGEVVSLTA HDFDVVDIES EEEGNFYVPP DMRGVTRAPG
RQRLRSSDPP SRHTHRRTPG GACPATQFPP PMSDSE
