GenomeNet

Database: UniProt
Entry: Q8UZG1_9GAMA
LinkDB: Q8UZG1_9GAMA
Original site: Q8UZG1_9GAMA 
ID   Q8UZG1_9GAMA            Unreviewed;        74 AA.
AC   Q8UZG1;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   02-DEC-2020, entry version 49.
DE   RecName: Full=Cytoplasmic envelopment protein 3 {ECO:0000256|HAMAP-Rule:MF_04042};
OS   Macacine gammaherpesvirus 4 (Rhesus lymphocryptovirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX   NCBI_TaxID=45455 {ECO:0000313|EMBL:AAK95450.1, ECO:0000313|Proteomes:UP000201521};
RN   [1] {ECO:0000313|EMBL:AAK95450.1, ECO:0000313|Proteomes:UP000201521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCL8664 {ECO:0000313|EMBL:AAK95450.1,
RC   ECO:0000313|Proteomes:UP000201521};
RX   PubMed=8892903;
RA   Franken M., Devergne O., Rosenzweig M., Annis B., Kieff E., Wang F.;
RT   "Comparative analysis identifies conserved tumor necrosis factor receptor-
RT   associated factor 3 binding sites in the human and simian Epstein-Barr
RT   virus oncogene LMP1.";
RL   J. Virol. 70:7819-7826(1996).
RN   [2] {ECO:0000313|EMBL:AAK95450.1, ECO:0000313|Proteomes:UP000201521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCL8664 {ECO:0000313|EMBL:AAK95450.1,
RC   ECO:0000313|Proteomes:UP000201521};
RX   PubMed=10482645;
RA   Rivailler P., Quink C., Wang F.;
RT   "Strong selective pressure for evolution of an Epstein-Barr virus LMP2B
RT   homologue in the rhesus lymphocryptovirus.";
RL   J. Virol. 73:8867-8872(1999).
RN   [3] {ECO:0000313|EMBL:AAK95450.1, ECO:0000313|Proteomes:UP000201521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCL8664 {ECO:0000313|EMBL:AAK95450.1,
RC   ECO:0000313|Proteomes:UP000201521};
RX   PubMed=10970361;
RA   Rao P., Jiang H., Wang F.;
RT   "Cloning of the rhesus lymphocryptovirus viral capsid antigen and Epstein-
RT   Barr virus-encoded small RNA homologues and use in diagnosis of acute and
RT   persistent infections.";
RL   J. Clin. Microbiol. 38:3219-3225(2000).
RN   [4] {ECO:0000313|EMBL:AAK95450.1, ECO:0000313|Proteomes:UP000201521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCL8664 {ECO:0000313|EMBL:AAK95450.1,
RC   ECO:0000313|Proteomes:UP000201521};
RX   PubMed=10846073; DOI=10.1128/JVI.74.13.5921-5932.2000;
RA   Jiang H., Cho Y.G., Wang F.;
RT   "Structural, functional, and genetic comparisons of Epstein-Barr virus
RT   nuclear antigen 3A, 3B, and 3C homologues encoded by the rhesus
RT   lymphocryptovirus.";
RL   J. Virol. 74:5921-5932(2000).
RN   [5] {ECO:0000313|EMBL:AAK95450.1, ECO:0000313|Proteomes:UP000201521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCL8664 {ECO:0000313|EMBL:AAK95450.1,
RC   ECO:0000313|Proteomes:UP000201521};
RX   PubMed=11739708; DOI=10.1128/JVI.76.1.421-426.2002;
RA   Rivailler P., Jiang H., Cho Y.G., Quink C., Wang F.;
RT   "Complete nucleotide sequence of the rhesus lymphocryptovirus: genetic
RT   validation for an Epstein-Barr virus animal model.";
RL   J. Virol. 76:421-426(2002).
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:0000256|HAMAP-
CC       Rule:MF_04042}.
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       {ECO:0000256|HAMAP-Rule:MF_04042}.
CC   -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000256|HAMAP-
CC       Rule:MF_04042}. Virion membrane {ECO:0000256|HAMAP-Rule:MF_04042};
CC       Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_04042}. Host cell membrane
CC       {ECO:0000256|HAMAP-Rule:MF_04042}; Lipid-anchor {ECO:0000256|HAMAP-
CC       Rule:MF_04042}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_04042}.
CC       Host Golgi apparatus membrane {ECO:0000256|HAMAP-Rule:MF_04042}; Lipid-
CC       anchor {ECO:0000256|HAMAP-Rule:MF_04042}; Cytoplasmic side
CC       {ECO:0000256|HAMAP-Rule:MF_04042}. 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:0000256|HAMAP-
CC       Rule:MF_04042}.
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:0000256|HAMAP-Rule:MF_04042}.
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:0000256|HAMAP-Rule:MF_04042}.
CC   -!- SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment
CC       protein 3 family. {ECO:0000256|HAMAP-Rule:MF_04042}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY037858; AAK95450.1; -; Genomic_DNA.
DR   RefSeq; YP_067983.1; NC_006146.1.
DR   GeneID; 2949741; -.
DR   KEGG; vg:2949741; -.
DR   Proteomes; UP000201521; 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:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046760; P:viral budding from Golgi membrane; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04042; HSV_CEP3_gammahv; 1.
DR   InterPro; IPR024360; Herpesvirus_UL11_homo.
DR   Pfam; PF10813; DUF2733; 1.
PE   3: Inferred from homology;
KW   Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04042};
KW   Host Golgi apparatus {ECO:0000256|ARBA:ARBA00022812, ECO:0000256|HAMAP-
KW   Rule:MF_04042}; Host membrane {ECO:0000256|HAMAP-Rule:MF_04042};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW   Rule:MF_04042};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_04042};
KW   Myristate {ECO:0000256|ARBA:ARBA00022707, ECO:0000256|HAMAP-Rule:MF_04042};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_04042};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW   Rule:MF_04042}; Reference proteome {ECO:0000313|Proteomes:UP000201521};
KW   Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|HAMAP-Rule:MF_04042};
KW   Virion tegument {ECO:0000256|ARBA:ARBA00022580, ECO:0000256|HAMAP-
KW   Rule:MF_04042}.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04042"
FT   REGION          42..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04042"
SQ   SEQUENCE   74 AA;  8244 MW;  A6FD0A74038D2AD2 CRC64;
     MGALWSLCRR RVNSIANVDG GMINLYEDYE AFSMETAQLM AVEEGRAGGE TNEGLDDDES
     ENDELPFLPN KRSN
//
DBGET integrated database retrieval system