ID   TG11_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   19-OCT-2011, entry version 72.
DE   RecName: Full=Tegument protein UL11;
GN   ORFNames=UL11;
OS   Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus
OS   1).
OC   Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
OC   Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10299;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=86205244; 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
RT   1 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   MEDLINE=88274327; PubMed=2839594;
RA   McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C.,
RA   McNab D., 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
RT   herpes simplex virus type 1 mutant HF10, a potential oncolytic
RT   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;
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   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
RT   for secondary envelopment and binding of tegument proteins VP22 and
RT   UL11 to gE and gD.";
RL   J. Virol. 81:319-331(2007).
RN   [7]
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
RT   type 1 virions.";
RL   J. Virol. 82:8605-8618(2008).
CC   -!- FUNCTION: Tegument protein that may play a role in the
CC       nucleocapsid secondary envelopment at the trans-Golgi network
CC       during virus morphogenesis (Potential).
CC   -!- SUBUNIT: Interacts with UL16. Interacts with gE (via C-terminus).
CC       Interacts with gD (via C-terminus). Interacts with UL56 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Virion tegument. Virion membrane; Lipid-
CC       anchor (By similarity). Host cell membrane; Lipid-anchor;
CC       Cytoplasmic side (By similarity). Host Golgi apparatus membrane;
CC       Lipid-anchor; Cytoplasmic side (By similarity). Host nucleus
CC       membrane; Lipid-anchor; Cytoplasmic side. Note=Virion membrane-
CC       associated tegument protein (about 700 copies per virion).
CC       Associates with host membrane lipids rafts (By similarity). During
CC       virion morphogenesis, this protein probably accumulates in the
CC       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) (By
CC       similarity).
CC   -!- DOMAIN: The acidic region is required for efficient packaging. It
CC       is also involved in recycling the protein from the plasma membrane
CC       to the Golgi apparatus, and in the interaction with the capsid-
CC       binding protein UL16 (By similarity).
CC   -!- PTM: Myristoylation and palmitoylation (probably on one or more of
CC       the nearby cysteines at the N-terminus) enable membrane-binding
CC       and Golgi apparatus-specific targeting and are essential for
CC       efficient packaging (By similarity).
CC   -!- PTM: Phosphorylated. Phosphorylation does not seem to be needed
CC       for UL11 recycling to the Golgi apparatus. Packaging is selective
CC       for underphosphorylated forms (By similarity).
CC   -!- SIMILARITY: Belongs to the herpesviridae HHV-1 UL11 family.
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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; NP_044612.1; NC_001806.1.
DR   MINT; MINT-6732677; -.
DR   GeneID; 2703380; -.
DR   ProtClustDB; PHA3356; -.
DR   GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044200; C:host cell nuclear 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:InterPro.
DR   InterPro; IPR024351; Tegument_UL11_Herpesvir.
DR   InterPro; IPR016395; UL11_simplexvir-type.
DR   Pfam; PF11094; UL11; 1.
DR   PIRSF; PIRSF003496; Myristoylat_tegument_UL11; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Host cell membrane; Host Golgi apparatus;
KW   Host membrane; Host nucleus; Lipoprotein; Membrane; Myristate;
KW   Palmitate; Phosphoprotein; Reference proteome; Virion;
KW   Virion tegument.
FT   INIT_MET      1      1       Removed; by host.
FT   CHAIN         2     96       Tegument protein UL11.
FT                                /FTId=PRO_0000115925.
FT   REGION       37     43       Asp/Glu-rich (acidic).
FT   MOTIF        18     19       Di-leucine-like internalization motif
FT                                (Potential).
FT   MOD_RES      40     40       Phosphoserine (By similarity).
FT   LIPID         2      2       N-myristoyl glycine; by host.
FT   VARIANT      39     39       E -> K (in strain: 17 syn+).
FT   VARIANT      54     54       G -> V (in strain: Nonneuroinvasive
FT                                mutant HF10).
FT   VARIANT      65     65       R -> C (in strain: Nonneuroinvasive
FT                                mutant HF10).
SQ   SEQUENCE   96 AA;  10487 MW;  5D09A5B1F2034B09 CRC64;
     MGLSFSGARP CCCRNNVLIT DDGEVVSLTA HDFDVVDIES EEEGNFYVPP DMRGVTRAPG
     RQRLRSSDPP SRHTHRRTPG GACPATQFPP PMSDSE
//