CEP3_EBVB9
ID CEP3_EBVB9 Reviewed; 75 AA.
AC P0CK51; P03216; Q777D3;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 29-SEP-2021, entry version 25.
DE RecName: Full=Cytoplasmic envelopment protein 3 {ECO:0000255|HAMAP-Rule:MF_04042};
GN ORFNames=BBLF1;
OS Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10377;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6087149; DOI=10.1038/310207a0;
RA Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA Tuffnell P.S., Barrell B.G.;
RT "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL Nature 310:207-211(1984).
RN [2]
RP IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX PubMed=15534216; DOI=10.1073/pnas.0407320101;
RA Johannsen E., Luftig M., Chase M.R., Weicksel S., Cahir-McFarland E.,
RA Illanes D., Sarracino D., Kieff E.;
RT "Proteins of purified Epstein-Barr virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16286-16291(2004).
RN [3]
RP FUNCTION, INTERACTION WITH HOST PACS1, SUBCELLULAR LOCATION,
RP MYRISTOYLATION, AND PALMITOYLATION.
RX PubMed=22740416; DOI=10.1128/jvi.01126-12;
RA Chiu Y.F., Sugden B., Chang P.J., Chen L.W., Lin Y.J., Lan Y.C., Lai C.H.,
RA Liou J.Y., Liu S.T., Hung C.H.;
RT "Characterization and intracellular trafficking of Epstein-Barr virus
RT BBLF1, a protein involved in virion maturation.";
RL J. Virol. 86:9647-9655(2012).
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_04042,
CC ECO:0000269|PubMed:22740416}.
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:0000255|HAMAP-Rule:MF_04042}.
CC -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000255|HAMAP-Rule:MF_04042,
CC ECO:0000269|PubMed:15534216}. Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04042}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04042}. Host
CC cell membrane {ECO:0000255|HAMAP-Rule:MF_04042}; Lipid-anchor
CC {ECO:0000255|HAMAP-Rule:MF_04042}; Cytoplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_04042}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-
CC Rule:MF_04042, ECO:0000269|PubMed:22740416}; Lipid-anchor
CC {ECO:0000255|HAMAP-Rule:MF_04042}; Cytoplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_04042}. Note=Virion membrane-associated tegument protein.
CC Associates with host membrane lipids rafts. During virion
CC morphogenesis, this protein probably accumulates in the endosomes and
CC trans-Golgi where secondary envelopment occurs. It is probably
CC transported to the cell surface from where it is endocytosed and
CC directed to the trans-Golgi network (TGN). {ECO:0000255|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:0000255|HAMAP-Rule:MF_04042, ECO:0000269|PubMed:22740416}.
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_04042}.
CC -!- SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment
CC protein 3 family. {ECO:0000255|HAMAP-Rule:MF_04042}.
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DR EMBL; V01555; CAA24826.1; -; Genomic_DNA.
DR EMBL; AJ507799; CAD53436.1; -; Genomic_DNA.
DR PIR; H43043; QQBE36.
DR RefSeq; YP_401686.1; NC_007605.1.
DR IntAct; P0CK51; 1.
DR DNASU; 3783765; -.
DR GeneID; 3783765; -.
DR KEGG; vg:3783765; -.
DR Proteomes; UP000153037; 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: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 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_04042"
FT CHAIN 2..75
FT /note="Cytoplasmic envelopment protein 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04042"
FT /id="PRO_0000115933"
FT REGION 53..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04042"
SQ SEQUENCE 75 AA; 8470 MW; 4F6BAFD23770287A CRC64;
MGALWSLCRR RVNSIGDVDG GIINLYNDYE EFNLETTKLI AAEEGRACGE TNEGLEYDED
SENDELLFLP NKKPN
