Database: UniProt
Entry: E9M5M2_9GAMA
LinkDB: E9M5M2_9GAMA
Original site: E9M5M2_9GAMA 
ID   E9M5M2_9GAMA            Unreviewed;        77 AA.
AC   E9M5M2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   07-OCT-2020, entry version 21.
DE   RecName: Full=Cytoplasmic envelopment protein 3 {ECO:0000256|HAMAP-Rule:MF_04042};
GN   ORFNames=RHVP-L.38 {ECO:0000313|EMBL:ADW24462.1}, RHVP.38
GN   {ECO:0000313|EMBL:ADW24380.1};
OS   Cricetid gammaherpesvirus 2.
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=1605972 {ECO:0000313|EMBL:ADW24380.1, ECO:0000313|Proteomes:UP000134313};
RN   [1] {ECO:0000313|EMBL:ADW24380.1, ECO:0000313|Proteomes:UP000134313, ECO:0000313|Proteomes:UP000164320}
RX   PubMed=21209105; DOI=10.1128/JVI.01661-10;
RA   Loh J., Zhao G., Nelson C.A., Coder P., Droit L., Handley S.A.,
RA   Johnson L.S., Vachharajani P., Guzman H., Tesh R.B., Wang D., Fremont D.H.,
RA   Virgin H.W.;
RT   "Identification and sequencing of a novel rodent gammaherpesvirus that
RT   establishes acute and latent infection in laboratory mice.";
RL   J. Virol. 85:2642-2656(2011).
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}.
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DR   EMBL; HQ221963; ADW24380.1; -; Genomic_DNA.
DR   EMBL; HQ698924; ADW24462.1; -; Genomic_DNA.
DR   RefSeq; YP_004207875.1; NC_015049.1.
DR   GeneID; 10192230; -.
DR   KEGG; vg:10192230; -.
DR   Proteomes; UP000134313; Genome.
DR   Proteomes; UP000164320; 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:UP000134313};
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          28..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..65
FT                   /note="Polyampholyte"
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   77 AA;  8441 MW;  C92E90DF73687CAF CRC64;
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